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Conserved domains on  [gi|446581728|ref|WP_000659074|]
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MULTISPECIES: non-ribosomal peptide synthetase [Bacillus cereus group]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 13483049)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
 9-2113 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1343.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728    9 EIVEELDVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEF 88
Cdd:PRK12467   45 SAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   89 DIPIKDLTAFKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGE 168
Cdd:PRK12467  125 TIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  169 LLQGK--SNVEFESPYKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQ 246
Cdd:PRK12467  205 YSQGRepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAG 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  247 IQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKS 326
Cdd:PRK12467  285 LKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRT 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  327 IHLAITYKHNSYSHIVKDLNLNTNTNHNMVYSTAFN-----TM-------KIPELKIPDIESTvltdcKRVNPFNMTwrI 394
Cdd:PRK12467  365 ALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNhqntaTGgrdregaQLPGLTVEELSWA-----RHTAQFDLA--L 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  395 MRYEGETENKIEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDHRLYKEMNSNALTYPNLKTLDQL 474
Cdd:PRK12467  438 DTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQL 517

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFP 554
Cdd:PRK12467  518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  555 EKRIEYILKDSESQMIITKKEYRGLVERFA-IHTIYL---EDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVP 630
Cdd:PRK12467  598 QDRLAYMLDDSGVRLLLTQSHLLAQLPVPAgLRSLCLdepADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  631 HKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAF 710
Cdd:PRK12467  678 HGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSH 757

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  711 FKLIADMPKEMLLKlnSVKRLFVGGETLPAESVRKWQsKLGLKIPVLNAYGPTETTVCATMYEVNGEIQkEISNIPIGKP 790
Cdd:PRK12467  758 LQALLQASRVALPR--PQRALVCGGEALQVDLLARVR-ALGPGARLINHYGPTETTVGVSTYELSDEER-DFGNVPIGQP 833

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  791 IANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRK 870
Cdd:PRK12467  834 LANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVP-DPFGADGGRLYRTGDLARYRADGVIEYLGRM 912

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  871 DNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTY--QNDKIVCFYL----SKDNTE--LKQEALKTFLSESLPDFMMPNY 942
Cdd:PRK12467  913 DHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQpgDAGLQLVAYLvpaaVADGAEhqATRDELKAQLRQVLPDYMVPAH 992

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  943 IFHLESFPVSPSGKLDRKKLELQIPSLLenmQKQYVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGHSLIAVQV 1022
Cdd:PRK12467  993 LLLLDSLPLTPNGKLDRKALPKPDASAV---QATFVAPQTELEKRLAAIWADVLKVE--RVGLTDNFFELGGHSLLATQV 1067

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1023 LNQIQKEFHLKIEIRDIFEHTTIASLSAyidklmAVNHDREEQEMQVLKVADKESYQLSSAQKRIWFLNKYNAINRVYDT 1102
Cdd:PRK12467 1068 ISRVRQRLGIQVPLRTLFEHQTLAGFAQ------AVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHI 1141

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1103 PLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDEIEHMSKKEQQeyIRTTINQTDHTP 1182
Cdd:PRK12467 1142 PQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDEAQ--LKVYVEAEARQP 1219

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1183 FDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYAEWEQVQLNLG 1262
Cdd:PRK12467 1220 FDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAG 1299

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1263 RWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQ 1342
Cdd:PRK12467 1300 ERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQ 1379

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1343 KDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVIEQINPDRSFGNNPI 1422
Cdd:PRK12467 1380 DDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPL 1459

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1423 FSTMFSYQKD---ILQQHDAYKLQLLPNKQDISKFDISLAVEEGLDYVGISFEYDINLFKEESINRFTQNLLNILDAFIH 1499
Cdd:PRK12467 1460 FQVMFNHQRDdhqAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVA 1539

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1500 QRTVTYENLSFLSQEE-ESLYKKVNHTERPYPYFQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEK 1578
Cdd:PRK12467 1540 DPERRLGELDLLDEAErRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIAL 1619

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1579 GIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSII---E 1655
Cdd:PRK12467 1620 GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVldqE 1699

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1656 DIYRTTINDDVKILN-KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFS 1734
Cdd:PRK12467 1700 DDWLEGYSDSNPAVNlAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFW 1779

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1735 TLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELSTSLTKLdsEKIRSLRFIIMGGEAASTNAIRSWQNT 1814
Cdd:PRK12467 1780 PLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQV--EHPLSLRRVVCGGEALEVEALRPWLER 1857

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1815 FKNqVQLVNEYGPTEATVSAMYYFI--PVLEGENnllgSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGY 1892
Cdd:PRK12467 1858 LPD-TGLFNLYGPTETAVDVTHWTCrrKDLEGRD----SVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGY 1932

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1893 WKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTE 1972
Cdd:PRK12467 1933 LNRPALTAERFVADPFGTVGS-RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD 2011

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1973 G--GMLLQAYYKTVDGIGIE--------KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFGHEQKDe 2042
Cdd:PRK12467 2012 GanGKQLVAYVVPTDPGLVDddeaqvalRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQA- 2090

                        2090      2100      2110      2120      2130      2140      2150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728 2043 cKLKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKLKPLYPNLKIQDFFKYRTIEKLA 2113
Cdd:PRK12467 2091 -YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLA 2160
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 2162-2432 3.75e-89

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


:

Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 291.73  E-value: 3.75e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQLPSTTIYCLVRENEDQVIGAKLKERMEFYfgKEILQKLKERVELIEGDLSLMNLGLDS 2241
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRRTDARVYCLVRASDEAAARERLEALLERY--GLWLELDASRVVVVAGDLTQPRLGLSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKefeFFESDFDR 2320
Cdd:COG3320    79 AEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLkPFHYVSTIAVAGPADRSGV---FEEDDLDE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 GQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGKFQyniNENAFYRLLKGICLSSIAPDV-NTYVDLTP 2399
Cdd:COG3320   156 GQGFANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETN---KDDGFYRLLKGLLRLGAAPGLgDARLNLVP 232

                         250       260       270
                  ....*....|....*....|....*....|...
gi 446581728 2400 VDYGSLAITELSYKANTVNKTMHICNPNQLKWD 2432
Cdd:COG3320   233 VDYVARAIVHLSRQPEAAGRTFHLTNPQPLSLG 265
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 9-2113 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1343.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728    9 EIVEELDVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEF 88
Cdd:PRK12467   45 SAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   89 DIPIKDLTAFKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGE 168
Cdd:PRK12467  125 TIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  169 LLQGK--SNVEFESPYKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQ 246
Cdd:PRK12467  205 YSQGRepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAG 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  247 IQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKS 326
Cdd:PRK12467  285 LKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRT 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  327 IHLAITYKHNSYSHIVKDLNLNTNTNHNMVYSTAFN-----TM-------KIPELKIPDIESTvltdcKRVNPFNMTwrI 394
Cdd:PRK12467  365 ALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNhqntaTGgrdregaQLPGLTVEELSWA-----RHTAQFDLA--L 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  395 MRYEGETENKIEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDHRLYKEMNSNALTYPNLKTLDQL 474
Cdd:PRK12467  438 DTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQL 517

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFP 554
Cdd:PRK12467  518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  555 EKRIEYILKDSESQMIITKKEYRGLVERFA-IHTIYL---EDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVP 630
Cdd:PRK12467  598 QDRLAYMLDDSGVRLLLTQSHLLAQLPVPAgLRSLCLdepADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  631 HKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAF 710
Cdd:PRK12467  678 HGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSH 757

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  711 FKLIADMPKEMLLKlnSVKRLFVGGETLPAESVRKWQsKLGLKIPVLNAYGPTETTVCATMYEVNGEIQkEISNIPIGKP 790
Cdd:PRK12467  758 LQALLQASRVALPR--PQRALVCGGEALQVDLLARVR-ALGPGARLINHYGPTETTVGVSTYELSDEER-DFGNVPIGQP 833

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  791 IANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRK 870
Cdd:PRK12467  834 LANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVP-DPFGADGGRLYRTGDLARYRADGVIEYLGRM 912

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  871 DNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTY--QNDKIVCFYL----SKDNTE--LKQEALKTFLSESLPDFMMPNY 942
Cdd:PRK12467  913 DHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQpgDAGLQLVAYLvpaaVADGAEhqATRDELKAQLRQVLPDYMVPAH 992

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  943 IFHLESFPVSPSGKLDRKKLELQIPSLLenmQKQYVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGHSLIAVQV 1022
Cdd:PRK12467  993 LLLLDSLPLTPNGKLDRKALPKPDASAV---QATFVAPQTELEKRLAAIWADVLKVE--RVGLTDNFFELGGHSLLATQV 1067

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1023 LNQIQKEFHLKIEIRDIFEHTTIASLSAyidklmAVNHDREEQEMQVLKVADKESYQLSSAQKRIWFLNKYNAINRVYDT 1102
Cdd:PRK12467 1068 ISRVRQRLGIQVPLRTLFEHQTLAGFAQ------AVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHI 1141

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1103 PLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDEIEHMSKKEQQeyIRTTINQTDHTP 1182
Cdd:PRK12467 1142 PQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDEAQ--LKVYVEAEARQP 1219

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1183 FDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYAEWEQVQLNLG 1262
Cdd:PRK12467 1220 FDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAG 1299

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1263 RWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQ 1342
Cdd:PRK12467 1300 ERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQ 1379

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1343 KDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVIEQINPDRSFGNNPI 1422
Cdd:PRK12467 1380 DDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPL 1459

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1423 FSTMFSYQKD---ILQQHDAYKLQLLPNKQDISKFDISLAVEEGLDYVGISFEYDINLFKEESINRFTQNLLNILDAFIH 1499
Cdd:PRK12467 1460 FQVMFNHQRDdhqAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVA 1539

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1500 QRTVTYENLSFLSQEE-ESLYKKVNHTERPYPYFQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEK 1578
Cdd:PRK12467 1540 DPERRLGELDLLDEAErRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIAL 1619

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1579 GIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSII---E 1655
Cdd:PRK12467 1620 GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVldqE 1699

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1656 DIYRTTINDDVKILN-KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFS 1734
Cdd:PRK12467 1700 DDWLEGYSDSNPAVNlAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFW 1779

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1735 TLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELSTSLTKLdsEKIRSLRFIIMGGEAASTNAIRSWQNT 1814
Cdd:PRK12467 1780 PLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQV--EHPLSLRRVVCGGEALEVEALRPWLER 1857

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1815 FKNqVQLVNEYGPTEATVSAMYYFI--PVLEGENnllgSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGY 1892
Cdd:PRK12467 1858 LPD-TGLFNLYGPTETAVDVTHWTCrrKDLEGRD----SVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGY 1932

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1893 WKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTE 1972
Cdd:PRK12467 1933 LNRPALTAERFVADPFGTVGS-RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD 2011

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1973 G--GMLLQAYYKTVDGIGIE--------KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFGHEQKDe 2042
Cdd:PRK12467 2012 GanGKQLVAYVVPTDPGLVDddeaqvalRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQA- 2090

                        2090      2100      2110      2120      2130      2140      2150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728 2043 cKLKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKLKPLYPNLKIQDFFKYRTIEKLA 2113
Cdd:PRK12467 2091 -YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLA 2160
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1079-2082 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 847.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1079 QLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDE 1158
Cdd:COG1020    19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1159 IEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRN 1238
Cdd:COG1020    99 LLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1239 PELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCE 1318
Cdd:COG1020   179 LPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALAR 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1319 QENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQ 1398
Cdd:COG1020   259 RHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYA 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1399 NQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDILQQHDAYKLQL--LPNKQDISKFDISLAVEEGLDYVGISFEYDIN 1476
Cdd:COG1020   339 HQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLepLELDSGTAKFDLTLTVVETGDGLRLTLEYNTD 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1477 LFKEESINRFTQNLLNILDAFIHQRTVTYENLSFLSQEE-ESLYKKVNHTERPYPYFQNIQEQFYMQVDRQPERIAIATA 1555
Cdd:COG1020   419 LFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAErQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFG 498

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1556 TESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRII 1635
Cdd:COG1020   499 DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVL 578

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1636 TSNKFKSHLNVSDYKVSIIEDIYRTTIN-DDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPN 1714
Cdd:COG1020   579 TQSALAARLPELGVPVLALDALALAAEPaTNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPG 658

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1715 DKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELSTSLTkldsEKIRSLR 1794
Cdd:COG1020   659 DRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP----EALPSLR 734

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1795 FIIMGGEAASTNAIRSWQNTFKnQVQLVNEYGPTEATVSAMYYfipVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCP 1874
Cdd:COG1020   735 LVLVGGEALPPELVRRWRARLP-GARLVNLYGPTETTVDSTYY---EVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVP 810

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1875 VGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIE 1954
Cdd:COG1020   811 VGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGA-RLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIE 889

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1955 DAMLQLEGISQAVVTQTE---GGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLP 2031
Cdd:COG1020   890 AALLQHPGVREAVVVAREdapGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969

                         970       980       990      1000      1010
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446581728 2032 KIEFGHEQKDEcklKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSL 2082
Cdd:COG1020   970 APAAAAAAAAA---APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGL 1017
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1547-2026 2.57e-174

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 542.50  E-value: 2.57e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSnkfkshlnvsdykvsiiediyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRN 1706
Cdd:cd05930    81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELstsLTKLD 1786
Cdd:cd05930   127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLL---LQELE 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1787 SEKIRSLRFIIMGGEAASTNAIRSWQNTFkNQVQLVNEYGPTEATVSAMYYfipVLEGENNLLGSVPIGIPISNTKVHIL 1866
Cdd:cd05930   204 LAALPSLRLVLVGGEALPPDLVRRWRELL-PGARLVNLYGPTEATVDATYY---RVPPDDEEDGRVPIGRPIPNTRVYVL 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1867 NSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEdnSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGH 1946
Cdd:cd05930   280 DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP--GERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGY 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1947 RIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANG 2023
Cdd:cd05930   358 RIELGEIEAALLAHPGVREAAVVareDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437


                  ...
gi 446581728 2024 KID 2026
Cdd:cd05930   438 KVD 440
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1560-1968 2.99e-143

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 453.26  E-value: 2.99e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1560 TYRQLNMSSNQVAQHLL-EKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSN 1638
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1639 KFKSHLNVSDYKVSIIEDIYRTTINDD-----VKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISP 1713
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDApapppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1714 NDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVE-YAQAIQETQATISDLPTVFFNelstSLTKLDSEKIRS 1792
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAAlLAALIAEHPVTVLNLTPSLLA----LLAAALPPALAS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1793 LRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYfiPVLEGENNLLGSVPIGIPISNTKVHILNSYMQY 1872
Cdd:TIGR01733  237 LRLVILGGEALTPALVDRWRARGPG-ARLINLYGPTETTVWSTAT--LVDPDDAPRESPVPIGRPLANTRLYVLDDDLRP 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1873 CPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGE 1952
Cdd:TIGR01733  314 VPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393

                          410
                   ....*....|....*.
gi 446581728  1953 IEDAMLQLEGISQAVV 1968
Cdd:TIGR01733  394 IEAALLRHPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1078-1515 5.80e-102

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 336.23  E-value: 5.80e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1078 YQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFI-ERNGEPRQVILNSIAIDLIH 1156
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFELEI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1157 DEIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKR 1236
Cdd:pfam00668   85 IDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1237 RNPELPTISNrYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQV 1316
Cdd:pfam00668  165 EPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1317 CEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNS 1396
Cdd:pfam00668  244 AKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSA 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1397 FQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDILQQH-------DAYKLQLLPNKQDISKFDISLAVEEGLDYVGI 1469
Cdd:pfam00668  324 EPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSqeeefqlSELDLSVSSVIEEEAKYDLSLTASERGGGLTI 403

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 446581728  1470 SFEYDINLFKEESINRFTQNLLNILDAFIHQRTVTYENLSFLSQEE 1515
Cdd:pfam00668  404 KIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE 449
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 2162-2432 3.75e-89

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 291.73  E-value: 3.75e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQLPSTTIYCLVRENEDQVIGAKLKERMEFYfgKEILQKLKERVELIEGDLSLMNLGLDS 2241
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRRTDARVYCLVRASDEAAARERLEALLERY--GLWLELDASRVVVVAGDLTQPRLGLSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKefeFFESDFDR 2320
Cdd:COG3320    79 AEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLkPFHYVSTIAVAGPADRSGV---FEEDDLDE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 GQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGKFQyniNENAFYRLLKGICLSSIAPDV-NTYVDLTP 2399
Cdd:COG3320   156 GQGFANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETN---KDDGFYRLLKGLLRLGAAPGLgDARLNLVP 232

                         250       260       270
                  ....*....|....*....|....*....|...
gi 446581728 2400 VDYGSLAITELSYKANTVNKTMHICNPNQLKWD 2432
Cdd:COG3320   233 VDYVARAIVHLSRQPEAAGRTFHLTNPQPLSLG 265
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
 2163-2455 7.95e-74

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 248.72  E-value: 7.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLP-STTIYCLVRENEDQVIGAKLKERMEFYFGKEILQKLKERVELIEGDLSLMNLGLDS 2241
Cdd:cd05235     1 TVLLTGATGFLGAYLLRELLKRKnVSKIYCLVRAKDEEAALERLIDNLKEYGLNLWDELELSRIKVVVGDLSKPNLGLSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKEFEFFESDFDR 2320
Cdd:cd05235    81 DDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLkPLHFVSTLSVFSAEEYNALDDEESDDMLES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 GQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGkfqYNINENAFYRLLKGICLSSIAPDVNTYVDLTPV 2400
Cdd:cd05235   161 QNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETG---IGNTDDFFWRLLKGCLQLGIYPISGAPLDLSPV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 2401 DYGSLAITELSYKANTVNKTMHICNPNQLKWDQFINSLQAFGYDillMKQEKYIE 2455
Cdd:cd05235   238 DWVARAIVKLALNESNEFSIYHLLNPPLISLNDLLDALEEKGYS---IKEVSYEE 289
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
 2163-2451 8.76e-54

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 193.79  E-value: 8.76e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2163 TVFLTGATGYLGAHILERLL-QLPSTTIYCLVRENEDQVIGAKLKERMEFYFGKEiLQKLKERVELIEGDLSLMNLGLDS 2241
Cdd:TIGR01746    1 TVLLTGATGFLGAYLLEELLrRSTRAKVICLVRADSEEHAMERLREALRSYRLWH-ENLAMERIEVVAGDLSKPRLGLSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2242 KQLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSvVGQAERDPKEFEFFESDFDR 2320
Cdd:TIGR01746   80 AEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKpLHYVSTIS-VGAAIDLSTGVTEDDATVTP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2321 GQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGKFQYNineNAFYRLLKGiCLS-SIAPDVN-TYVDLT 2398
Cdd:TIGR01746  159 YPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSS---DILWRMVKG-CLAlGAYPQSPeLTEDLT 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728  2399 PVDYGSLAITELS--YKANTVNKTMHICNPNQLKWDQFINSLQAFGYDILLMKQE 2451
Cdd:TIGR01746  235 PVDFVARAIVALSsrPAASAGGIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFD 289
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 2166-2407 1.31e-51

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 183.58  E-value: 1.31e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2166 LTGATGYLGAHILERLLQLPS--TTIYCLVRENEDQVIGAKLKERMEFYF-GKEILQKLKERVELIEGDLSLMNLGLDSK 2242
Cdd:pfam07993    1 LTGATGFLGKVLLEKLLRSTPdvKKIYLLVRAKDGESALERLRQELEKYPlFDALLKEALERIVPVAGDLSEPNLGLSEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2243 QLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNT--NVRFHYISTlSVVGQAERDPKEFEFFES---- 2316
Cdd:pfam07993   81 DFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGkqLKPFHHVST-AYVNGERGGLVEEKPYPEgedd 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2317 ------DFDRGQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGKFQyniNENAFYRLLKGIC----LSS 2386
Cdd:pfam07993  160 mlldedEPALLGGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWIN---NFDFGPRGLLGGIgkgvLPS 236

                          250       260
                   ....*....|....*....|.
gi 446581728  2387 IAPDVNTYVDLTPVDYGSLAI 2407
Cdd:pfam07993  237 ILGDPDAVLDLVPVDYVANAI 257
PRK07201 PRK07201
SDR family oxidoreductase;
2163-2426 8.97e-31

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 131.61  E-value: 8.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQL-PSTTIYCLVRENEDqvigAKLkERMEFYFGKEilqklkeRVELIEGDLSLMNLGLDS 2241
Cdd:PRK07201    2 RYFVTGGTGFIGRRLVSRLLDRrREATVHVLVRRQSL----SRL-EALAAYWGAD-------RVVPLVGDLTEPGLGLSE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHLKKnVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSVVGQAERdpkefEFFESDFDR 2320
Cdd:PRK07201   70 ADIAELGD-IDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAAtFHHVSSIAVAGDYEG-----VFREDDFDE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 GQNLDNLYLESKFQGEKMVREamEKGVRATIYRVGNLVGNSKTGKFQ------YninenaFYRLLKGIC-----LSSIAP 2389
Cdd:PRK07201  144 GQGLPTPYHRTKFEAEKLVRE--ECGLPWRVYRPAVVVGDSRTGEMDkidgpyY------FFKVLAKLAklpswLPMVGP 215

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 446581728 2390 DVNtYVDLTPVDYGSLAITELSYKANTVNKTMHICNP 2426
Cdd:PRK07201  216 DGG-RTNIVPVDYVADALDHLMHKDGRDGQTFHLTDP 251
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1003-1052 1.64e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 51.10  E-value: 1.64e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 446581728   1003 IGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIASLSAYI 1052
Cdd:smart00823   33 IDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 9-2113 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1343.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728    9 EIVEELDVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEF 88
Cdd:PRK12467   45 SAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   89 DIPIKDLTAFKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGE 168
Cdd:PRK12467  125 TIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  169 LLQGK--SNVEFESPYKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQ 246
Cdd:PRK12467  205 YSQGRepSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAG 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  247 IQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKS 326
Cdd:PRK12467  285 LKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRT 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  327 IHLAITYKHNSYSHIVKDLNLNTNTNHNMVYSTAFN-----TM-------KIPELKIPDIESTvltdcKRVNPFNMTwrI 394
Cdd:PRK12467  365 ALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNhqntaTGgrdregaQLPGLTVEELSWA-----RHTAQFDLA--L 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  395 MRYEGETENKIEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDHRLYKEMNSNALTYPNLKTLDQL 474
Cdd:PRK12467  438 DTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQL 517

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFP 554
Cdd:PRK12467  518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  555 EKRIEYILKDSESQMIITKKEYRGLVERFA-IHTIYL---EDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVP 630
Cdd:PRK12467  598 QDRLAYMLDDSGVRLLLTQSHLLAQLPVPAgLRSLCLdepADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  631 HKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAF 710
Cdd:PRK12467  678 HGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSH 757

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  711 FKLIADMPKEMLLKlnSVKRLFVGGETLPAESVRKWQsKLGLKIPVLNAYGPTETTVCATMYEVNGEIQkEISNIPIGKP 790
Cdd:PRK12467  758 LQALLQASRVALPR--PQRALVCGGEALQVDLLARVR-ALGPGARLINHYGPTETTVGVSTYELSDEER-DFGNVPIGQP 833

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  791 IANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRK 870
Cdd:PRK12467  834 LANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVP-DPFGADGGRLYRTGDLARYRADGVIEYLGRM 912

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  871 DNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTY--QNDKIVCFYL----SKDNTE--LKQEALKTFLSESLPDFMMPNY 942
Cdd:PRK12467  913 DHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQpgDAGLQLVAYLvpaaVADGAEhqATRDELKAQLRQVLPDYMVPAH 992

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  943 IFHLESFPVSPSGKLDRKKLELQIPSLLenmQKQYVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGHSLIAVQV 1022
Cdd:PRK12467  993 LLLLDSLPLTPNGKLDRKALPKPDASAV---QATFVAPQTELEKRLAAIWADVLKVE--RVGLTDNFFELGGHSLLATQV 1067

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1023 LNQIQKEFHLKIEIRDIFEHTTIASLSAyidklmAVNHDREEQEMQVLKVADKESYQLSSAQKRIWFLNKYNAINRVYDT 1102
Cdd:PRK12467 1068 ISRVRQRLGIQVPLRTLFEHQTLAGFAQ------AVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHI 1141

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1103 PLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDEIEHMSKKEQQeyIRTTINQTDHTP 1182
Cdd:PRK12467 1142 PQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDEAQ--LKVYVEAEARQP 1219

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1183 FDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYAEWEQVQLNLG 1262
Cdd:PRK12467 1220 FDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAG 1299

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1263 RWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQ 1342
Cdd:PRK12467 1300 ERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQ 1379

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1343 KDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVIEQINPDRSFGNNPI 1422
Cdd:PRK12467 1380 DDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPL 1459

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1423 FSTMFSYQKD---ILQQHDAYKLQLLPNKQDISKFDISLAVEEGLDYVGISFEYDINLFKEESINRFTQNLLNILDAFIH 1499
Cdd:PRK12467 1460 FQVMFNHQRDdhqAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVA 1539

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1500 QRTVTYENLSFLSQEE-ESLYKKVNHTERPYPYFQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEK 1578
Cdd:PRK12467 1540 DPERRLGELDLLDEAErRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIAL 1619

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1579 GIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSII---E 1655
Cdd:PRK12467 1620 GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVldqE 1699

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1656 DIYRTTINDDVKILN-KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFS 1734
Cdd:PRK12467 1700 DDWLEGYSDSNPAVNlAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFW 1779

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1735 TLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELSTSLTKLdsEKIRSLRFIIMGGEAASTNAIRSWQNT 1814
Cdd:PRK12467 1780 PLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQV--EHPLSLRRVVCGGEALEVEALRPWLER 1857

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1815 FKNqVQLVNEYGPTEATVSAMYYFI--PVLEGENnllgSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGY 1892
Cdd:PRK12467 1858 LPD-TGLFNLYGPTETAVDVTHWTCrrKDLEGRD----SVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGY 1932

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1893 WKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTE 1972
Cdd:PRK12467 1933 LNRPALTAERFVADPFGTVGS-RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD 2011

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1973 G--GMLLQAYYKTVDGIGIE--------KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFGHEQKDe 2042
Cdd:PRK12467 2012 GanGKQLVAYVVPTDPGLVDddeaqvalRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQA- 2090

                        2090      2100      2110      2120      2130      2140      2150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728 2043 cKLKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKLKPLYPNLKIQDFFKYRTIEKLA 2113
Cdd:PRK12467 2091 -YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLA 2160
PRK12316 PRK12316
peptide synthase; Provisional
 19-2114 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1066.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   19 GQEALWIAHQMEIEIGmnnepiiiklkgNLQIEVLKKALTTIVQSHPALRTIFKKRD--EKIKQLIQKNVEfdIPIKDLT 96
Cdd:PRK12316 1573 EQEAGDYINQLRVDVQ------------GLDPDRFRAAWQATVDRHEILRSGFLWQDglEQPLQVIHKQVE--LPFAELD 1638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   97 AFKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFilHLMF--HHIIYDGWSLgvfirqlSNTYGELLQGKS 174
Cdd:PRK12316 1639 WRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRH--HLIYtnHHILMDGWSN-------AQLLGEVLQRYA 1709

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  175 NVEFESP---YKNLVkheeSFIDSAIYKEGSSYWKDYLQGELTPTEFpidfnkMNEKRYTDKNIS-----KNINSDLFYQ 246
Cdd:PRK12316 1710 GQPVAAPggrYRDYI----AWLQRQDAAASEAFWKEQLAALEEPTRL------AQAARTEDGQVGygdhqQLLDPAQTRA 1779

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  247 IQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPY----TEERntFGYFVNTLPIRITIEKGETFKGILNK 322
Cdd:PRK12316 1780 LAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelpgIEQQ--IGLFINTLPVIAAPRPDQSVADWLQE 1857

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  323 VnKSIHLAI-TYKHNSYSHIVKDLNLNTntnhnmvySTAFNTMKIPElKIPDIESTvltdcKRVNPFNMTW-RIMRYE-- 398
Cdd:PRK12316 1858 V-QALNLALrEHEHTPLYDIQRWAGQGG--------EALFDSLLVFE-NYPVAEAL-----KQGAPAGLVFgRVSNHEqt 1922

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  399 ----------GETEnKIEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDHRLYKEMNSNALT-YPN 467
Cdd:PRK12316 1923 nypltlavtlGETL-SLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEaYPR 2001

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  468 LKTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYV 547
Cdd:PRK12316 2002 GPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYV 2081

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  548 PIDPKFPEKRIEYILKDSESQMIITKkeyRGLVERFAIHT-IYLEDFHYANSIENIASTHTI-----EDAAYIIYTSGST 621
Cdd:PRK12316 2082 PLDPNYPAERLAYMLEDSGAALLLTQ---RHLLERLPLPAgVARLPLDRDAEWADYPDTAPAvqlagENLAYVIYTSGST 2158

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  622 GLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMhLISEIEKRSAEEFINVSQKYGI 701
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGV 2237

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  702 TNVVLPTAFFKLIADMpKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEIQKE 781
Cdd:PRK12316 2238 TILDFPPVYLQQLAEH-AERDGRPPAVRVYCFGGEAVPAASLRLAWEALR-PVYLFNGYGPTEAVVTPLLWKCRPQDPCG 2315

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  782 ISNIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLAN 861
Cdd:PRK12316 2316 AAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVP-DPFSASGERLYRTGDLARYRAD 2394

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  862 GNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN---DKIVCFYLSKDNTELKQEALKTFLSESLPDFM 938
Cdd:PRK12316 2395 GVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGasgKQLVAYVVPDDAAEDLLAELRAWLAARLPAYM 2474

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  939 MPNYIFHLESFPVSPSGKLDRKKLELQIPSLLenmQKQYVPPISETEKRLAKTWAEILNLgkYRIGRDDDFFKLGGHSLI 1018
Cdd:PRK12316 2475 VPAHWVVLERLPLNPNGKLDRKALPKPDVSQL---RQAYVAPQEGLEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLL 2549

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1019 AVQVLNQIQKEFHLKIEIRDIFEHTTIASLSAyidklmAVNHDREEQEMQVLKVADKESYQLSSAQKRIWFLNKYNAINR 1098
Cdd:PRK12316 2550 ATQVVSRVRQDLGLEVPLRILFERPTLAAFAA------SLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESA 2623

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1099 VYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDEIEHMSkkeqQEYIRTTINQT 1178
Cdd:PRK12316 2624 AYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVA----DAAIRQRVAEE 2699

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1179 DHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYAEWEQVQ 1258
Cdd:PRK12316 2700 IQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAW 2779

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1259 LNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQENISMYMLFLAAYIQLLHY 1338
Cdd:PRK12316 2780 MDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHR 2859

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1339 LTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVIEQINPDRSFG 1418
Cdd:PRK12316 2860 YSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLS 2939

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1419 NNPIFSTMFSYQKDILQ--QHDAYKLQLLPNKQDISKFDISLAVEEGLDYVGISFEYDINLFKEESINRFTQNLLNILDA 1496
Cdd:PRK12316 2940 HSPLFQVMYNHQSGERAaaQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRG 3019

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1497 FIHQRTVTYENLSFLSQEE-ESLYKKVNHTERPYPYFQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHL 1575
Cdd:PRK12316 3020 MVENPQRSVDELAMLDAEErGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRL 3099

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1576 LEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITsnkfKSHL---NVSDYKVS 1652
Cdd:PRK12316 3100 IERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS----QSHLrlpLAQGVQVL 3175

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1653 IIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEI 1732
Cdd:PRK12316 3176 DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEEL 3255

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1733 FSTLLNGAELyLLSDEQRYSTVEYAQAIQETQATisDLPTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQ 1812
Cdd:PRK12316 3256 FWPLMSGARV-VLAGPEDWRDPALLVELINSEGV--DVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVF 3332

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1813 ntfkNQVQLVNEYGPTEATVSAMyyfipVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGY 1892
Cdd:PRK12316 3333 ----AGLPLYNLYGPTEATITVT-----HWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGY 3403

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1893 WKQKEKTKQAFISNPFSEdnSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTE 1972
Cdd:PRK12316 3404 HNRPGLTAERFVPDPFVP--GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD 3481

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1973 GGMLLqAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFGHEQKDEckLKPQTKVQ 2052
Cdd:PRK12316 3482 GRQLV-AYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDY--VAPVNELE 3558

                        2090      2100      2110      2120      2130      2140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728 2053 KDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKLKPLYPNLKIQDFFKYRTIEKLAS 2114
Cdd:PRK12316 3559 RRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLAR 3620
PRK05691 PRK05691
peptide synthase; Validated
 12-2114 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1055.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   12 EELDVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIP 91
Cdd:PRK05691  674 QALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQ 753

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   92 IKDLTAFKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQ 171
Cdd:PRK05691  754 RIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQ 833

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  172 GKSNVEFESP--YKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQC 249
Cdd:PRK05691  834 GQTAELAPLPlgYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRG 913

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  250 FAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHL 329
Cdd:PRK05691  914 LAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLG 993

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  330 AITYKHNSYSHIVKdlnLNTNTNHNMVYSTAFNTMK--IPELK-IPDIESTVLTDCKRVNPFNMTwriMRYEGETENKIE 406
Cdd:PRK05691  994 AQAHQDLPFEQLVE---ALPQAREQGLFQVMFNHQQrdLSALRrLPGLLAEELPWHSREAKFDLQ---LHSEEDRNGRLT 1067

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  407 V--DYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDHRLYKEMNSNALTyPNLKTLDQLIDLQALKSPN 484
Cdd:PRK05691 1068 LsfDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCA-PAQAWLPELLNEQARQTPE 1146

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  485 QIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKD 564
Cdd:PRK05691 1147 RIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLAD 1226

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  565 SESQMIITKkeyRGLVERF----AIHTIYLEDFHYANSIENIASTHTIED-AAYIIYTSGSTGLPKGVVVPHKGVVNLSY 639
Cdd:PRK05691 1227 SGVELLLTQ---SHLLERLpqaeGVSAIALDSLHLDSWPSQAPGLHLHGDnLAYVIYTSGSTGQPKGVGNTHAALAERLQ 1303

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  640 SVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPk 719
Cdd:PRK05691 1304 WMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP- 1382

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  720 eMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEiqkEISNIPIGKPIANSEVFVI 799
Cdd:PRK05691 1383 -LAAACTSLRRLFSGGEALPAELRNRVLQRLP-QVQLHNRYGPTETAINVTHWQCQAE---DGERSPIGRPLGNVLCRVL 1457

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  800 SPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGY 879
Cdd:PRK05691 1458 DAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP-DPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGF 1536

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  880 RIELDEIEGTLFKHPEVRDAVVF---TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGK 956
Cdd:PRK05691 1537 RVEPEEIQARLLAQPGVAQAAVLvreGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGK 1616

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  957 LDRKKLELqiPSLLenmQKQYVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEI 1036
Cdd:PRK05691 1617 LDRRALPE--PVWQ---QREHVEPRTELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLLATQIVSRTRQACDVELPL 1689

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1037 RDIFEHTTIASLSAYIDKLMAVNhdREEQEMQVLKVADKESYQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDI 1116
Cdd:PRK05691 1690 RALFEASELGAFAEQVARIQAAG--ERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDR 1767

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1117 LQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDEIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIF 1196
Cdd:PRK05691 1768 FEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLV 1847

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1197 NLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELA 1276
Cdd:PRK05691 1848 KAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLG 1927

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1277 APLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNH 1356
Cdd:PRK05691 1928 NEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIR 2007

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1357 QEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDILQQ 1436
Cdd:PRK05691 2008 PESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQ 2087

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1437 HD---AYKLQLLPNKQDISKFDISLAVEEgLDY-VGISFEYDINLFKEESINRFTQNLLNILDAFIHQRTVTYENLSFLS 1512
Cdd:PRK05691 2088 SRqlaGMTVEYLVNDARATKFDLNLEVTD-LDGrLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLA 2166

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1513 QEEES-LYKKVNHTERPYPYFQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLD 1591
Cdd:PRK05691 2167 AAEQQqLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALE 2246

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1592 RSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIItsnkfkSHLNVSDYKVSIIEDIYRTTINDDVKIL-- 1669
Cdd:PRK05691 2247 RSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL------SDRALFEALGELPAGVARWCLEDDAAALaa 2320

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1670 ---------NKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGA 1740
Cdd:PRK05691 2321 ysdaplpflSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGA 2400

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1741 ELYLLSDEQrYSTVEYAQAIQETQATISDLPTVFFNELSTSLTKLDseKIRSLRFIIMGGEAASTNAIRSWQNTFKNQvQ 1820
Cdd:PRK05691 2401 RVVLRAQGQ-WGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQG--EQLPVRMCITGGEALTGEHLQRIRQAFAPQ-L 2476

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1821 LVNEYGPTEATVSAMYYFIP--VLEGEnnllGSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEK 1898
Cdd:PRK05691 2477 FFNAYGPTETVVMPLACLAPeqLEEGA----ASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGL 2552

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1899 TKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV--TQTEGGML 1976
Cdd:PRK05691 2553 TAERFVADPFAADGG-RLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVlaLDTPSGKQ 2631

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1977 LQAYYKT-VDGIGIE-----KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFghEQKDECKLKPQTK 2050
Cdd:PRK05691 2632 LAGYLVSaVAGQDDEaqaalREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDP--ELNRQAYQAPRSE 2709

                        2090      2100      2110      2120      2130      2140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581728 2051 VQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKLKPLYPNLKIQDFFKYRTIEKLAS 2114
Cdd:PRK05691 2710 LEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAA 2773
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1079-2082 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 847.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1079 QLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDE 1158
Cdd:COG1020    19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1159 IEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRN 1238
Cdd:COG1020    99 LLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1239 PELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCE 1318
Cdd:COG1020   179 LPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALAR 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1319 QENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQ 1398
Cdd:COG1020   259 RHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYA 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1399 NQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDILQQHDAYKLQL--LPNKQDISKFDISLAVEEGLDYVGISFEYDIN 1476
Cdd:COG1020   339 HQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLepLELDSGTAKFDLTLTVVETGDGLRLTLEYNTD 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1477 LFKEESINRFTQNLLNILDAFIHQRTVTYENLSFLSQEE-ESLYKKVNHTERPYPYFQNIQEQFYMQVDRQPERIAIATA 1555
Cdd:COG1020   419 LFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAErQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFG 498

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1556 TESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRII 1635
Cdd:COG1020   499 DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVL 578

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1636 TSNKFKSHLNVSDYKVSIIEDIYRTTIN-DDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPN 1714
Cdd:COG1020   579 TQSALAARLPELGVPVLALDALALAAEPaTNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPG 658

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1715 DKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELSTSLTkldsEKIRSLR 1794
Cdd:COG1020   659 DRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP----EALPSLR 734

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1795 FIIMGGEAASTNAIRSWQNTFKnQVQLVNEYGPTEATVSAMYYfipVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCP 1874
Cdd:COG1020   735 LVLVGGEALPPELVRRWRARLP-GARLVNLYGPTETTVDSTYY---EVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVP 810

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1875 VGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIE 1954
Cdd:COG1020   811 VGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGA-RLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIE 889

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1955 DAMLQLEGISQAVVTQTE---GGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLP 2031
Cdd:COG1020   890 AALLQHPGVREAVVVAREdapGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969

                         970       980       990      1000      1010
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446581728 2032 KIEFGHEQKDEcklKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSL 2082
Cdd:COG1020   970 APAAAAAAAAA---APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGL 1017
PRK05691 PRK05691
peptide synthase; Validated
 470-2082 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 727.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  470 TLDQLIDLQALKSPNQIAISM----GDQS--ITYYELQQRSNQIVNYLRENdLKKGQRVSITMEREIDTIVWILGILKSG 543
Cdd:PRK05691   10 TLVQALQRRAAQTPDRLALRFladdPGEGvvLSYRDLDLRARTIAAALQAR-ASFGDRAVLLFPSGPDYVAAFFGCLYAG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  544 GVYVPIDPkfPE-------KRIEYILKDSESQMIITKKEYRG-------LVERFAIHTIYLEDFHYANSIENIASTHTIE 609
Cdd:PRK05691   89 VIAVPAYP--PEsarrhhqERLLSIIADAEPRLLLTVADLRDsllqmeeLAAANAPELLCVDTLDPALAEAWQEPALQPD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTF--HLGKEDVFLQFATIIFDASIM-----EIF---PILLCGGRMH 679
Cdd:PRK05691  167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGLIggllqPIFsgvPCVLMSPAYF 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  680 LISEIEKRSAeefinVSQkYGITNVVLPTAFFKLIADMPKEMLLK---LNSVKRLFVGGETLPAESVRKWQSKL---GLK 753
Cdd:PRK05691  247 LERPLRWLEA-----ISE-YGGTISGGPDFAYRLCSERVSESALErldLSRWRVAYSGSEPIRQDSLERFAEKFaacGFD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  754 I-PVLNAYGPTEttvcATMYEVNGEIQKEISNIPI---------------------GKPIANSEVFVISPFN-TLCPSGV 810
Cdd:PRK05691  321 PdSFFASYGLAE----ATLFVSGGRRGQGIPALELdaealarnraepgtgsvlmscGRSQPGHAVLIVDPQSlEVLGDNR 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  811 VGELFIGGDGVANGYLNQKEKTEGAFISLD-KSYNRdkkmycTGDLvRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGT 889
Cdd:PRK05691  397 VGEIWASGPSIAHGYWRNPEASAKTFVEHDgRTWLR------TGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKT 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  890 LFKHPEVrdavvftYQNDKIVCFYLSKDNTE---------------LKQEALKTFLSESLPDFM--MPNYIFHLE--SFP 950
Cdd:PRK05691  470 VEREVEV-------VRKGRVAAFAVNHQGEEgigiaaeisrsvqkiLPPQALIKSIRQAVAEACqeAPSVVLLLNpgALP 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  951 VSPSGKLDRKKLELQI-----------PSLLENMQKQYVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGHSLIA 1019
Cdd:PRK05691  543 KTSSGKLQRSACRLRLadgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVE--QVAADDHFFLLGGNSIAA 620

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1020 VQVLNQIQKEFHLKIEIRDIFEHTTIASLSAYIDKLMAvnhDREEQEMQVLKVADKESYQLSSAQKRIWFLNKYNAINRV 1099
Cdd:PRK05691  621 TQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLA---GGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAA 697

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1100 YDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDEIEHMSKKEQQEYIRTTINQTD 1179
Cdd:PRK05691  698 YNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEA 777

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1180 HTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYAEWEQVQL 1259
Cdd:PRK05691  778 RQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWL 857

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1260 NLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQENISMYMLFLAAYIQLLHYL 1339
Cdd:PRK05691  858 AQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRY 937

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1340 TDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVIEQINPDRSFGn 1419
Cdd:PRK05691  938 SGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG- 1016

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1420 npIFSTMFSYqkdilQQHDAYKLQLLPN--------KQDISKFDISLAVEEglDYVG---ISFEYDINLFKEESINRFTQ 1488
Cdd:PRK05691 1017 --LFQVMFNH-----QQRDLSALRRLPGllaeelpwHSREAKFDLQLHSEE--DRNGrltLSFDYAAELFDAATIERLAE 1087

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1489 NLLNILDAFIHQRTVTYENLSFLSQEEESLYKKVNHTERPyPYFQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSS 1568
Cdd:PRK05691 1088 HFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCA-PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQA 1166

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1569 NQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSD 1648
Cdd:PRK05691 1167 NRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAE 1246

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1649 YKVSIIEDiyrtTINDDVKILNKP------DDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYS 1722
Cdd:PRK05691 1247 GVSAIALD----SLHLDSWPSQAPglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAP 1322

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1723 HSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQAT----ISDLPTVFFNElstsltkLDSEKIRSLRFIIM 1798
Cdd:PRK05691 1323 ISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTtlhfVPPLLQLFIDE-------PLAAACTSLRRLFS 1395

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1799 GGEAASTnAIRSWQNTFKNQVQLVNEYGPTEATVSAMYYFIPVLEGENnllgsVPIGIPISNTKVHILNSYMQYCPVGCM 1878
Cdd:PRK05691 1396 GGEALPA-ELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGER-----SPIGRPLGNVLCRVLDAELNLLPPGVA 1469

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1879 GELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAML 1958
Cdd:PRK05691 1470 GELCIGGAGLARGYLGRPALTAERFVPDPLGEDGA-RLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLL 1548

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1959 QLEGISQAVVTQTEG--GMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPkiEFG 2036
Cdd:PRK05691 1549 AQPGVAQAAVLVREGaaGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALP--EPV 1626

                        1690      1700      1710      1720
                  ....*....|....*....|....*....|....*....|....*.
gi 446581728 2037 HEQKDEckLKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSL 2082
Cdd:PRK05691 1627 WQQREH--VEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSL 1670
PRK12316 PRK12316
peptide synthase; Provisional
 1069-2114 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 706.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1069 VLKVADKESYQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILN 1148
Cdd:PRK12316   41 PAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1149 SIAIDLIHDEIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMK 1228
Cdd:PRK12316  121 DRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSR 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1229 VYSAFAKRRNPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNE 1308
Cdd:PRK12316  201 FYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPA 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1309 MKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQV 1388
Cdd:PRK12316  281 LAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAG 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1389 VREKCLNSFQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQK---DI--LQQHDAYKLQLLPNKQDISKFDISLAVEEG 1463
Cdd:PRK12316  361 VKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPlvaDIeaLDTVAGLEFGQLEWKSRTTQFDLTLDTYEK 440

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1464 LDYVGISFEYDINLFKEESINRFTQNLLNILDAFIHQRTVTYENLSFLSQEEES-LYKKVNHTERPYPYFQNIQEQFYMQ 1542
Cdd:PRK12316  441 GGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGqLVEGWNATAAEYPLQRGVHRLFEEQ 520

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRI 1622
Cdd:PRK12316  521 VERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERL 600

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1623 NYIVRDSEACRIITSNKFKSHLNVS------DYKVSIIEDIYRTTINDDVKIlnKPDDLAYVIYTSGSTGKPKGTLLTHK 1696
Cdd:PRK12316  601 AYMLEDSGVQLLLSQSHLGRKLPLAagvqvlDLDRPAAWLEGYSEENPGTEL--NPENLAYVIYTSGSTGKPKGAGNRHR 678

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1697 GVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFN 1776
Cdd:PRK12316  679 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQ 758

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1777 ELstsLTKLDSEKIRSLRFIIMGGEAASTNAIrswQNTF--KNQVQLVNEYGPTEATVSAMyYFIPVLEGEnnllGSVPI 1854
Cdd:PRK12316  759 AF---LQDEDVASCTSLRRIVCSGEALPADAQ---EQVFakLPQAGLYNLYGPTEAAIDVT-HWTCVEEGG----DSVPI 827

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1855 GIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSedNSKRLYRTGDLVRWLPNGNIEFM 1934
Cdd:PRK12316  828 GRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFV--AGERMYRTGDLARYRADGVIEYA 905

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1935 GRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVtQTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHV 2014
Cdd:PRK12316  906 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV-LAVDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLAL 984

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2015 LEIPITANGKIDFEKLPKIEFGHEQKDEckLKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKLKPL 2094
Cdd:PRK12316  985 ERLPLTPNGKLDRKALPAPEASVAQQGY--VAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA 1062

                        1050      1060
                  ....*....|....*....|
gi 446581728 2095 YPNLKIQDFFKYRTIEKLAS 2114
Cdd:PRK12316 1063 GIQLSPRDLFQHQTIRSLAL 1082
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 20-1293 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 700.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   20 QEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIPIKDLTAFK 99
Cdd:COG1020    24 QQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  100 NTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKSNVEFE 179
Cdd:COG1020   104 EALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  180 SP--YKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFAKKNNIS 257
Cdd:COG1020   184 LPiqYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVT 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  258 IYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAITYKHNS 337
Cdd:COG1020   264 LFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLP 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  338 YSHIVKDLNLNTNTNHNMVYSTAFN--TMKIPELKIPDIESTVLTDCKRVNPFNMTWRIMRYEGETEnkIEVDYNSALYK 415
Cdd:COG1020   344 FERLVEELQPERDLSRNPLFQVMFVlqNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGDGLR--LTLEYNTDLFD 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  416 PESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKD-HRLYKEMNSNALTYPNLKTLDQLIDLQALKSPNQIAISMGDQS 494
Cdd:COG1020   422 AATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAErQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQS 501

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  495 ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKK 574
Cdd:COG1020   502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQS 581

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  575 EYRGLVERFAIHTIYLEDFHYAN-SIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVF 653
Cdd:COG1020   582 ALAARLPELGVPVLALDALALAAePATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRV 661

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  654 LQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLklnSVKRLFV 733
Cdd:COG1020   662 LQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALP---SLRLVLV 738

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  734 GGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEIQKEiSNIPIGKPIANSEVFVISPFNTLCPSGVVGE 813
Cdd:COG1020   739 GGEALPPELVRRWRARLP-GARLVNLYGPTETTVDSTYYEVTPPDADG-GSVPIGRPIANTRVYVLDAHLQPVPVGVPGE 816

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  814 LFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKH 893
Cdd:COG1020   817 LYIGGAGLARGYLNRPELTAERFVA-DPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH 895

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  894 PEVRDAVVFTYQN---DKIVCFYL-SKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQIPSL 969
Cdd:COG1020   896 PGVREAVVVAREDapgDKRLVAYVvPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA 975

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  970 LENmqkQYVPPISETEKRLAKTWAEILNLgkyRIGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIASLS 1049
Cdd:COG1020   976 AAA---AAAPPAEEEEEEAALALLLLLVV---VVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAA 1049

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1050 AYIDKLMAVNHDREEQEMQVLKVADKESYQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLnkdILQDTIRFLVERHE 1129
Cdd:COG1020  1050 AAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALL---LLLALLLALLAALR 1126

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1130 MLRTVFIERNGEPRQVILNSIAIDLIHDEIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFnlnkkksYLYINL 1209
Cdd:COG1020  1127 ARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLL-------LLLLLL 1199

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1210 HHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFS 1289
Cdd:COG1020  1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279


                  ....
gi 446581728 1290 RNRQ 1293
Cdd:COG1020  1280 LPAL 1283
PRK12467 PRK12467
peptide synthase; Provisional
 20-1315 5.87e-178

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 613.32  E-value: 5.87e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   20 QEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQK--NVEFDIPIKDLTa 97
Cdd:PRK12467 1123 QERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPvgSLTLEEPLLLAA- 1201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   98 fknTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKSNVE 177
Cdd:PRK12467 1202 ---DKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQL 1278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  178 FESP--YKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFAKKNN 255
Cdd:PRK12467 1279 PALPiqYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREG 1358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  256 ISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAITYKH 335
Cdd:PRK12467 1359 VTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQD 1438

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  336 NSYSHIVKDLNLNTNTNHNMVYSTAFN--------TMKIPELKIPDIESTVltdckRVNPFNMTWRImrYEGETENKIEV 407
Cdd:PRK12467 1439 LPFEQLVEALQPERSLSHSPLFQVMFNhqrddhqaQAQLPGLSVESLSWES-----QTAQFDLTLDT--YESSEGLQASL 1511

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  408 DYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDHRLYKEM-NSNALTYPNLKTLDQLIDLQALKSPNQI 486
Cdd:PRK12467 1512 TYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGwNATHTGYPLARLVHQLIEDQAAATPEAV 1591

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  487 AISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSE 566
Cdd:PRK12467 1592 ALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSG 1671

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  567 SQMIITKkeyRGLVERFAI----HTIYLE---DFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSY 639
Cdd:PRK12467 1672 IELLLTQ---SHLQARLPLpdglRSLVLDqedDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLC 1748

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  640 SVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPk 719
Cdd:PRK12467 1749 ATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD- 1827

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  720 EMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEVFVI 799
Cdd:PRK12467 1828 EQVEHPLSLRRVVCGGEALEVEALRPWLERLP-DTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYIL 1906

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  800 SPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGY 879
Cdd:PRK12467 1907 DASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVA-DPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 1985

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  880 RIELDEIEGTLFKHPEVRDAVVFTYQ--NDKIVCFYLSKDNTELK---------QEALKTFLSESLPDFMMPNYIFHLES 948
Cdd:PRK12467 1986 RIELGEIEARLREQGGVREAVVIAQDgaNGKQLVAYVVPTDPGLVdddeaqvalRAILKNHLKASLPEYMVPAHLVFLAR 2065

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  949 FPVSPSGKLDRKKLELQIPSLlenMQKQYVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGHSLIAVQVLNQIQK 1028
Cdd:PRK12467 2066 MPLTPNGKLDRKALPAPDASE---LQQAYVAPQSELEQRLAAIWQDVLGLE--QVGLHDNFFELGGDSIISIQVVSRARQ 2140

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1029 EfHLKIEIRDIFEHTTIASLSAYI---DKLMAVNHDREEQEMQVLKVaDKESYQLSSAQKRIWflNKynainrvydtplH 1105
Cdd:PRK12467 2141 A-GIRFTPKDLFQHQTVQSLAAVAqegDGTVSIDQGPVTGDLPLLPI-QQMFFADDIPERHHW--NQ------------S 2204

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1106 IYIEP--SLNKDILQDTIRFLVERHEMLRTVFIERNG-----------EPRQVILNSIAIDLihDEIEHMSKKEQQEyir 1172
Cdd:PRK12467 2205 VLLEPreALDAELLEAALQALLVHHDALRLGFVQEDGgwsamhrapeqERRPLLWQVVVADK--EELEALCEQAQRS--- 2279

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1173 ttinqtdhtpFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYA 1252
Cdd:PRK12467 2280 ----------LDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWA 2349

                        1290      1300      1310      1320      1330      1340
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581728 1253 EWEQVQLNLGRWDTEKSYWMAEL-AAPlpiLNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQ 1315
Cdd:PRK12467 2350 ERLQTYAASAALADELGYWQAQLqGAS---TELPCDHPQGGLQRRHAASVTTHLDSEWTRRLLQ 2410
PRK12316 PRK12316
peptide synthase; Provisional
 11-1315 3.40e-177

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 611.19  E-value: 3.40e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   11 VEELDVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNvefdI 90
Cdd:PRK12316 2600 VQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPN----M 2675

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   91 PIKDLTAFKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELL 170
Cdd:PRK12316 2676 SLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGAR 2755

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  171 QGKSNVEFESP--YKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQ 248
Cdd:PRK12316 2756 RGEQPTLPPLPlqYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELL 2835

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  249 CFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIH 328
Cdd:PRK12316 2836 ALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQAL 2915

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  329 LAITYKHNSYSHIVKDLNLNTNTNHNMVYSTAFN----TMKIPELKIPDIEStvLTDCKRVNPFNMTwrIMRYEGETENK 404
Cdd:PRK12316 2916 GAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNhqsgERAAAQLPGLHIES--FAWDGAATQFDLA--LDTWESAEGLG 2991

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  405 IEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLL-LEKDHRLYKEMNSNALTYPNLKTLDQLIDLQALKSP 483
Cdd:PRK12316 2992 ASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLdAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTP 3071

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  484 NQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILK 563
Cdd:PRK12316 3072 DAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLE 3151

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  564 DSESQMIITKKEYRgLVERFAIHTIYLEDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVIN 643
Cdd:PRK12316 3152 DSGAQLLLSQSHLR-LPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ 3230

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  644 TFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITnvVLPTAFFKLIADMPKEMLL 723
Cdd:PRK12316 3231 AYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVD--VLHAYPSMLQAFLEEEDAH 3308

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  724 KLNSVKRLFVGGETLPAESVRKWQSKLglkiPVLNAYGPTETTVCATMYEVNGEIQkeiSNIPIGKPIANSEVFVISPFN 803
Cdd:PRK12316 3309 RCTSLKRIVCGGEALPADLQQQVFAGL----PLYNLYGPTEATITVTHWQCVEEGK---DAVPIGRPIANRACYILDGSL 3381

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  804 TLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIEL 883
Cdd:PRK12316 3382 EPVPVGALGELYLGGEGLARGYHNRPGLTAERFVP--DPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIEL 3459

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  884 DEIEGTLFKHPEVRDAVVFTYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLE 963
Cdd:PRK12316 3460 GEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALP 3539

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  964 LQIPSLLenmQKQYVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGHSLIAVQVLNQIQK---EFHLKieirDIF 1040
Cdd:PRK12316 3540 RPDAALL---QQDYVAPVNELERRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQagiRFTPK----DLF 3610

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1041 EHTTIASLS--AYIDKLMAVNHDREEQEMqVLKVADKESYQLSSAQKRIWFLNkynainrvydtplhIYIEPS--LNKDI 1116
Cdd:PRK12316 3611 QHQTIQGLArvARVGGGVAVDQGPVSGET-LLLPIQQQFFEEPVPERHHWNQS--------------LLLKPReaLDAAA 3675

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1117 LQDTIRFLVERHEMLRTVFIERNG----EPRQVILNSIAidLIHDEIEHMSKKEQqeyirttINQTDHTPFDLEKGPLFR 1192
Cdd:PRK12316 3676 LEAALQALVEHHDALRLRFVEDAGgwtaEHLPVELGGAL--LWRAELDDAEELER-------LGEEAQRSLDLADGPLLR 3746

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1193 IRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWM 1272
Cdd:PRK12316 3747 ALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQ 3826

                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|...
gi 446581728 1273 AELAAPLPilNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQ 1315
Cdd:PRK12316 3827 EQLQGVSS--ELPCDHPQGALQNRHAASVQTRLDRELTRRLLQ 3867
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1547-2026 2.57e-174

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 542.50  E-value: 2.57e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSnkfkshlnvsdykvsiiediyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRN 1706
Cdd:cd05930    81 EDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELstsLTKLD 1786
Cdd:cd05930   127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLL---LQELE 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1787 SEKIRSLRFIIMGGEAASTNAIRSWQNTFkNQVQLVNEYGPTEATVSAMYYfipVLEGENNLLGSVPIGIPISNTKVHIL 1866
Cdd:cd05930   204 LAALPSLRLVLVGGEALPPDLVRRWRELL-PGARLVNLYGPTEATVDATYY---RVPPDDEEDGRVPIGRPIPNTRVYVL 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1867 NSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEdnSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGH 1946
Cdd:cd05930   280 DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP--GERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGY 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1947 RIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANG 2023
Cdd:cd05930   358 RIELGEIEAALLAHPGVREAAVVareDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437


                  ...
gi 446581728 2024 KID 2026
Cdd:cd05930   438 KVD 440
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 483-962 9.96e-170

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 529.79  E-value: 9.96e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITkkeyrglverfaihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVI 642
Cdd:cd05930    81 EDSGAKLVLT----------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  643 NTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEML 722
Cdd:cd05930   127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  723 lkLNSVKRLFVGGETLPAESVRKWqSKLGLKIPVLNAYGPTETTVCATMYEVNGEIQKEiSNIPIGKPIANSEVFVISPF 802
Cdd:cd05930   207 --LPSLRLVLVGGEALPPDLVRRW-RELLPGARLVNLYGPTEATVDATYYRVPPDDEED-GRVPIGRPIPNTRVYVLDEN 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  803 NTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLdkSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIE 882
Cdd:cd05930   283 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPN--PFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIE 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  883 LDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:cd05930   361 LGEIEAALLAHPGVREAAVVAREDGDgekrLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440


                  ....
gi 446581728  959 RKKL 962
Cdd:cd05930   441 RKAL 444
PRK12316 PRK12316
peptide synthase; Provisional
 4-1315 3.45e-169

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 586.15  E-value: 3.45e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728    4 IQKKYEIVEELDVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQ 83
Cdd:PRK12316   40 IPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   84 KNVEFDIPIKDLTAFKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLS 163
Cdd:PRK12316  120 LDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFS 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  164 NTYGELLQGKSnVEFES---PYKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNIN 240
Cdd:PRK12316  200 RFYSAYATGAE-PGLPAlpiQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSID 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  241 SDLFYQIQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGIL 320
Cdd:PRK12316  279 PALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLL 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  321 NKVNKSIHLAITYKHNSYSHIVKdlnlNTNTNHNMVYSTAFNTMKIPELKIPDIESTVLTDCKRVNPFNMTWRIMR---- 396
Cdd:PRK12316  359 AGVKDTVLGAQAHQDLPFERLVE----ALKVERSLSHSPLFQVMYNHQPLVADIEALDTVAGLEFGQLEWKSRTTQfdlt 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  397 ---YEGETENKIEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDH-RLYKEMNSNALTYPNLKTLD 472
Cdd:PRK12316  435 ldtYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERgQLVEGWNATAAEYPLQRGVH 514

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  473 QLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPK 552
Cdd:PRK12316  515 RLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  553 FPEKRIEYILKDSESQMIITKKEYRGLVERFA-IHTIYLED---FHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVV 628
Cdd:PRK12316  595 YPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAgVQVLDLDRpaaWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAG 674

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  629 VPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPT 708
Cdd:PRK12316  675 NRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVP 754

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  709 AFfkLIADMPKEMLLKLNSVKRLFVGGETLPAESV-----RKWQSKLglkipvLNAYGPTETTVCATMYEVNGEIQKEIs 783
Cdd:PRK12316  755 SM--LQAFLQDEDVASCTSLRRIVCSGEALPADAQeqvfaKLPQAGL------YNLYGPTEAAIDVTHWTCVEEGGDSV- 825

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  784 niPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldKSYNRDKKMYCTGDLVRLLANGN 863
Cdd:PRK12316  826 --PIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVP--SPFVAGERMYRTGDLARYRADGV 901

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  864 LEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYI 943
Cdd:PRK12316  902 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQW 981

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  944 FHLESFPVSPSGKLDRKKLELQIPSLlenMQKQYVPPISETEKRLAKTWAEILNLgkYRIGRDDDFFKLGGHSLIAVQVL 1023
Cdd:PRK12316  982 LALERLPLTPNGKLDRKALPAPEASV---AQQGYVAPRNALERTLAAIWQDVLGV--ERVGLDDNFFELGGDSIVSIQVV 1056

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1024 NQiQKEFHLKIEIRDIFEHTTIASLS--AYIDKLMAVNHDREEQEMQVLKVaDKESYQLSSAQKRIWflnkynainrvyD 1101
Cdd:PRK12316 1057 SR-ARQAGIQLSPRDLFQHQTIRSLAlvAKAGQATAADQGPASGEVALAPV-QRWFFEQAIPQRQHW------------N 1122

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1102 TPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIhdeieHMSKKEQQEYIRTTINQTDHT 1181
Cdd:PRK12316 1123 QSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVL-----WQRQAASEEELLALCEEAQRS 1197

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1182 pFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYsafaKRRNPELPTISNRYVDYAewEQVQLNL 1261
Cdd:PRK12316 1198 -LDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAY----ADLDADLPARTSSYQAWA--RRLHEHA 1270

                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1262 GRWDTEKSYWMAELA-APlpiLNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQ 1315
Cdd:PRK12316 1271 GARAEELDYWQAQLEdAP---HELPCENPDGALENRHERKLELRLDAERTRQLLQ 1322
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1537-2032 1.98e-158

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 499.93  E-value: 1.98e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1537 EQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVK 1616
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1617 YPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHK 1696
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1697 GVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFN 1776
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1777 ELStsltKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVQLVNEYGPTEATVSAMYYfipVLEGENNLLGSVPIGI 1856
Cdd:cd17655   241 LLD----AADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIY---QYEPETDQQVSVPIGK 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1857 PISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEdnSKRLYRTGDLVRWLPNGNIEFMGR 1936
Cdd:cd17655   314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVP--GERMYRTGDLARWLPDGNIEFLGR 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1937 KDKQVKIRGHRIELGEIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKTVDGIGIEknKLAIHLSNVLPEYMVPKYYSH 2013
Cdd:cd17655   392 IDHQVKIRGYRIELGEIEARLLQHPDIKEAVViarKDEQGQNYLCAYIVSEKELPVA--QLREFLARELPDYMIPSYFIK 469

                         490
                  ....*....|....*....
gi 446581728 2014 VLEIPITANGKIDFEKLPK 2032
Cdd:cd17655   470 LDEIPLTPNGKVDRKALPE 488
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 473-962 4.29e-158

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 498.78  E-value: 4.29e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  473 QLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPK 552
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  553 FPEKRIEYILKDSESQMIITKKEYRGLvERFAIHTIYLEDFH-YANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPH 631
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPP-IAFIGLIDLLDEDTiYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  632 KGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFF 711
Cdd:cd17655   160 RGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  712 KLIADMPKEMLLKLnsvKRLFVGGETLPAESVRKWQSKLGLKIPVLNAYGPTETTVCATMYEVNGEIQKEISnIPIGKPI 791
Cdd:cd17655   240 KLLDAADDSEGLSL---KHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQVS-VPIGKPL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  792 ANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFIslDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKD 871
Cdd:cd17655   316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFV--DDPFVPGERMYRTGDLARWLPDGNIEFLGRID 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  872 NQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTY---QNDKIVCFYLSKDNtELKQEALKTFLSESLPDFMMPNYIFHLES 948
Cdd:cd17655   394 HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARkdeQGQNYLCAYIVSEK-ELPVAQLREFLARELPDYMIPSYFIKLDE 472

                         490
                  ....*....|....
gi 446581728  949 FPVSPSGKLDRKKL 962
Cdd:cd17655   473 IPLTPNGKVDRKAL 486
PRK12316 PRK12316
peptide synthase; Provisional
 1037-2117 1.57e-154

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 539.93  E-value: 1.57e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1037 RDIFEHTTIASLS-AYIDKLMA-VNHDREEqEMQVLKVAD---------------------KESYQLSSAQKRIWFLNKY 1093
Cdd:PRK12316 4040 REMFEEATIQRLAdDYAAELTAlVEHCCDA-ERHGVTPSDfplagldqarldalplplgeiEDIYPLSPMQQGMLFHSLY 4118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1094 NAINRVYDTPLHIYIEpSLNKDILQDTIRFLVERHEMLRTVFIERN--GEPRQVILNSIaiDLIHDEIEHMSKKEQQEYI 1171
Cdd:PRK12316 4119 EQEAGDYINQMRVDVQ-GLDVERFRAAWQAALDRHDVLRSGFVWQGelGRPLQVVHKQV--SLPFAELDWRGRADLQAAL 4195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1172 RTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAfakrRNPELPtiSNRYVDY 1251
Cdd:PRK12316 4196 DALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSG----RPPAQP--GGRYRDY 4269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1252 AEWeqvqlnLGRWDTE--KSYWMAELAAPLPILNLPLDFSRNRQSTNKGTV-FEMKLDNEMKESLKQVCEQENISMYMLF 1328
Cdd:PRK12316 4270 IAW------LQRQDAAasEAFWREQLAALDEPTRLAQAIARADLRSANGYGeHVRELDATATARLREFARTQRVTLNTLV 4343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1329 LAAYIQLLHYLTDQKDIIVGTPVVGR--NHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFdk 1406
Cdd:PRK12316 4344 QAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPL-- 4421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1407 viEQINPDRSFGNNPIFSTMFSYQ----KDILQQHDAYKL---QLLPNKQDISKFDISLAVEEGLDyvgISFEYDINLFK 1479
Cdd:PRK12316 4422 --YEIQRWAGQGGEALFDSLLVFEnypvSEALQQGAPGGLrfgEVTNHEQTNYPLTLAVGLGETLS---LQFSYDRGHFD 4496

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1480 EESINRFTQNLLNILDAFIHQRTVTYENLSFLSQEEESLYKKV-NHTERPYPYFQNIQEQFYMQVDRQPERIAIATATES 1558
Cdd:PRK12316 4497 AATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALwNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEK 4576

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSN 1638
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1639 KFKSHLNVSDYKVSIIEDIY-----RTTINDDVKIlnKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISP 1713
Cdd:PRK12316 4657 HLLQRLPIPDGLASLALDRDedwegFPAHDPAVRL--HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTP 4734

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1714 NDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQaIQETQATISDLPTVFFNELSTSLTKlDSEkIRSL 1793
Cdd:PRK12316 4735 DDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAE-IHEHRVTVLVFPPVYLQQLAEHAER-DGE-PPSL 4811

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1794 RFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYfiPVLEGENNLLGSVPIGIPISNTKVHILNSYMQYC 1873
Cdd:PRK12316 4812 RVYCFGGEAVAQASYDLAWRALKP-VYLFNGYGPTETTVTVLLW--KARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPL 4888

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1874 PVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEI 1953
Cdd:PRK12316 4889 PVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGG-RLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEI 4967

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1954 EDAMLQLEGISQAVVTQTEG--GMLLQAYY-----KTVDGIGIE---KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANG 2023
Cdd:PRK12316 4968 EARLREHPAVREAVVIAQEGavGKQLVGYVvpqdpALADADEAQaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNG 5047

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2024 KIDFEKLPKIEFGHEQkdECKLKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKLKpLYPNLKI--Q 2101
Cdd:PRK12316 5048 KLDRKALPQPDASLLQ--QAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQ-LELGLELplR 5124

                        1130
                  ....*....|....*.
gi 446581728 2102 DFFKYRTIEKLASHIE 2117
Cdd:PRK12316 5125 ELFQTPTLAAFVELAA 5140
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1537-2030 1.08e-147

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 468.99  E-value: 1.08e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1537 EQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVK 1616
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1617 YPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVsIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHK 1696
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAV-VIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1697 GVLNLVEWRNEVfQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFN 1776
Cdd:cd12117   160 GVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1777 ElstsLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYFIPVLEGENnllGSVPIGI 1856
Cdd:cd12117   239 Q----LADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPG-LRLVNGYGPTENTTFTTSHVVTELDEVA---GSIPIGR 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1857 PISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFseDNSKRLYRTGDLVRWLPNGNIEFMGR 1936
Cdd:cd12117   311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF--GPGERLYRTGDLARWLPDGRLEFLGR 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1937 KDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEknKLAIHLSNVLPEYMVPKYYSH 2013
Cdd:cd12117   389 IDDQVKIRGFRIELGEIEAALRAHPGVREAVVVvreDAGGDKRLVAYVVAEGALDAA--ELRAFLRERLPAYMVPAAFVV 466

                         490
                  ....*....|....*..
gi 446581728 2014 VLEIPITANGKIDFEKL 2030
Cdd:cd12117   467 LDELPLTANGKVDRRAL 483
PRK12467 PRK12467
peptide synthase; Provisional
 1125-2113 1.30e-146

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 513.94  E-value: 1.30e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1125 VERHEMLRTVFIERNG--EPRQVILNSIAIDLIhdEIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKK 1202
Cdd:PRK12467 2693 IDRHEILRSGFLWDGEleEPLQVVYKQARLPFS--RLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDR 2770

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1203 SYLYINLHHIITDEWSVRNLLDELMKVYSAFAkrrnpeLPTISNRYVDYAEWeqvqlnLGRWDTEKS--YWMAELAA-PL 1279
Cdd:PRK12467 2771 HHLIYTNHHILMDGWSGSQLLGEVLQRYFGQP------PPAREGRYRDYIAW------LQAQDAEASeaFWKEQLAAlEE 2838

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1280 PILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQ-- 1357
Cdd:PRK12467 2839 PTRLARALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQlr 2918

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1358 EFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYP---------------FDKVIeqinpdrSFGNNPI 1422
Cdd:PRK12467 2919 GAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPladiqrwagqggealFDSIL-------VFENYPI 2991

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1423 fstmfsyqKDILQQHDAYKLQL--LPNkQDISKFDISLAVEEGlDYVGISFEYDINLFKEESINRFTQNLLNILDAFIHQ 1500
Cdd:PRK12467 2992 --------SEALKQGAPSGLRFgaVSS-REQTNYPLTLAVGLG-DTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNN 3061

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1501 RTVTYENLSFLSQEE-ESLYKKVNHTERPYPYFQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKG 1579
Cdd:PRK12467 3062 PAARLGELPTLAAHErRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIG 3141

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1580 IKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLNV--SDYKVSIIEDI 1657
Cdd:PRK12467 3142 VGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPApaGDTALTLDRLD 3221

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1658 YRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLL 1737
Cdd:PRK12467 3222 LNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLI 3301

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1738 NGAELyLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELstsLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKn 1817
Cdd:PRK12467 3302 CGGCL-VVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQF---AEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLK- 3376

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1818 QVQLVNEYGPTEATVSAMYYFIPVleGENNLLGSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKE 1897
Cdd:PRK12467 3377 PRGLTNGYGPTEAVVTVTLWKCGG--DAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPS 3454

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1898 KTKQAFISNPFSeDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV--TQTEGGM 1975
Cdd:PRK12467 3455 LTAERFVADPFS-GSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVlaRDGAGGK 3533

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1976 LLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFgheQKDECKLKPQTKVQKDI 2055
Cdd:PRK12467 3534 QLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA---KGSREYVAPRSEVEQQL 3610

                         970       980       990      1000      1010
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728 2056 AKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKL-KPLYPNLKIQDFFKYRTIEKLA 2113
Cdd:PRK12467 3611 AAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIrQSLGLKLSLRDLMSAPTIAELA 3669
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1560-1968 2.99e-143

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 453.26  E-value: 2.99e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1560 TYRQLNMSSNQVAQHLL-EKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSN 1638
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1639 KFKSHLNVSDYKVSIIEDIYRTTINDD-----VKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISP 1713
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDApapppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1714 NDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVE-YAQAIQETQATISDLPTVFFNelstSLTKLDSEKIRS 1792
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAAlLAALIAEHPVTVLNLTPSLLA----LLAAALPPALAS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1793 LRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYfiPVLEGENNLLGSVPIGIPISNTKVHILNSYMQY 1872
Cdd:TIGR01733  237 LRLVILGGEALTPALVDRWRARGPG-ARLINLYGPTETTVWSTAT--LVDPDDAPRESPVPIGRPLANTRLYVLDDDLRP 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1873 CPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGE 1952
Cdd:TIGR01733  314 VPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393

                          410
                   ....*....|....*.
gi 446581728  1953 IEDAMLQLEGISQAVV 1968
Cdd:TIGR01733  394 IEAALLRHPGVREAVV 409
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 473-962 5.54e-142

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 452.43  E-value: 5.54e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  473 QLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPK 552
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  553 FPEKRIEYILKDSESQMIITKKEYRGLVeRFAIHTIYLEDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHK 632
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRA-GGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  633 GVVNLsysVINTFH--LGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAF 710
Cdd:cd12117   160 GVVRL---VKNTNYvtLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAAL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  711 FKLIADMPKEMllkLNSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVnGEIQKEISNIPIGKP 790
Cdd:cd12117   237 FNQLADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACP-GLRLVNGYGPTENTTFTTSHVV-TELDEVAGSIPIGRP 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  791 IANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLdkSYNRDKKMYCTGDLVRLLANGNLEFIGRK 870
Cdd:cd12117   312 IANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVAD--PFGPGERLYRTGDLARWLPDGRLEFLGRI 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  871 DNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN---DKIVCFYLSKDnTELKQEALKTFLSESLPDFMMPNYIFHLE 947
Cdd:cd12117   390 DDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDaggDKRLVAYVVAE-GALDAAELRAFLRERLPAYMVPAAFVVLD 468

                         490
                  ....*....|....*
gi 446581728  948 SFPVSPSGKLDRKKL 962
Cdd:cd12117   469 ELPLTANGKVDRRAL 483
PRK05691 PRK05691
peptide synthase; Validated
 20-1315 1.72e-139

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 491.22  E-value: 1.72e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   20 QEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIPIKDLTAFK 99
Cdd:PRK05691 1735 QQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALP 1814

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  100 NTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKsnvefE 179
Cdd:PRK05691 1815 ADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDR-----E 1889

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  180 SPYKNLVKHeesFIDSAIYK-------EGS---SYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQC 249
Cdd:PRK05691 1890 SPLEPLPVQ---YLDYSVWQrqwlesgERQrqlDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRA 1966

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  250 FAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHL 329
Cdd:PRK05691 1967 FNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIE 2046

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  330 AITYKHNSYSHIVKdlnlNTNTNHNMVYSTAFNTM---------KIPELKIPDIEstVLTDCKRVNPFNMTWRIMRYEGE 400
Cdd:PRK05691 2047 GQSHQDLPFDHLVE----ALQPPRSAAYNPLFQVMcnvqrwefqQSRQLAGMTVE--YLVNDARATKFDLNLEVTDLDGR 2120

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  401 TenKIEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDH-RLYKEMNSNALTYPNLKTLDQLIDLQA 479
Cdd:PRK05691 2121 L--GCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQqQLLDSLAGEAGEARLDQTLHGLFAAQA 2198

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  480 LKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIE 559
Cdd:PRK05691 2199 ARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLH 2278

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  560 YILKDSESQMIITkkeYRGLVERFA-----IHTIYLED-----FHYANSieNIASTHTIEDAAYIIYTSGSTGLPKGVVV 629
Cdd:PRK05691 2279 YMIEDSGIGLLLS---DRALFEALGelpagVARWCLEDdaaalAAYSDA--PLPFLSLPQHQAYLIYTSGSTGKPKGVVV 2353

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  630 PHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEiEKRSAEEFINVSQKYGITNVVLPTA 709
Cdd:PRK05691 2354 SHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQ-GQWGAEEICQLIREQQVSILGFTPS 2432

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  710 FFKLIAdmpkEMLLKLN---SVKRLFVGGETLPAEsvrKWQSKLGLKIPVL--NAYGPTETTVCATMYEVNGEIQKEISN 784
Cdd:PRK05691 2433 YGSQLA----QWLAGQGeqlPVRMCITGGEALTGE---HLQRIRQAFAPQLffNAYGPTETVVMPLACLAPEQLEEGAAS 2505

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  785 IPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNL 864
Cdd:PRK05691 2506 VPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVA-DPFAADGGRLYRTGDLVRLRADGLV 2584

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  865 EFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK-------IVCFYLSKDNTELKQ--EALKTFLSESLP 935
Cdd:PRK05691 2585 EYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSgkqlagyLVSAVAGQDDEAQAAlrEALKAHLKQQLP 2664

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  936 DFMMPNYIFHLESFPVSPSGKLDRKKLELqiPSLLENMQkQYVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGH 1015
Cdd:PRK05691 2665 DYMVPAHLILLDSLPLTANGKLDRRALPA--PDPELNRQ-AYQAPRSELEQQLAQIWREVLNVE--RVGLGDNFFELGGD 2739

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1016 SLIAVQVLNQI-QKEFHLKIeiRDIFEHTTIASLSAYIDKLMAVNhdreeqemqvlkvADKESYQLSSAQKRI--WFlnk 1092
Cdd:PRK05691 2740 SILSIQVVSRArQLGIHFSP--RDLFQHQTVQTLAAVATHSEAAQ-------------AEQGPLQGASGLTPIqhWF--- 2801

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1093 ynainrvYDTPL----H----IYIEPS--LNKDILQDTIRFLVERHEMLRTVFIERNGEPRQvilnsiaidlihdeiEHM 1162
Cdd:PRK05691 2802 -------FDSPVpqpqHwnqaLLLEPRqaLDPALLEQALQALVEHHDALRLRFSQADGRWQA---------------EYR 2859

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1163 SKKEQQEYIRTTINQTD---------HTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAF 1233
Cdd:PRK05691 2860 AVTAQELLWQVTVADFAecaalfadaQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQL 2939

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1234 AKRRNPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLpiLNLPLDFSRNRQSTNKGTVFEMKLDNEMKESL 1313
Cdd:PRK05691 2940 SAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPR--AELPCDRPQGGNLNRHAQTVSVRLDAERTRQL 3017


                  ..
gi 446581728 1314 KQ 1315
Cdd:PRK05691 3018 LQ 3019
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 1547-2031 6.70e-139

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 441.69  E-value: 6.70e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSnkfkshlnvsdykvsiiediyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRN 1706
Cdd:cd17652    81 ADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVffnelstSLTKLD 1786
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPA-------ALAALP 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1787 SEKIRSLRFIIMGGEAASTNAIRSWQNTfknqVQLVNEYGPTEATVSAMYYfiPVLEGEnnllGSVPIGIPISNTKVHIL 1866
Cdd:cd17652   200 PDDLPDLRTLVVAGEACPAELVDRWAPG----RRMINAYGPTETTVCATMA--GPLPGG----GVPPIGRPVPGTRVYVL 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1867 NSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGH 1946
Cdd:cd17652   270 DARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGS-RMYRTGDLARWRADGQLEFLGRADDQVKIRGF 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1947 RIELGEIEDAMLQLEGISQAVVTQTE---GGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANG 2023
Cdd:cd17652   349 RIELGEVEAALTEHPGVAEAVVVVRDdrpGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNG 428


                  ....*...
gi 446581728 2024 KIDFEKLP 2031
Cdd:cd17652   429 KLDRRALP 436
PRK12316 PRK12316
peptide synthase; Provisional
 1078-2120 3.06e-138

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 487.54  E-value: 3.06e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1078 YQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEpSLNKDILQDTIRFLVERHEMLRTVFIERNG--EPRQVILNSIAIDLI 1155
Cdd:PRK12316 1557 YPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQ-GLDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIHKQVELPFA 1635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1156 hdEIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAfak 1235
Cdd:PRK12316 1636 --ELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG--- 1710

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1236 rrnPELPTISNRYVDYAEWEQVQlnlgRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMkLDNEMKESLKQ 1315
Cdd:PRK12316 1711 ---QPVAAPGGRYRDYIAWLQRQ----DAAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQL-LDPAQTRALAE 1782

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1316 VCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNH--QEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKC 1393
Cdd:PRK12316 1783 FARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALN 1862

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1394 LNSFQNQSYPfdkvIEQINPDRSFGNNPIFSTMFSYQK----DILQQHDAYKLQL-LPNKQDISKFDISLAVEEGlDYVG 1468
Cdd:PRK12316 1863 LALREHEHTP----LYDIQRWAGQGGEALFDSLLVFENypvaEALKQGAPAGLVFgRVSNHEQTNYPLTLAVTLG-ETLS 1937

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1469 ISFEYDINLFKEESINRFTQNLLNILDAFIHQRTVTYENLSFLSQEEESLY-KKVNHTERPYPYFQNIQEQFYMQVDRQP 1547
Cdd:PRK12316 1938 LQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRIlADWDRTPEAYPRGPGVHQRIAEQAARAP 2017

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1548 ERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVR 1627
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLE 2097

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1628 DSEACRIITSNKFKSHLNVSDYKVSII---EDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEW 1704
Cdd:PRK12316 2098 DSGAALLLTQRHLLERLPLPAGVARLPldrDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQA 2177

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1705 RNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQaIQETQATISDLPTVFFNELSTSLtK 1784
Cdd:PRK12316 2178 AGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDE-MERHGVTILDFPPVYLQQLAEHA-E 2255

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1785 LDSEKIrSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYFIPVLEGENNllGSVPIGIPISNTKVH 1864
Cdd:PRK12316 2256 RDGRPP-AVRVYCFGGEAVPAASLRLAWEALRP-VYLFNGYGPTEAVVTPLLWKCRPQDPCGA--AYVPIGRALGNRRAY 2331

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1865 ILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIR 1944
Cdd:PRK12316 2332 ILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGE-RLYRTGDLARYRADGVVEYLGRIDHQVKIR 2410

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1945 GHRIELGEIEDAMLQLEGISQAVVTQTEG--GMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITAN 2022
Cdd:PRK12316 2411 GFRIELGEIEARLQAHPAVREAVVVAQDGasGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPN 2490

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2023 GKIDFEKLPKIEFghEQKDECKLKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKLK-PLYPNLKIQ 2101
Cdd:PRK12316 2491 GKLDRKALPKPDV--SQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRqDLGLEVPLR 2568

                        1050
                  ....*....|....*....
gi 446581728 2102 DFFKYRTIEKLASHIEEME 2120
Cdd:PRK12316 2569 ILFERPTLAAFAASLESGQ 2587
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1080-2121 3.49e-137

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 466.06  E-value: 3.49e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIA------ID 1153
Cdd:PRK10252   10 LVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTfplpeiID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1154 LIHDEIEHMSKKEQqeyIRTTINQtdhtPFDLEKG-PLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSA 1232
Cdd:PRK10252   90 LRTQPDPHAAAQAL---MQADLQQ----DLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1233 FAKRRNP---ELPTISNRYVDYAEWEQVQlnlgRWDTEKSYW---MAEL-------AAPLPILNLPLDFSRNRQSTNkgt 1299
Cdd:PRK10252  163 WLRGEPTpasPFTPFADVVEEYQRYRASE----AWQRDAAFWaeqRRQLpppaslsPAPLPGRSASADILRLKLEFT--- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1300 vfemklDNEMKESLKQVCEQENISMYMLFLAAYiqlLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDV 1379
Cdd:PRK10252  236 ------DGAFRQLAAQASGVQRPDLALALVALW---LGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQ 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1380 KNLTQLLQVVREKCLNSFQNQSYPfdkvIEQINPD--RSFGNNPIFST-----MFSYQKDI--LQqhdAYKLQLLPNKQD 1450
Cdd:PRK10252  307 ETLPELATRLAAQLKKMRRHQRYD----AEQIVRDsgRAAGDEPLFGPvlnikVFDYQLDFpgVQ---AQTHTLATGPVN 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1451 iskfDISLAV---EEGldyvGISFEYDIN--LFKEESINRFTQNLLNILDAFIHQRTVTYENLSFLSQEEESLYKKVNHT 1525
Cdd:PRK10252  380 ----DLELALfpdEHG----GLSIEILANpqRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNAT 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1526 ERPYPYfQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILK 1605
Cdd:PRK10252  452 AVEIPE-TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1606 AGAAYIPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGST 1685
Cdd:PRK10252  531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGST 610

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1686 GKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQA 1765
Cdd:PRK10252  611 GRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGV 690

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1766 TisdlpTVFF--NELSTSLTKLDSE----KIRSLRFIIMGGEAASTNAIRSWQNTFknQVQLVNEYGPTEATVSAMYYFI 1839
Cdd:PRK10252  691 T-----TTHFvpSMLAAFVASLTPEgarqSCASLRQVFCSGEALPADLCREWQQLT--GAPLHNLYGPTEAAVDVSWYPA 763

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1840 PVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEdnSKRLYRT 1919
Cdd:PRK10252  764 FGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP--GERMYRT 841

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1920 GDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV-------TQTEGGMLLQ--AYYKTVDGIGIE 1990
Cdd:PRK10252  842 GDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQlvGYLVSQSGLPLD 921

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1991 KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFGHEQKDeckLKPQTKVQKDIAKVWSEVLNVKSIGL 2070
Cdd:PRK10252  922 TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPG---RAPKTGTETIIAAAFSSLLGCDVVDA 998

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446581728 2071 KDDFFNLGGHSLKVMPALVKLK-PLYPNLKIQDFFKYRTIEKLASHIEEMED 2121
Cdd:PRK10252  999 DADFFALGGHSLLAMKLAAQLSrQFARQVTPGQVMVASTVAKLATLLDAEED 1050
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1539-2031 5.79e-137

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 438.70  E-value: 5.79e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1539 FYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYP 1618
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1619 EDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNK-PDDLAYVIYTSGSTGKPKGTLLTHKG 1697
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALdADDLAYVIYTSGSTGRPKGVVMPHRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1698 VLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNE 1777
Cdd:cd17651   161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1778 LSTSLTKLDSEkIRSLRFIIMGGEAAS-TNAIRSWqNTFKNQVQLVNEYGPTEATVsAMYYFIPVLEGENNLLgsVPIGI 1856
Cdd:cd17651   241 LAEHGRPLGVR-LAALRYLLTGGEQLVlTEDLREF-CAGLPGLRLHNHYGPTETHV-VTALSLPGDPAAWPAP--PPIGR 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1857 PISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDnsKRLYRTGDLVRWLPNGNIEFMGR 1936
Cdd:cd17651   316 PIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPG--ARMYRTGDLARWLPDGELEFLGR 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1937 KDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTE---GGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSH 2013
Cdd:cd17651   394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdrpGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVL 473

                         490
                  ....*....|....*...
gi 446581728 2014 VLEIPITANGKIDFEKLP 2031
Cdd:cd17651   474 LDALPLTPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 496-901 2.01e-136

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 433.62  E-value: 2.01e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   496 TYYELQQRSNQIVNYLREND-LKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKK 574
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGgVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   575 EYRGLVER--FAIHTIYLEDFHYANSiENIASTHTI----EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLG 648
Cdd:TIGR01733   81 ALASRLAGlvLPVILLDPLELAALDD-APAPPPPDApsgpDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   649 KEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFIN-VSQKYGITNVVLPTAFFKLIADmpkEMLLKLNS 727
Cdd:TIGR01733  160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLALLAA---ALPPALAS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   728 VKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEVFVISPFNTLCP 807
Cdd:TIGR01733  237 LRLVILGGEALTPALVDRWRARGP-GARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVP 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   808 SGVVGELFIGGDGVANGYLNQKEKTEGAFISLDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIE 887
Cdd:TIGR01733  316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395

                          410
                   ....*....|....
gi 446581728   888 GTLFKHPEVRDAVV 901
Cdd:TIGR01733  396 AALLRHPGVREAVV 409
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1535-2031 1.90e-135

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 433.01  E-value: 1.90e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1535 IQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPID 1614
Cdd:cd17644     2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1615 VKYPEDRINYIVRDSEacriitsnkfkshlnvsdykVSIIediyrttinddvkiLNKPDDLAYVIYTSGSTGKPKGTLLT 1694
Cdd:cd17644    82 PNYPQERLTYILEDAQ--------------------ISVL--------------LTQPENLAYVIYTSGSTGKPKGVMIE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1695 HKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVF 1774
Cdd:cd17644   128 HQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAY 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1775 FNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVQLVNEYGPTEATVSAMYYFIPVLEGENNLlgSVPI 1854
Cdd:cd17644   208 WHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNIT--SVPI 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1855 GIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSKRLYRTGDLVRWLPNGNIEFM 1934
Cdd:cd17644   286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPDGNIEYL 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1935 GRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTE---GGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYY 2011
Cdd:cd17644   366 GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREdqpGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAF 445

                         490       500
                  ....*....|....*....|
gi 446581728 2012 SHVLEIPITANGKIDFEKLP 2031
Cdd:cd17644   446 VVLEELPLTPNGKIDRRALP 465
PRK12316 PRK12316
peptide synthase; Provisional
 48-1062 1.38e-134

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 475.60  E-value: 1.38e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   48 LQIEVLKKALTTIVQSHPALRTIFKKRDEKIK--QLIQKNVEFDIPIKDLTAFKNTEqkSILKNFLESIVNEKFSLEEGP 125
Cdd:PRK12316 4136 LDVERFRAAWQAALDRHDVLRSGFVWQGELGRplQVVHKQVSLPFAELDWRGRADLQ--AALDALAAAERERGFDLQRAP 4213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  126 LFKFHIIKFSEDTFILHLMFHHIIYDGWSLgvfirqlSNTYGELLQGKSNVEFESP---YKNLVkheeSFIDSAIYKEGS 202
Cdd:PRK12316 4214 LLRLVLVRTAEGRHHLIYTNHHILMDGWSN-------SQLLGEVLERYSGRPPAQPggrYRDYI----AWLQRQDAAASE 4282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  203 SYWKDYLQGELTPTEFPIDFNK---MNEKRYTDknISKNINSDLFYQIQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEI 279
Cdd:PRK12316 4283 AFWREQLAALDEPTRLAQAIARadlRSANGYGE--HVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTV 4360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  280 IVGIPINTRPYT--EERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAITYKHNSYSHIVK-----DLNLNTNTN 352
Cdd:PRK12316 4361 AFGATVAGRPAElpGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRwagqgGEALFDSLL 4440

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  353 HNMVYSTAFNTMKIPELKIpdIESTVLTDCKRVNPFNMTWRImryeGETEnKIEVDYNSALYKPESISDLVERYIYLLQK 432
Cdd:PRK12316 4441 VFENYPVSEALQQGAPGGL--RFGEVTNHEQTNYPLTLAVGL----GETL-SLQFSYDRGHFDAATIERLARHLTNLLEA 4513

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  433 LMKNVNEPIHSLDLLLEKDHRLYKEM-NSNALTYPNLKTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYL 511
Cdd:PRK12316 4514 MAEDPQRRLGELQLLEKAEQQRIVALwNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHAL 4593

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  512 RENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKkeyRGLVERFAI----HT 587
Cdd:PRK12316 4594 IARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ---SHLLQRLPIpdglAS 4670

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  588 IYL------EDFHYANSIENIASthtiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIF 661
Cdd:PRK12316 4671 LALdrdedwEGFPAHDPAVRLHP----DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSF 4746

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  662 DASIMEIFPILLCGGRMHlISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMlLKLNSVKRLFVGGETLPAE 741
Cdd:PRK12316 4747 DGSHEGLYHPLINGASVV-IRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERD-GEPPSLRVYCFGGEAVAQA 4824

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  742 SVRKWQSKLGLKiPVLNAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGV 821
Cdd:PRK12316 4825 SYDLAWRALKPV-YLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGV 4903

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  822 ANGYLNQKEKTEGAFIS--LDKSYNRdkkMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDA 899
Cdd:PRK12316 4904 ARGYLERPALTAERFVPdpFGAPGGR---LYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4980

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  900 VVFTYQ---NDKIVCFYLSKD---------NTELKQEaLKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQIP 967
Cdd:PRK12316 4981 VVIAQEgavGKQLVGYVVPQDpaladadeaQAELRDE-LKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDA 5059

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  968 SLLenmQKQYVPPISETEKRLAKTWAEILNLgkYRIGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIAS 1047
Cdd:PRK12316 5060 SLL---QQAYVAPRSELEQQVAAIWAEVLQL--ERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAA 5134

                        1050
                  ....*....|....*
gi 446581728 1048 LSAYIDKLMAVNHDR 1062
Cdd:PRK12316 5135 FVELAAAAGSGDDEK 5149
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 1547-2026 4.20e-133

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 425.57  E-value: 4.20e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEAcriitsnkfkshlnvsdykvsiiediyrttinddVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRN 1706
Cdd:cd17643    81 ADSGP----------------------------------SLLLTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATI-SDLPTVFFNELSTsltkL 1785
Cdd:cd17643   127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVlNQTPSAFYQLVEA----A 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1786 DSEKIR--SLRFIIMGGEAASTNAIRSWQNTFKNQ-VQLVNEYGPTEATVSAMYYfiPVLEGENNLLGSVPIGIPISNTK 1862
Cdd:cd17643   203 DRDGRDplALRYVIFGGEALEAAMLRPWAGRFGLDrPQLVNMYGITETTVHVTFR--PLDAADLPAAAASPIGRPLPGLR 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1863 VHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDnSKRLYRTGDLVRWLPNGNIEFMGRKDKQVK 1942
Cdd:cd17643   281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGP-GSRMYRTGDLARRLPDGELEYLGRADEQVK 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1943 IRGHRIELGEIEDAMLQLEGISQAVVTQTE---GGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPI 2019
Cdd:cd17643   360 IRGFRIELGEIEAALATHPSVRDAAVIVREdepGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPL 439


                  ....*..
gi 446581728 2020 TANGKID 2026
Cdd:cd17643   440 TVNGKLD 446
PRK12467 PRK12467
peptide synthase; Provisional
 48-1052 8.07e-132

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 466.18  E-value: 8.07e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   48 LQIEVLKKALTTIVQSHPALRTIFKKRDEKIK--QLIQKNVEFDIPIKDLTAFKNTEQKsiLKNFLESIVNEKFSLEEGP 125
Cdd:PRK12467 2680 LDVERFRTAWQAVIDRHEILRSGFLWDGELEEplQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADRQQGFDLLSAP 2757

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  126 LFKFHIIKFSEDTFILHLMFHHIIYDGWSLgvfirqlSNTYGELLQ---GKSNVEFESPYKNLVkheeSFIDSAIYKEGS 202
Cdd:PRK12467 2758 LLRLTLVRTGEDRHHLIYTNHHILMDGWSG-------SQLLGEVLQryfGQPPPAREGRYRDYI----AWLQAQDAEASE 2826

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  203 SYWKDYLQGELTPTEF-------PIDFNKMNEKRYtdknisKNINSDLFYQIQCFAKKNNISIYRVMLSTYCTLLHQMTN 275
Cdd:PRK12467 2827 AFWKEQLAALEEPTRLaralypaPAEAVAGHGAHY------LHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTG 2900

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  276 AEEIIVGIPINTRPyTEERNT---FGYFVNTLPIRITIEKGETFKGILNKVnKSIHLAI-TYKHNSYSHIVK--DLNLNT 349
Cdd:PRK12467 2901 QDTVCFGATVAGRP-AQLRGAeqqLGLFINTLPVIASPRAEQTVSDWLQQV-QAQNLALrEFEHTPLADIQRwaGQGGEA 2978

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  350 NTNHNMVYSTAFNTMKIPELKIPDIESTVLTDCKRVN-PFNMTWRImryeGETENkIEVDYNSALYKPESISDLVERYIY 428
Cdd:PRK12467 2979 LFDSILVFENYPISEALKQGAPSGLRFGAVSSREQTNyPLTLAVGL----GDTLE-LEFSYDRQHFDAAAIERLAESFDR 3053

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  429 LLQKLMKNVNEPIHSLDLLLEKDHR-LYKEMNSNALTYPNLKTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQI 507
Cdd:PRK12467 3054 LLQAMLNNPAARLGELPTLAAHERRqVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRL 3133

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  508 VNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKEyrgLVERFAI-- 585
Cdd:PRK12467 3134 AHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAH---LLEQLPApa 3210

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  586 --HTIYLEDFHYANSIENIASTHTI-EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFD 662
Cdd:PRK12467 3211 gdTALTLDRLDLNGYSENNPSTRVMgENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFD 3290

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  663 ASIMEIFPILLCGGRMHlISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMllKLNSVKRLFVGGETLPAES 742
Cdd:PRK12467 3291 GAQERFLWTLICGGCLV-VRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAA 3367

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  743 VRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVA 822
Cdd:PRK12467 3368 FEQVKRKLK-PRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLA 3446

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  823 NGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF 902
Cdd:PRK12467 3447 RGYHQRPSLTAERFVA-DPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVL 3525

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  903 ---TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLelqiPSLLENMQKQYVP 979
Cdd:PRK12467 3526 ardGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL----PDPDAKGSREYVA 3601

                         970       980       990      1000      1010      1020      1030
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446581728  980 PISETEKRLAKTWAEIlnLGKYRIGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIASLSAYI 1052
Cdd:PRK12467 3602 PRSEVEQQLAAIWADV--LGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS 3672
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
12-1053 5.33e-128

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 438.71  E-value: 5.33e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   12 EELDVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIP 91
Cdd:PRK10252    6 QHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   92 -IKDLTAfkNTEQKSILKNFLESIVNEKFSLEEG-PLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGEL 169
Cdd:PRK10252   86 eIIDLRT--QPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  170 LQGKSNVEFE-SPYKNLVKHEESFIDSAIYKEGSSYWKDYLQG-----ELTPTEFPI-----DFNKMnekrytdkniSKN 238
Cdd:PRK10252  164 LRGEPTPASPfTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQlpppaSLSPAPLPGrsasaDILRL----------KLE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  239 INSDLFYQIQCFAKKnnISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKG 318
Cdd:PRK10252  234 FTDGAFRQLAAQASG--VQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  319 ILNKVNKSihLAITYKHNSY--------SHIVKDLNLntntnhnmVYSTAFNTMKIPE-LKIPDIESTVLTDCK-RVNPF 388
Cdd:PRK10252  312 LATRLAAQ--LKKMRRHQRYdaeqivrdSGRAAGDEP--------LFGPVLNIKVFDYqLDFPGVQAQTHTLATgPVNDL 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  389 NMTWRImryEGETENKIEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKDHRLYKEMNSNALTYPnL 468
Cdd:PRK10252  382 ELALFP---DEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIP-E 457

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVP 548
Cdd:PRK10252  458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  549 IDPKFPEKRIEYILKDSESQMIITKKEYRGlveRFAiHTIYLEDFHYAN-----SIENIASTHTiEDAAYIIYTSGSTGL 623
Cdd:PRK10252  538 LDTGYPDDRLKMMLEDARPSLLITTADQLP---RFA-DVPDLTSLCYNAplapqGAAPLQLSQP-HHTAYIIFTSGSTGR 612

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  624 PKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITN 703
Cdd:PRK10252  613 PKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTT 692

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  704 V-VLPT---AFfkLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCATMYEVNGE-- 777
Cdd:PRK10252  693 ThFVPSmlaAF--VASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTG--APLHNLYGPTEAAVDVSWYPAFGEel 768

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  778 IQKEISNIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFIslDKSYNRDKKMYCTGDLVR 857
Cdd:PRK10252  769 AAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFI--ADPFAPGERMYRTGDVAR 846

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  858 LLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVR----DAVVFTYQND------KIVCFYLSKDNTELKQEALK 927
Cdd:PRK10252  847 WLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEqavtHACVINQAAAtggdarQLVGYLVSQSGLPLDTSALQ 926

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  928 TFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELqiPSLleNMQKQYVPPISETEKRLAKTWAEIlnLGKYRIGRDD 1007
Cdd:PRK10252  927 AQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPL--PEL--KAQVPGRAPKTGTETIIAAAFSSL--LGCDVVDADA 1000

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*.
gi 446581728 1008 DFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIASLSAYID 1053
Cdd:PRK10252 1001 DFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLD 1046
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1078-1500 7.35e-127

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 406.74  E-value: 7.35e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1078 YQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHD 1157
Cdd:cd19531     2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1158 EIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRR 1237
Cdd:cd19531    82 DLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1238 NPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVC 1317
Cdd:cd19531   162 PSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRALA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1318 EQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSF 1397
Cdd:cd19531   242 RREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAY 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1398 QNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDILQQHDAYKLQL--LPNKQDISKFDISLAVEEGLDYVGISFEYDI 1475
Cdd:cd19531   322 AHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVepLEVDSGTAKFDLTLSLTETDGGLRGSLEYNT 401

                         410       420
                  ....*....|....*....|....*
gi 446581728 1476 NLFKEESINRFTQNLLNILDAFIHQ 1500
Cdd:cd19531   402 DLFDAATIERMAGHFQTLLEAIVAD 426
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 478-963 4.48e-126

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 407.11  E-value: 4.48e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  478 QALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKR 557
Cdd:cd17651     4 QAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  558 IEYILKDSESQMIITKKEYRGLVERFAIHTIYLEDFHYANSIENiasTHTIE----DAAYIIYTSGSTGLPKGVVVPHKG 633
Cdd:cd17651    84 LAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADA---EPDPAldadDLAYVIYTSGSTGRPKGVVMPHRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  634 VVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKL 713
Cdd:cd17651   161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  714 IADMPKEMLLKLNSVKRLFVGGETLP-AESVRKWQSKL-GLKipVLNAYGPTETTVcATMYEVNGEIQKEISNIPIGKPI 791
Cdd:cd17651   241 LAEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCAGLpGLR--LHNHYGPTETHV-VTALSLPGDPAAWPAPPPIGRPI 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  792 ANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDksYNRDKKMYCTGDLVRLLANGNLEFIGRKD 871
Cdd:cd17651   318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDP--FVPGARMYRTGDLARWLPDGELEFLGRAD 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  872 NQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLE 947
Cdd:cd17651   396 DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRpgekRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLD 475

                         490
                  ....*....|....*.
gi 446581728  948 SFPVSPSGKLDRKKLE 963
Cdd:cd17651   476 ALPLTPNGKLDRRALP 491
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 1547-2031 6.37e-126

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 405.21  E-value: 6.37e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSNkfkshlnvsdykvsiiediyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRN 1706
Cdd:cd17649    81 EDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELSTSLTKLD 1786
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1787 SEKIRSLRFIIMGGEAASTNAIRSWQntfKNQVQLVNEYGPTEATVSAMYYFIPvlEGENNLLGSVPIGIPISNTKVHIL 1866
Cdd:cd17649   208 DGRPPSLRLYIFGGEALSPELLRRWL---KAPVRLFNAYGPTEATVTPLVWKCE--AGAARAGASMPIGRPLGGRSAYIL 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1867 NSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGH 1946
Cdd:cd17649   283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGS-RLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1947 RIELGEIEDAMLQLEGISQAVVT--QTEGGMLLQAYYKTVDGIGIE--KNKLAIHLSNVLPEYMVPKYYSHVLEIPITAN 2022
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVValDGAGGKQLVAYVVLRAAAAQPelRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441


                  ....*....
gi 446581728 2023 GKIDFEKLP 2031
Cdd:cd17649   442 GKLDRKALP 450
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 483-962 1.51e-125

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 404.00  E-value: 1.51e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITkkeyrglverfaihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVI 642
Cdd:cd17643    81 ADSGPSLLLT----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  643 NTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITnvVL---PTAFFKLI--ADM 717
Cdd:cd17643   127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVT--VLnqtPSAFYQLVeaADR 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  718 PKEMLLKLNSVkrlFVGGETLPAESVRKWQSKLGLKIPVL-NAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEV 796
Cdd:cd17643   205 DGRDPLALRYV---IFGGEALEAAMLRPWAGRFGLDRPQLvNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRV 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  797 FVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDKSyNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKI 876
Cdd:cd17643   282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFG-GPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  877 RGYRIELDEIEGTLFKHPEVRDAVVFTYQ----NDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVS 952
Cdd:cd17643   361 RGFRIELGEIEAALATHPSVRDAAVIVREdepgDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLT 440

                         490
                  ....*....|
gi 446581728  953 PSGKLDRKKL 962
Cdd:cd17643   441 VNGKLDRAAL 450
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 1547-2031 1.83e-125

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 404.93  E-value: 1.83e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRN 1706
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELStSLTKLD 1786
Cdd:cd17656   162 EKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIF-SEREFI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1787 SEKIRSLRFIIMGGEAASTNairswqNTF-----KNQVQLVNEYGPTEATVSAMYYFIPvlEGENNLLGsvPIGIPISNT 1861
Cdd:cd17656   241 NRFPTCVKHIITAGEQLVIT------NEFkemlhEHNVHLHNHYGPSETHVVTTYTINP--EAEIPELP--PIGKPISNT 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1862 KVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFseDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQV 1941
Cdd:cd17656   311 WIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF--DPNERMYRTGDLARYLPDGNIEFLGRADHQV 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1942 KIRGHRIELGEIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKTVDGIGIEknKLAIHLSNVLPEYMVPKYYSHVLEIP 2018
Cdd:cd17656   389 KIRGYRIELGEIEAQLLNHPGVSEAVVldkADDKGEKYLCAYFVMEQELNIS--QLREYLAKQLPEYMIPSFFVPLDQLP 466

                         490
                  ....*....|...
gi 446581728 2019 ITANGKIDFEKLP 2031
Cdd:cd17656   467 LTPNGKVDRKALP 479
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1539-2031 1.97e-125

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 403.09  E-value: 1.97e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1539 FYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYP 1618
Cdd:cd17645     4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1619 EDRINYIVRDSEACRIITsnkfkshlnvsdykvsiiediyrttinddvkilnKPDDLAYVIYTSGSTGKPKGTLLTHKGV 1698
Cdd:cd17645    84 GERIAYMLADSSAKILLT----------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNL 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1699 LNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTvffnEL 1778
Cdd:cd17645   130 VNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPT----GA 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1779 STSLTKLDSEkirSLRFIIMGGEAAstnairswQNTFKNQVQLVNEYGPTEATVSAMYYFIPVLEgennllGSVPIGIPI 1858
Cdd:cd17645   206 AEQFMQLDNQ---SLRVLLTGGDKL--------KKIERKGYKLVNNYGPTENTVVATSFEIDKPY------ANIPIGKPI 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1859 SNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEdnSKRLYRTGDLVRWLPNGNIEFMGRKD 1938
Cdd:cd17645   269 DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVP--GERMYRTGDLAKFLPDGNIEFLGRLD 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1939 KQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEknKLAIHLSNVLPEYMVPKYYSHVL 2015
Cdd:cd17645   347 QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLakeDADGRKYLVAYVTAPEEIPHE--ELREWLKNDLPDYMIPTYFVHLK 424

                         490
                  ....*....|....*.
gi 446581728 2016 EIPITANGKIDFEKLP 2031
Cdd:cd17645   425 ALPLTANGKVDRKALP 440
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 470-962 2.05e-125

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 404.12  E-value: 2.05e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  470 TLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPI 549
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  550 DPKFPEKRIEYILKDSESQMIITKKEyrglverfaihtiyledfhyansieniasthtieDAAYIIYTSGSTGLPKGVVV 629
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLLTQPE----------------------------------NLAYVIYTSGSTGKPKGVMI 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  630 PHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTA 709
Cdd:cd17644   127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  710 FFK-LIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKIPVLNAYGPTETTVCATMYEVNGEIQKEISNIPIG 788
Cdd:cd17644   207 YWHlLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVPIG 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  789 KPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDKSYNRDKKMYCTGDLVRLLANGNLEFIG 868
Cdd:cd17644   287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPDGNIEYLG 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  869 RKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQ---NDK-IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIF 944
Cdd:cd17644   367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREdqpGNKrLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFV 446

                         490
                  ....*....|....*...
gi 446581728  945 HLESFPVSPSGKLDRKKL 962
Cdd:cd17644   447 VLEELPLTPNGKIDRRAL 464
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 483-962 4.50e-125

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 403.60  E-value: 4.50e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITKKE----YRGLVERFAIHTIYLedfhyANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLS 638
Cdd:cd12116    81 EDAEPALVLTDDAlpdrLPAGLPVLLLALAAA-----AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  639 YSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMP 718
Cdd:cd12116   156 HSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  719 KEmllKLNSVkRLFVGGETLPAESVRKWQSKLGlkiPVLNAYGPTETTVCATMYEVNGeiqkEISNIPIGKPIANSEVFV 798
Cdd:cd12116   236 WQ---GRAGL-TALCGGEALPPDLAARLLSRVG---SLWNLYGPTETTIWSTAARVTA----AAGPIPIGRPLANTQVYV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  799 ISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRG 878
Cdd:cd12116   305 LDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVP-DPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRG 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  879 YRIELDEIEGTLFKHPEVRDAVVFTYQND---KIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSG 955
Cdd:cd12116   384 HRIELGEIEAALAAHPGVAQAAVVVREDGgdrRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANG 463


                  ....*..
gi 446581728  956 KLDRKKL 962
Cdd:cd12116   464 KLDRKAL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 483-962 4.86e-125

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 402.02  E-value: 4.86e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITkkeyrglverfaihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVI 642
Cdd:cd17652    81 ADARPALLLT----------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  643 NTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAffkLIADMPKEML 722
Cdd:cd17652   127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPA---ALAALPPDDL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  723 LKLNSvkrLFVGGETLPAESVRKWQSklGLKipVLNAYGPTETTVCATMYEVNGEIQkeisNIPIGKPIANSEVFVISPF 802
Cdd:cd17652   204 PDLRT---LVVAGEACPAELVDRWAP--GRR--MINAYGPTETTVCATMAGPLPGGG----VPPIGRPVPGTRVYVLDAR 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  803 NTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFIsLDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIE 882
Cdd:cd17652   273 LRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFV-ADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIE 351

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  883 LDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:cd17652   352 LGEVEAALTEHPGVAEAVVVVRDDRpgdkRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLD 431


                  ....
gi 446581728  959 RKKL 962
Cdd:cd17652   432 RRAL 435
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1535-2030 5.26e-123

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 398.07  E-value: 5.26e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1535 IQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPID 1614
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1615 VKYPEDRINYIVRDSEACRIITSnkfkshlnvsdykvsiiediyrttinddvkilnKPDDLAYVIYTSGSTGKPKGTLLT 1694
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTS---------------------------------SPSDAAYVIFTSGSTGKPKGVVIE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1695 HKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVeyAQAIQETQATISDL-PTV 1773
Cdd:cd05918   128 HRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDL--AGFINRLRVTWAFLtPSV 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1774 FfnelstSLtkLDSEKIRSLRFIIMGGEAASTNAIRSWQntfkNQVQLVNEYGPTEATVSAMyYFIPVLEGENNLLGSvP 1853
Cdd:cd05918   206 A------RL--LDPEDVPSLRTLVLGGEALTQSDVDTWA----DRVRLINAYGPAECTIAAT-VSPVVPSTDPRNIGR-P 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1854 IGipiSNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNP-----FSEDNSKRLYRTGDLVRWLPN 1928
Cdd:cd05918   272 LG---ATCWVVDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqEGSGRGRRLYRTGDLVRYNPD 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1929 GNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQ-------TEGGML---LQAYYKTVDGIGIEKNKLAI-- 1996
Cdd:cd05918   349 GSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkpkdgSSSPQLvafVVLDGSSSGSGDGDSLFLEPsd 428

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 446581728 1997 -----------HLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKL 2030
Cdd:cd05918   429 efralvaelrsKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 1547-2030 6.69e-122

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 394.35  E-value: 6.69e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSNKFKSHLNVSDYKVSI-IEDIYRTTINDDVKILnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWR 1705
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLaLAAAAAAPAAPRTPVS--PDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1706 NEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQE-----TQATisdlPTVFfnelsT 1780
Cdd:cd12116   159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAhsitvMQAT----PATW-----R 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1781 SLTKLDSEKIRSLRfIIMGGEAASTNAIRSWQNTFKnqvQLVNEYGPTEATV--SAMyyfiPVLEGennlLGSVPIGIPI 1858
Cdd:cd12116   230 MLLDAGWQGRAGLT-ALCGGEALPPDLAARLLSRVG---SLWNLYGPTETTIwsTAA----RVTAA----AGPIPIGRPL 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1859 SNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkRLYRTGDLVRWLPNGNIEFMGRKD 1938
Cdd:cd12116   298 ANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGS-RLYRTGDLVRRRADGRLEYLGRAD 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1939 KQVKIRGHRIELGEIEDAMLQLEGISQAVVT--QTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLE 2016
Cdd:cd12116   377 GQVKIRGHRIELGEIEAALAAHPGVAQAAVVvrEDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDA 456

                         490
                  ....*....|....
gi 446581728 2017 IPITANGKIDFEKL 2030
Cdd:cd12116   457 LPLTANGKLDRKAL 470
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 1542-2026 9.53e-122

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 394.72  E-value: 9.53e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1542 QVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDR 1621
Cdd:cd17646     7 QAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1622 INYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNL 1701
Cdd:cd17646    87 LAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1702 VEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEqRYSTVEY-AQAIQETQATisdlpTVFF--NEL 1778
Cdd:cd17646   167 LLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPG-GHRDPAYlAALIREHGVT-----TCHFvpSML 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1779 STSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFknQVQLVNEYGPTEATVSAMYYfiPVLEGENNllGSVPIGIPI 1858
Cdd:cd17646   241 RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALP--GAELHNLYGPTEAAIDVTHW--PVRGPAET--PSVPIGRPV 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1859 SNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFseDNSKRLYRTGDLVRWLPNGNIEFMGRKD 1938
Cdd:cd17646   315 PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF--GPGSRMYRTGDLARWRPDGALEFLGRSD 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1939 KQVKIRGHRIELGEIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKTVDG-IGIEKNKLAIHLSNVLPEYMVPKYYSHV 2014
Cdd:cd17646   393 DQVKIRGFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPAAGaAGPDTAALRAHLAERLPEYMVPAAFVVL 472

                         490
                  ....*....|..
gi 446581728 2015 LEIPITANGKID 2026
Cdd:cd17646   473 DALPLTANGKLD 484
PRK05691 PRK05691
peptide synthase; Validated
 1040-2128 1.43e-121

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 433.06  E-value: 1.43e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1040 FEHTTIASL-SAYIDKLMAVNHDREEQEMQVLKVADKESYQLSSAQkriwfLNKY----NAINRVYD-TP------LHIY 1107
Cdd:PRK05691 3198 YDEQTIAELaEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQ-----LDALpvpaAEIEDVYPlTPmqegllLHTL 3272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1108 IEPSLNKDILQDTIRF---------------LVERHEMLRTVFIERNGEPR-QVILNSIAIDLIHDEIEHMSKKEQQEYI 1171
Cdd:PRK05691 3273 LEPGTGLYYMQDRYRInsaldperfaqawqaVVARHEALRASFSWNAGETMlQVIHKPGRTPIDYLDWRGLPEDGQEQRL 3352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1172 RTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTiSNRYVDY 1251
Cdd:PRK05691 3353 QALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPV-PPRYRDY 3431

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1252 AEWEQVQ-LNLGRwdtekSYWMAELA---APLPIlnlPLD--FSRNRQSTNKGTVFE---MKLDNEMKESLKQVCEQENI 1322
Cdd:PRK05691 3432 IGWLQRQdLAQAR-----QWWQDNLRgfeRPTPI---PSDrpFLREHAGDSGGMVVGdcyTRLDAADGARLRELAQAHQL 3503

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1323 SMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGR--NHQEFEKIQGFFVNTLAIRTQLNDV---KNLTQLLQVVREKCLNSF 1397
Cdd:PRK05691 3504 TVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVQLPAAgqrCSVRQWLQGLLDSNMELR 3583

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1398 QNQSYPFdkVIEQINPDRSFGNnPIFSTMFSYQKDILQQHDAYKLQLLPNKQDISK----FDISLAVEEGlDYVGISFEY 1473
Cdd:PRK05691 3584 EYEYLPL--VAIQECSELPKGQ-PLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRthtnFPLTAVCYPG-DDLGLHLSY 3659

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1474 DINLFKEESINR----FTQNLLNILDAFIHQrtvtYENLSFLS-QEEESLYKKVNHTERPYPYFQNIQEQFYMQVDRQPE 1548
Cdd:PRK05691 3660 DQRYFDAPTVERllgeFKRLLLALVQGFHGD----LSELPLLGeQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQ 3735

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1549 RIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRD 1628
Cdd:PRK05691 3736 RIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIEL 3815

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1629 S--------EACRIITSNKFKSHLNVSDYKVSIIEDIYRTTIND-DVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVL 1699
Cdd:PRK05691 3816 SrtpvlvcsAACREQARALLDELGCANRPRLLVWEEVQAGEVAShNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGML 3895

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1700 NLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATIsdLPTVffNELS 1779
Cdd:PRK05691 3896 NNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITV--LESV--PSLI 3971

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1780 TSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKnQVQLVNEYGPTEATVSAMYYFIPVLEGENNLLgsvPIGIPIS 1859
Cdd:PRK05691 3972 QGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYP-QIGLVNAYGPAECSDDVAFFRVDLASTRGSYL---PIGSPTD 4047

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1860 NTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDnSKRLYRTGDLVRWLPNGNIEFMGRKDK 1939
Cdd:PRK05691 4048 NNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAP-GERLYRTGDLARRRSDGVLEYVGRIDH 4126

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1940 QVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEG--GMLLQAYYKTVDGI---GIEKNKLAIHLSNVLPEYMVPKYYSHV 2014
Cdd:PRK05691 4127 QVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGvnGKHLVGYLVPHQTVlaqGALLERIKQRLRAELPDYMVPLHWLWL 4206

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2015 LEIPITANGKIDFEKLPKIEFGHEQKDEcKLKPQTKVQKDIAKVWSEVLNVKSIGLKDDFFNLGGHSLKVMPALVKL-KP 2093
Cdd:PRK05691 4207 DRLPLNANGKLDRKALPALDIGQLQSQA-YLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVqKA 4285

                        1130      1140      1150
                  ....*....|....*....|....*....|....*
gi 446581728 2094 LYPNLKIQDFFKYRTIEKLASHIEEMEDMSFKKEK 2128
Cdd:PRK05691 4286 LQRNVPLRAMFECSTVEELAEYIEGLAGSAIDEQK 4320
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1271-2480 5.24e-121

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 419.47  E-value: 5.24e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1271 WMAELAAPlPILNLPLDFSRNRQSTNKGTVFEMKLdnemkeSLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTp 1350
Cdd:TIGR03443    2 WSERLDNP-TLSVLPHDYLRPANNRLVEATYSLQL------PSAEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1351 vvgrnhqEFEKIQGFFVntlaIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVIEQINPDRSFGNNPIFsTMFSYQ 1430
Cdd:TIGR03443   74 -------SSNKSGRPFV----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPL-FRLAFQ 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1431 KDILQQHDAYklqllpNKQDISkfDISLAVEEGLDYVGISFEYDINLFKEESINRFTQNLLNILDAFIHQRTVTYENLSF 1510
Cdd:TIGR03443  142 DAPDNQQTTY------STGSTT--DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSL 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1511 LSQEEESLYkkvnhterPYP--------YFQNIQEQFYMQVDRQPER---------IAIATATESLTYRQLNMSSNQVAQ 1573
Cdd:TIGR03443  214 ITPSQKSLL--------PDPtkdldwsgFRGAIHDIFADNAEKHPDRtcvvetpsfLDPSSKTRSFTYKQINEASNILAH 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1574 HLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRIN-YI-VRDSEACRIITSNKFKSHLnVSDY-- 1649
Cdd:TIGR03443  286 YLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTiYLsVAKPRALIVIEKAGTLDQL-VRDYid 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1650 -KVSIIEDIYRTTINDD------------VKILNK--------------PDDLAYVIYTSGSTGKPKGTLLTHKGVLNLV 1702
Cdd:TIGR03443  365 kELELRTEIPALALQDDgslvggsleggeTDVLAPyqalkdtptgvvvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYF 444

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1703 EWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLpTVFFNELstsL 1782
Cdd:TIGR03443  445 PWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHL-TPAMGQL---L 520

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1783 TKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYFIPVLEGENNLLGS----VPIGIPI 1858
Cdd:TIGR03443  521 SAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAEN-VCIVNMYGTTETQRAVSYFEIPSRSSDSTFLKNlkdvMPAGKGM 599

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1859 SNTKVHILNSY--MQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPF---------SEDNSK-----------RL 1916
Cdd:TIGR03443  600 KNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidlDKENNKperefwlgprdRL 679

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1917 YRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEI-----------EDAML----------------------QLEGI 1963
Cdd:TIGR03443  680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIdthlsqhplvrENVTLvrrdkdeeptlvsyivpqdksdELEEF 759

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1964 SQAVVTQTEGGML---LQAYYKTVDGIgieKNklaiHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLP--------- 2031
Cdd:TIGR03443  760 KSEVDDEESSDPVvkgLIKYRKLIKDI---RE----YLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPfpdtaqlaa 832

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2032 KIEFGHEQKDECKLkpqTKVQKDIAKVWSEVLNVK--SIGLKDDFFNLGGHSLKVMPALVKL-KPLYPNLKIQDFFKYRT 2108
Cdd:TIGR03443  833 VAKNRSASAADEEF---TETEREIRDLWLELLPNRpaTISPDDSFFDLGGHSILATRMIFELrKKLNVELPLGLIFKSPT 909

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2109 IEKLASHIEEMEDMSfKKEKNMNVACMENETKTTPVY--ETTKLEKCELE--------MVNYPKTVFLTGATGYLGAHIL 2178
Cdd:TIGR03443  910 IKGFAKEVDRLKKGE-ELADEGDSEIEEEETVLELDYakDAKTLVDSLPKsypsrkelDASTPITVFLTGATGFLGSFIL 988

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2179 ERLL---QLPSTTIYCLVRENEDQVIGAKLKERMEFY-FGKEilqKLKERVELIEGDLSLMNLGLDSKQLDHLKKNVESI 2254
Cdd:TIGR03443  989 RDLLtrrSNSNFKVFAHVRAKSEEAGLERLRKTGTTYgIWDE---EWASRIEVVLGDLSKEKFGLSDEKWSDLTNEVDVI 1065

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2255 IHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSVVGqaerdpKEFEFFESD--FDRGQN-------- 2323
Cdd:TIGR03443 1066 IHNGALVHWVYPYSKLRDANVIGTINVLNLCAEGKAKqFSFVSSTSALD------TEYYVNLSDelVQAGGAgipesddl 1139

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2324 ------LDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGkfqyNINENAF-YRLLKG-ICLSSIaPDVNTYV 2395
Cdd:TIGR03443 1140 mgsskgLGTGYGQSKWVAEYIIREAGKRGLRGCIVRPGYVTGDSKTG----ATNTDDFlLRMLKGcIQLGLI-PNINNTV 1214

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2396 DLTPVDYGS--LAITELSYKANTVNKTMHICNPNQLKWDQFINSLQAFGYDIllmKQEKY------IEKFFNtnlTTDEQ 2467
Cdd:TIGR03443 1215 NMVPVDHVArvVVAAALNPPKESELAVAHVTGHPRIRFNDFLGTLKTYGYDV---EIVDYvhwrksLERFVI---ERSED 1288

                         1370
                   ....*....|...
gi 446581728  2468 KALeliMPLLESV 2480
Cdd:TIGR03443 1289 NAL---FPLLHFV 1298
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 482-962 4.20e-120

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 389.53  E-value: 4.20e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  482 SPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYI 561
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  562 LKDSESQMIITKKEYRGLVERFAIHTIYLEDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNL---- 637
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLlhfe 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  638 -SYSVINTFhlgkeDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIAD 716
Cdd:cd17656   161 rEKTNINFS-----DKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  717 MPKEMLLKLNSVKRLFVGGETL--PAESVRKWQSKlglKIPVLNAYGPTETTVcATMYEVNGEIqkEISNI-PIGKPIAN 793
Cdd:cd17656   236 EREFINRFPTCVKHIITAGEQLviTNEFKEMLHEH---NVHLHNHYGPSETHV-VTTYTINPEA--EIPELpPIGKPISN 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  794 SEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQ 873
Cdd:cd17656   310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFP--DPFDPNERMYRTGDLARYLPDGNIEFLGRADHQ 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  874 VKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND---KIVCFYLSKDNTeLKQEALKTFLSESLPDFMMPNYIFHLESFP 950
Cdd:cd17656   388 VKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDkgeKYLCAYFVMEQE-LNISQLREYLAKQLPEYMIPSFFVPLDQLP 466

                         490
                  ....*....|..
gi 446581728  951 VSPSGKLDRKKL 962
Cdd:cd17656   467 LTPNGKVDRKAL 478
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1539-2030 4.07e-119

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 384.74  E-value: 4.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1539 FYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYP 1618
Cdd:cd17653     3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1619 EDRINYIVRDSEACRIITsnkfkshlnvsdykvsiiediyrttinddvkiLNKPDDLAYVIYTSGSTGKPKGTLLTHKGV 1698
Cdd:cd17653    83 SARIQAILRTSGATLLLT--------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHRGV 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1699 LNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVeyAQAIQETQATisdlPTVffnel 1778
Cdd:cd17653   131 LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHV--ARTVDALMST----PSI----- 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1779 stsLTKLDSEKIRSLRFIIMGGEAASTNAIRSWqntfKNQVQLVNEYGPTEATVSAmyyFIPVLEGENNllgsVPIGIPI 1858
Cdd:cd17653   200 ---LSTLSPQDFPNLKTIFLGGEAVPPSLLDRW----SPGRRLYNAYGPTECTISS---TMTELLPGQP----VTIGKPI 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1859 SNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFseDNSKRLYRTGDLVRWLPNGNIEFMGRKD 1938
Cdd:cd17653   266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF--WPGSRMYRTGDYGRWTEDGGLEFLGRED 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1939 KQVKIRGHRIELGEIEDAMLQLEG-ISQAVVTQTEGgmLLQAYY--KTVDGIGIEKnklaiHLSNVLPEYMVPKYYSHVL 2015
Cdd:cd17653   344 NQVKVRGFRINLEEIEEVVLQSQPeVTQAAAIVVNG--RLVAFVtpETVDVDGLRS-----ELAKHLPSYAVPDRIIALD 416

                         490
                  ....*....|....*
gi 446581728 2016 EIPITANGKIDFEKL 2030
Cdd:cd17653   417 SFPLTANGKVDRKAL 431
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 473-969 5.55e-119

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 386.13  E-value: 5.55e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  473 QLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPK 552
Cdd:cd05918     3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  553 FPEKRIEYILKDSESQMIITkkeyrglverfaihtiyledfhyansieniastHTIEDAAYIIYTSGSTGLPKGVVVPHK 632
Cdd:cd05918    83 HPLQRLQEILQDTGAKVVLT---------------------------------SSPSDAAYVIFTSGSTGKPKGVVIEHR 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  633 GVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSA-EEFINvsqKYGITNVVLPTAFF 711
Cdd:cd05918   130 ALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDlAGFIN---RLRVTWAFLTPSVA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  712 KLIAdmPKEmllkLNSVKRLFVGGETLPAESVRKWQSKLGLkipvLNAYGPTETTVCATMYEVNGEiqKEISNipIGKPI 791
Cdd:cd05918   207 RLLD--PED----VPSLRTLVLGGEALTQSDVDTWADRVRL----INAYGPAECTIAATVSPVVPS--TDPRN--IGRPL 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  792 ANSeVFVISPFNT--LCPSGVVGELFIGGDGVANGYLNQKEKTEGAFIS-----LDKSYNRDKKMYCTGDLVRLLANGNL 864
Cdd:cd05918   273 GAT-CWVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEdpawlKQEGSGRGRRLYRTGDLVRYNPDGSL 351

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  865 EFIGRKDNQVKIRGYRIELDEIEGTLFKH-PEVRDAVVFTYQN------DKIVCFyLSKDNTELKQ-------------- 923
Cdd:cd05918   352 EYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPkdgsssPQLVAF-VVLDGSSSGSgdgdslflepsdef 430

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 446581728  924 ----EALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQIPSL 969
Cdd:cd05918   431 ralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 483-962 4.50e-118

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 382.49  E-value: 4.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITkkeyrglverfaihtiyledfhyansieniastHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVI 642
Cdd:cd17649    81 EDSGAGLLLT---------------------------------HHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  643 NTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAF-FKLIADMPKEM 721
Cdd:cd17649   128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYlQQLAEEADRTG 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  722 LLKLNSVKRLFVGGETLPAESVRKWQsklglKIPV--LNAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEVFVI 799
Cdd:cd17649   208 DGRPPSLRLYIFGGEALSPELLRRWL-----KAPVrlFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYIL 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  800 SPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGY 879
Cdd:cd17649   283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVP-DPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  880 RIELDEIEGTLFKHPEVRDAVVFTYQND---KIVCFYLSKDNTELKQ--EALKTFLSESLPDFMMPNYIFHLESFPVSPS 954
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVVALDGAggkQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441


                  ....*...
gi 446581728  955 GKLDRKKL 962
Cdd:cd17649   442 GKLDRKAL 449
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 1547-2026 3.29e-117

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 381.23  E-value: 3.29e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITsNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRN 1706
Cdd:cd12114    81 ADAGARLVLT-DGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATI-SDLPTVFfnELSTSLTKL 1785
Cdd:cd12114   160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLwNSVPALL--EMLLDVLEA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1786 DSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYFI-PVLEGennlLGSVPIGIPISNTKVH 1864
Cdd:cd12114   238 AQALLPSLRLVLLSGDWIPLDLPARLRALAPD-ARLISLGGATEASIWSIYHPIdEVPPD----WRSIPYGRPLANQRYR 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1865 ILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEdnskRLYRTGDLVRWLPNGNIEFMGRKDKQVKIR 1944
Cdd:cd12114   313 VLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPDGE----RLYRTGDLGRYRPDGTLEFLGRRDGQVKVR 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1945 GHRIELGEIEDAMLQLEGISQAVVT--QTEGGMLLQAYYKTV-DGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITA 2021
Cdd:cd12114   389 GYRIELGEIEAALQAHPGVARAVVVvlGDPGGKRLAAFVVPDnDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTA 468


                  ....*
gi 446581728 2022 NGKID 2026
Cdd:cd12114   469 NGKVD 473
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 473-962 3.41e-116

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 376.51  E-value: 3.41e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  473 QLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPK 552
Cdd:cd17645     2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  553 FPEKRIEYILKDSESQMIITKKEyrglverfaihtiyledfhyansieniasthtieDAAYIIYTSGSTGLPKGVVVPHK 632
Cdd:cd17645    82 YPGERIAYMLADSSAKILLTNPD----------------------------------DLAYVIYTSGSTGLPKGVMIEHH 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  633 GVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFK 712
Cdd:cd17645   128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAE 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  713 liadmpKEMLLKLNSVKRLFVGGETLPAESVRKWQsklglkipVLNAYGPTETTVCATMYevngEIQKEISNIPIGKPIA 792
Cdd:cd17645   208 ------QFMQLDNQSLRVLLTGGDKLKKIERKGYK--------LVNNYGPTENTVVATSF----EIDKPYANIPIGKPID 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  793 NSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDN 872
Cdd:cd17645   270 NTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIV--HPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQ 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  873 QVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN---DKIVCFYLSKDnTELKQEALKTFLSESLPDFMMPNYIFHLESF 949
Cdd:cd17645   348 QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDadgRKYLVAYVTAP-EEIPHEELREWLKNDLPDYMIPTYFVHLKAL 426

                         490
                  ....*....|...
gi 446581728  950 PVSPSGKLDRKKL 962
Cdd:cd17645   427 PLTANGKVDRKAL 439
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1535-2030 4.13e-116

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 376.66  E-value: 4.13e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1535 IQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPID 1614
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1615 VKYPEDRINYIVRDSeACRIItsnkfkshlnvsdykvsiiediyrttinddvkiLNKPDDLAYVIYTSGSTGKPKGTLLT 1694
Cdd:cd12115    81 PAYPPERLRFILEDA-QARLV---------------------------------LTDPDDLAYVIYTSGSTGRPKGVAIE 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1695 HKGVLNLVEWRNEVFqisPNDKVTQFY---SHSFDSSVSEIFSTLLNGAELYLLSDEQrySTVEYAQAIQETqaTISDLP 1771
Cdd:cd12115   127 HRNAAAFLQWAAAAF---SAEELAGVLastSICFDLSVFELFGPLATGGKVVLADNVL--ALPDLPAAAEVT--LINTVP 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1772 TVFfNELstsltkLDSEKI-RSLRFIIMGGEAASTNAIRSWQNTfKNQVQLVNEYGPTEATVSAMYYFIPvlegeNNLLG 1850
Cdd:cd12115   200 SAA-AEL------LRHDALpASVRVVNLAGEPLPRDLVQRLYAR-LQVERVVNLYGPSEDTTYSTVAPVP-----PGASG 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1851 SVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDnsKRLYRTGDLVRWLPNGN 1930
Cdd:cd12115   267 EVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPG--ARLYRTGDLVRWRPDGL 344

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1931 IEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGML---LQAYYKTVDGIGIEKNKLAIHLSNVLPEYMV 2007
Cdd:cd12115   345 LEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGerrLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMV 424

                         490       500
                  ....*....|....*....|...
gi 446581728 2008 PKYYSHVLEIPITANGKIDFEKL 2030
Cdd:cd12115   425 PSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 1547-2031 6.15e-113

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 367.88  E-value: 6.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDK-VAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYI 1625
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1626 VRDSEACRIITSnkfkshlnvsdykvsiiediyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNL-VEW 1704
Cdd:cd17648    81 LEDTGARVVITN----------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLrTSL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1705 RNEVFQISPNDKVTQFYS-HSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQAT-ISDLPTVffnelstsL 1782
Cdd:cd17648   127 SERYFGRDNGDEAVLFFSnYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTyLSGTPSV--------L 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1783 TKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVqlVNEYGPTEATVSAMYYFIPVLEGENNllgsvPIGIPISNTK 1862
Cdd:cd17648   199 QQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLI--INAYGPTETTVTNHKRFFPGDQRFDK-----SLGRPVRNTK 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1863 VHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSK------RLYRTGDLVRWLPNGNIEFMGR 1936
Cdd:cd17648   272 CYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQERargrnaRLYKTGDLVRWLPSGELEYLGR 351

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1937 KDKQVKIRGHRIELGEIEDAMLQLEGISQAVV--------TQTEGGMLLQAYYKTVDGiGIEKNKLAIHLSNVLPEYMVP 2008
Cdd:cd17648   352 NDFQVKIRGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPG-HVPESDLLSFLRAKLPRYMVP 430

                         490       500
                  ....*....|....*....|...
gi 446581728 2009 KYYSHVLEIPITANGKIDFEKLP 2031
Cdd:cd17648   431 ARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 471-962 3.67e-111

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 362.41  E-value: 3.67e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  471 LDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPID 550
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  551 PKFPEKRIEYILKDSESQMIITkkeyrglverfaihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVP 630
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLT----------------------------------DPDDLAYVIYTSGSTGRPKGVAIE 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  631 HKGVVNLSYSVINTFhlGKEDV--FLQFATIIFDASIMEIFPILLCGGRMHLISeiekrSAEEFINVSQKYGIT--NVVl 706
Cdd:cd12115   127 HRNAAAFLQWAAAAF--SAEELagVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTliNTV- 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  707 PTAFfkliadmpkEMLLKLN----SVKRLFVGGETLPAESVRKWQSKLGLKIpVLNAYGPTETTVCATMYEVNGEIQKEI 782
Cdd:cd12115   199 PSAA---------AELLRHDalpaSVRVVNLAGEPLPRDLVQRLYARLQVER-VVNLYGPSEDTTYSTVAPVPPGASGEV 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  783 SnipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldKSYNRDKKMYCTGDLVRLLANG 862
Cdd:cd12115   269 S---IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLP--DPFGPGARLYRTGDLVRWRPDG 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  863 NLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFM 938
Cdd:cd12115   344 LLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYM 423

                         490       500
                  ....*....|....*....|....
gi 446581728  939 MPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd12115   424 VPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 473-963 1.69e-110

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 360.09  E-value: 1.69e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  473 QLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPK 552
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  553 FPEKRIEYILKDSESQMIITkkeyrglverfaihtiyledfhyansieniasTHTIEDAAYIIYTSGSTGLPKGVVVPHK 632
Cdd:cd17653    81 LPSARIQAILRTSGATLLLT--------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHR 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  633 GVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLiseieKRSAEEFINVSQKYGITNVVlPTAFFK 712
Cdd:cd17653   129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL-----ADPSDPFAHVARTVDALMST-PSILST 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  713 L-IADMPkemllklnSVKRLFVGGETLPAESVRKWqsklGLKIPVLNAYGPTETTVCATMYEVngeiqKEISNIPIGKPI 791
Cdd:cd17653   203 LsPQDFP--------NLKTIFLGGEAVPPSLLDRW----SPGRRLYNAYGPTECTISSTMTEL-----LPGQPVTIGKPI 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  792 ANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldKSYNRDKKMYCTGDLVRLLANGNLEFIGRKD 871
Cdd:cd17653   266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVP--DPFWPGSRMYRTGDYGRWTEDGGLEFLGRED 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  872 NQVKIRGYRIELDEIEGTLFK-HPEVRDAVVFTYqNDKIVCFYLSKDnteLKQEALKTFLSESLPDFMMPNYIFHLESFP 950
Cdd:cd17653   344 NQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIVV-NGRLVAFVTPET---VDVDGLRSELAKHLPSYAVPDRIIALDSFP 419

                         490
                  ....*....|...
gi 446581728  951 VSPSGKLDRKKLE 963
Cdd:cd17653   420 LTANGKVDRKALR 432
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 474-962 8.37e-110

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 360.05  E-value: 8.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  474 LIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKF 553
Cdd:cd17646     3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  554 PEKRIEYILKDSESQMIITKkeyRGLVERFA----IHTIYLEDFHYANSIENIASTHTiEDAAYIIYTSGSTGLPKGVVV 629
Cdd:cd17646    83 PADRLAYMLADAGPAVVLTT---ADLAARLPaggdVALLGDEALAAPPATPPLVPPRP-DNLAYVIYTSGSTGRPKGVMV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  630 PHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNV-VLPT 708
Cdd:cd17646   159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTChFVPS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  709 AFFKLIADMPKEmllKLNSVKRLFVGGETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCATMYEVNGEiqKEISNIPIG 788
Cdd:cd17646   239 MLRVFLAEPAAG---SCASLRRVFCSGEALPPELAARFLALPG--AELHNLYGPTEAAIDVTHWPVRGP--AETPSVPIG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  789 KPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFIslDKSYNRDKKMYCTGDLVRLLANGNLEFIG 868
Cdd:cd17646   312 RPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFV--PDPFGPGSRMYRTGDLARWRPDGALEFLG 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  869 RKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN---DKIVCFYL--SKDNTELKQEALKTFLSESLPDFMMPNYI 943
Cdd:cd17646   390 RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApagAARLVGYVvpAAGAAGPDTAALRAHLAERLPEYMVPAAF 469

                         490
                  ....*....|....*....
gi 446581728  944 FHLESFPVSPSGKLDRKKL 962
Cdd:cd17646   470 VVLDALPLTANGKLDRAAL 488
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 1547-2030 8.61e-110

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 358.32  E-value: 8.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEAcriitsnkfkshlnvsdyKVSIIEdiyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLV-EWR 1705
Cdd:cd17650    81 EDSGA------------------KLLLTQ----------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAhAWR 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1706 NEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISD-LPTVffneLSTSLTK 1784
Cdd:cd17650   127 REYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMEsTPAL----IRPVMAY 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1785 LDSEKIR--SLRFIIMGGEAASTNAIRSWQNTFKNQVQLVNEYGPTEATVSAMYYfipvLEGENNLLGS--VPIGIPISN 1860
Cdd:cd17650   203 VYRNGLDlsAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYY----EEGRDPLGDSanVPIGRPLPN 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1861 TKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEdnSKRLYRTGDLVRWLPNGNIEFMGRKDKQ 1940
Cdd:cd17650   279 TAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAP--GERMYRTGDLARWRADGNVELLGRVDHQ 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1941 VKIRGHRIELGEIEDAMLQLEGISQAVVTQTE---GGMLLQAYykTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEI 2017
Cdd:cd17650   357 VKIRGFRIELGEIESQLARHPAIDEAVVAVREdkgGEARLCAY--VVAAATLNTAELRAFLAKELPSYMIPSYYVQLDAL 434

                         490
                  ....*....|...
gi 446581728 2018 PITANGKIDFEKL 2030
Cdd:cd17650   435 PLTPNGKVDRRAL 447
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 471-962 7.39e-108

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 352.96  E-value: 7.39e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  471 LDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPID 550
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  551 PKFPEKRIEYILKDSESQMIITkkeyrglverfaihtiyledfhyansieniasthtiedaAYIIYTSGSTGLPKGVVVP 630
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  631 HKGVVNLSYSVINTFHLGKEDVFLQFATIIFDAS-IMEIFPILLCGGRMHLIseiEKRSAEEFINVSQKYGITNVVLPTA 709
Cdd:COG0318   122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGVPT 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  710 FFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCATMYEVNGEIQKEISnipIGK 789
Cdd:COG0318   199 MLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPGERRPGS---VGR 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  790 PIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKkMYCTGDLVRLLANGNLEFIGR 869
Cdd:COG0318   274 PLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--------RDG-WLRTGDLGRLDEDGYLYIVGR 344

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  870 KDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFH 945
Cdd:COG0318   345 KKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKwgerVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEF 424

                         490
                  ....*....|....*..
gi 446581728  946 LESFPVSPSGKLDRKKL 962
Cdd:COG0318   425 VDELPRTASGKIDRRAL 441
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 483-962 2.23e-106

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 348.69  E-value: 2.23e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITKKEyrglverfaihtiyledfhyansieniasthtieDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVI 642
Cdd:cd17650    81 EDSGAKLLLTQPE----------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWR 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  643 NTFHLGKEDV-FLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEM 721
Cdd:cd17650   127 REYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  722 LLKLNSVKRLFVGGETLPAESVRKWQSKLGLKIPVLNAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEVFVISP 801
Cdd:cd17650   207 GLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDE 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  802 FNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisLDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRI 881
Cdd:cd17650   287 RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERF--VENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  882 ELDEIEGTLFKHPEVRDAVVFTYQND---KIVCFYLSKDNTeLKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:cd17650   365 ELGEIESQLARHPAIDEAVVAVREDKggeARLCAYVVAAAT-LNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443


                  ....
gi 446581728  959 RKKL 962
Cdd:cd17650   444 RRAL 447
PRK05691 PRK05691
peptide synthase; Validated
 48-1064 5.72e-105

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 378.74  E-value: 5.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   48 LQIEVLKKALTTIVQSHPALRTIFK-KRDEKIKQLIQKNVEFDIPIKDLTAFKNTEQKSILKNFLESIVNEKFSLEEGPL 126
Cdd:PRK05691 3292 LDPERFAQAWQAVVARHEALRASFSwNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPP 3371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  127 FKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKsNVEFESP--YKNLVkheeSFIDSAIYKEGSSY 204
Cdd:PRK05691 3372 FHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGR-EAQLPVPprYRDYI----GWLQRQDLAQARQW 3446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  205 WKDYLQGELTPTEFPIDFNKMNEK-----------RYTDKNISKNInsdlfyQIQCFAKKNNISIYRVMLSTYCTLLHQM 273
Cdd:PRK05691 3447 WQDNLRGFERPTPIPSDRPFLREHagdsggmvvgdCYTRLDAADGA------RLRELAQAHQLTVNTFAQAAWALVLRRY 3520

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  274 TNAEEIIVGIPINTRPYT--EERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAITYKHNSYSHIVKDLNLNTNT 351
Cdd:PRK05691 3521 SGDRDVLFGVTVAGRPVSmpQMQRTVGLFINSIALRVQLPAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELP 3600

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  352 NHNMVYSTAFNTMKIPelkipdIESTVLTDCKRVNP----------FNMTwrIMRYEGEtENKIEVDYNSALYKPESISD 421
Cdd:PRK05691 3601 KGQPLFDSLFVFENAP------VEVSVLDRAQSLNAssdsgrthtnFPLT--AVCYPGD-DLGLHLSYDQRYFDAPTVER 3671

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  422 LVERYIYLLQKLMKNVNEPIHSLDLLLEKDHR-LYKEMNSNALTYPNLKTLDQLIDLQALKSPNQIAISMGDQSITYYEL 500
Cdd:PRK05691 3672 LLGEFKRLLLALVQGFHGDLSELPLLGEQERDfLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAEL 3751

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  501 QQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII----TKKEY 576
Cdd:PRK05691 3752 NRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVcsaaCREQA 3831

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  577 RGLVERFAIHT----IYLEDFHYANSIENIASTHTIEDA-AYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKED 651
Cdd:PRK05691 3832 RALLDELGCANrprlLVWEEVQAGEVASHNPGIYSGPDNlAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEAD 3911

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  652 VFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITnvVL---PTaffkLIADMPKEMLLKLNSV 728
Cdd:PRK05691 3912 VIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGIT--VLesvPS----LIQGMLAEDRQALDGL 3985

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  729 KRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEIQKEiSNIPIGKPIANSEVFVISPFNTLCPS 808
Cdd:PRK05691 3986 RWMLPTGEAMPPELARQWLQRYP-QIGLVNAYGPAECSDDVAFFRVDLASTRG-SYLPIGSPTDNNRLYLLDEALELVPL 4063

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  809 GVVGELFIGGDGVANGYLNQKEKTEGAFISlDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEG 888
Cdd:PRK05691 4064 GAVGELCVAGTGVGRGYVGDPLRTALAFVP-HPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEA 4142

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  889 TLFKHPEVRDAVVFTYQ--NDKIVCFYLSKDNTELKQEAL----KTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK05691 4143 RLHEQAEVREAAVAVQEgvNGKHLVGYLVPHQTVLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  963 elqiPSL-LENMQKQ-YVPPISETEKRLAKTWAEILNLGkyRIGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIF 1040
Cdd:PRK05691 4223 ----PALdIGQLQSQaYLAPRNELEQTLATIWADVLKVE--RVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMF 4296

                        1050      1060
                  ....*....|....*....|....
gi 446581728 1041 EHTTIASLSAYIDKLMAVNHDREE 1064
Cdd:PRK05691 4297 ECSTVEELAEYIEGLAGSAIDEQK 4320
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 483-962 1.77e-103

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 341.56  E-value: 1.77e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITKKEY-RGLVERFAihTIYLEDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSV 641
Cdd:cd12114    81 ADAGARLVLTDGPDaQLDVAVFD--VLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  642 INTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGIT--NVVlPtAFFKLIADMPK 719
Cdd:cd12114   159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTlwNSV-P-ALLEMLLDVLE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  720 EMLLKLNSVKRLFVGGETLPAESVRKWQsKLGLKIPVLNAYGPTETTVCATMYEVnGEIQKEISNIPIGKPIANSEVFVI 799
Cdd:cd12114   237 AAQALLPSLRLVLLSGDWIPLDLPARLR-ALAPDARLISLGGATEASIWSIYHPI-DEVPPDWRSIPYGRPLANQRYRVL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  800 SPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDKsynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGY 879
Cdd:cd12114   315 DPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPD----GERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGY 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  880 RIELDEIEGTLFKHPEVRDAVVFTYQNDK---IVCFYLSK-DNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSG 955
Cdd:cd12114   391 RIELGEIEAALQAHPGVARAVVVVLGDPGgkrLAAFVVPDnDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANG 470


                  ....*..
gi 446581728  956 KLDRKKL 962
Cdd:cd12114   471 KVDRAAL 477
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1078-1515 5.80e-102

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 336.23  E-value: 5.80e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1078 YQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFI-ERNGEPRQVILNSIAIDLIH 1156
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFELEI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1157 DEIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKR 1236
Cdd:pfam00668   85 IDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1237 RNPELPTISNrYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQV 1316
Cdd:pfam00668  165 EPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1317 CEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNS 1396
Cdd:pfam00668  244 AKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSA 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1397 FQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDILQQH-------DAYKLQLLPNKQDISKFDISLAVEEGLDYVGI 1469
Cdd:pfam00668  324 EPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSqeeefqlSELDLSVSSVIEEEAKYDLSLTASERGGGLTI 403

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 446581728  1470 SFEYDINLFKEESINRFTQNLLNILDAFIHQRTVTYENLSFLSQEE 1515
Cdd:pfam00668  404 KIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE 449
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 483-962 5.13e-101

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 333.60  E-value: 5.13e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLREN-DLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYI 561
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVaEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  562 LKDSESQMIITkkeyrglverfaihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSV 641
Cdd:cd17648    81 LEDTGARVVIT----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  642 INTFHLGKED--VFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIAdmpk 719
Cdd:cd17648   127 SERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYD---- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  720 emLLKLNSVKRLFVGGETLPAESVRKWQSklGLKIPVLNAYGPTETTVCATMYEVNGEIQKEISnipIGKPIANSEVFVI 799
Cdd:cd17648   203 --LARLPHLKRVDAAGEEFTAPVFEKLRS--RFAGLIINAYGPTETTVTNHKRFFPGDQRFDKS---LGRPVRNTKCYVL 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  800 SPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFIS------LDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQ 873
Cdd:cd17648   276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPnpfqteQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQ 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  874 VKIRGYRIELDEIEGTLFKHPEVRDAVVFT-YQNDK--------IVCFYLSkDNTELKQEALKTFLSESLPDFMMPNYIF 944
Cdd:cd17648   356 VKIRGQRIEPGEVEAALASYPGVRECAVVAkEDASQaqsriqkyLVGYYLP-EPGHVPESDLLSFLRAKLPRYMVPARLV 434

                         490
                  ....*....|....*...
gi 446581728  945 HLESFPVSPSGKLDRKKL 962
Cdd:cd17648   435 RLEGIPVTINGKLDVRAL 452
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 479-962 1.03e-98

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 326.51  E-value: 1.03e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRI 558
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  559 EYILKDSESQMIITkkeyrglverfaihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLS 638
Cdd:cd05945    81 REILDAAKPALLIA----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFT 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  639 YSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITnVVLPTAFFKLIADMP 718
Cdd:cd05945   127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGIT-VWVSTPSFAAMCLLS 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  719 KEMLLKLNSVKRLFV-GGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEVF 797
Cdd:cd05945   206 PTFTPESLPSLRHFLfCGEVLPHKTARALQQRFP-DARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKPGAKLV 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  798 VISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDKsynrdKKMYCTGDLVRLLANGNLEFIGRKDNQVKIR 877
Cdd:cd05945   285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEG-----QRAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  878 GYRIELDEIEGTLFKHPEVRDAVVF-TYQNDK---IVCFYLSKDNTELKQE-ALKTFLSESLPDFMMPNYIFHLESFPVS 952
Cdd:cd05945   360 GYRIELEEIEAALRQVPGVKEAVVVpKYKGEKvteLIAFVVPKPGAEAGLTkAIKAELAERLPPYMIPRRFVYLDELPLN 439

                         490
                  ....*....|
gi 446581728  953 PSGKLDRKKL 962
Cdd:cd05945   440 ANGKIDRKAL 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1545-2030 1.98e-98

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 325.74  E-value: 1.98e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:cd05945     3 ANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIRE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSnkfkshlnvsdykvsiiediyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEW 1704
Cdd:cd05945    83 ILDAAKPALLIAD----------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNW 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1705 RNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISdLPTVFFNELSTSLTK 1784
Cdd:cd05945   129 MLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVW-VSTPSFAAMCLLSPT 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1785 LDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVqLVNEYGPTEATVSAMYYFI--PVLEGennlLGSVPIGIPISNTK 1862
Cdd:cd05945   208 FTPESLPSLRHFLFCGEVLPHKTARALQQRFPDAR-IYNTYGPTEATVAVTYIEVtpEVLDG----YDRLPIGYAKPGAK 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1863 VHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpFSEDNsKRLYRTGDLVRWLPNGNIEFMGRKDKQVK 1942
Cdd:cd05945   283 LVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEG-QRAYRTGDLVRLEADGLLFYRGRLDFQVK 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1943 IRGHRIELGEIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKTVDGIGIEKNK-LAIHLSNVLPEYMVPKYYSHVLEIP 2018
Cdd:cd05945   358 LNGYRIELEEIEAALRQVPGVKEAVVvpkYKGEKVTELIAFVVPKPGAEAGLTKaIKAELAERLPPYMIPRRFVYLDELP 437

                         490
                  ....*....|..
gi 446581728 2019 ITANGKIDFEKL 2030
Cdd:cd05945   438 LNANGKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
478-877 3.92e-98

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 323.88  E-value: 3.92e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   478 QALKSPNQIAISMGD-QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEK 556
Cdd:pfam00501    4 QAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   557 RIEYILKDSESQMIITK--------KEYRGLVERFAIHTIYLEDFHYANSIENIASTH-----------TIEDAAYIIYT 617
Cdd:pfam00501   84 ELAYILEDSGAKVLITDdalkleelLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPadvppppppppDPDDLAYIIYT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   618 SGSTGLPKGVVVPHKGVVNLSYSVINT----FHLGKEDVFLQFATIIFDAS-IMEIFPILLCGGRMHLISEIEKRSAEEF 692
Cdd:pfam00501  164 SGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDPAAL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   693 INVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCATmY 772
Cdd:pfam00501  244 LELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG--GALVNGYGLTETTGVVT-T 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   773 EVNGEIQKEISNiPIGKPIANSEVFVISPfNTL--CPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDksynrdkkMY 850
Cdd:pfam00501  321 PLPLDEDLRSLG-SVGRPLPGTEVKIVDD-ETGepVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDG--------WY 390

                          410       420
                   ....*....|....*....|....*..
gi 446581728   851 CTGDLVRLLANGNLEFIGRKDNQVKIR 877
Cdd:pfam00501  391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
1539-1944 4.99e-98

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 323.50  E-value: 4.99e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1539 FYMQVDRQPERIAIATAT-ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKY 1617
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1618 PEDRINYIVRDSEACRIITSNKFKSHLNVSDykVSIIEDIYRTTINDDVKIL---------------------NKPDDLA 1676
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEA--LGKLEVVKLVLVLDRDPVLkeeplpeeakpadvpppppppPDPDDLA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1677 YVIYTSGSTGKPKGTLLTHKGVLNLV----EWRNEVFQISPNDKVTQFYSHSFDSSVS-EIFSTLLNGAELYLLSDEQRY 1751
Cdd:pfam00501  159 YIIYTSGTTGKPKGVMLTHRNLVANVlsikRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPAL 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1752 STVEYAQAIQETQATISDLPTVFFNELsTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVqlVNEYGPTEAT 1831
Cdd:pfam00501  239 DPAALLELIERYKVTVLYGVPTLLNML-LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGAL--VNGYGLTETT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1832 VSAMYYFIPvlEGENNLLGSvpIGIPISNTKVHILN-SYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFIsnpfse 1910
Cdd:pfam00501  316 GVVTTPLPL--DEDLRSLGS--VGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD------ 385

                          410       420       430
                   ....*....|....*....|....*....|....
gi 446581728  1911 dnSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIR 1944
Cdd:pfam00501  386 --EDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1535-2030 3.41e-90

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 302.11  E-value: 3.41e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1535 IQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPID 1614
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1615 VKYPEDRINYIVRDSEACRIITsnkfkshlnvsdykvsiiediyrttinddvkilnkpddlAYVIYTSGSTGKPKGTLLT 1694
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1695 HKGVLNLVEWRNEVFQISPNDKVTQFY--SHSFDSSVSeIFSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATISDLPT 1772
Cdd:COG0318   122 HRNLLANAAAIAAALGLTPGDVVLVALplFHVFGLTVG-LLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVP 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1773 VFFNELsTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFknQVQLVNEYGPTEATVSAMYyfiPVLEGENNLLGSV 1852
Cdd:COG0318   198 TMLARL-LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF--GVRIVEGYGLTETSPVVTV---NPEDPGERRPGSV 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1853 piGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpfsEDnskRLYRTGDLVRWLPNGNIE 1932
Cdd:COG0318   272 --GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF------RD---GWLRTGDLGRLDEDGYLY 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1933 FMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPK 2009
Cdd:COG0318   341 IVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVgvpDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPR 420

                         490       500
                  ....*....|....*....|.
gi 446581728 2010 YYSHVLEIPITANGKIDFEKL 2030
Cdd:COG0318   421 RVEFVDELPRTASGKIDRRAL 441
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
 2162-2432 3.75e-89

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 291.73  E-value: 3.75e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQLPSTTIYCLVRENEDQVIGAKLKERMEFYfgKEILQKLKERVELIEGDLSLMNLGLDS 2241
Cdd:COG3320     1 RTVLLTGATGFLGAHLLRELLRRTDARVYCLVRASDEAAARERLEALLERY--GLWLELDASRVVVVAGDLTQPRLGLSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKefeFFESDFDR 2320
Cdd:COG3320    79 AEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLkPFHYVSTIAVAGPADRSGV---FEEDDLDE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 GQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGKFQyniNENAFYRLLKGICLSSIAPDV-NTYVDLTP 2399
Cdd:COG3320   156 GQGFANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETN---KDDGFYRLLKGLLRLGAAPGLgDARLNLVP 232

                         250       260       270
                  ....*....|....*....|....*....|...
gi 446581728 2400 VDYGSLAITELSYKANTVNKTMHICNPNQLKWD 2432
Cdd:COG3320   233 VDYVARAIVHLSRQPEAAGRTFHLTNPQPLSLG 265
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1080-1500 1.66e-85

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 288.01  E-value: 1.66e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILN--SIAIDLIHD 1157
Cdd:cd19538     4 LSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEedEATPKLEIK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1158 EIEhmsKKEQQEYIRTTINQtdhtPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRR 1237
Cdd:cd19538    84 EVD---EEELESEINEAVRY----PFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1238 NPELPTISNRYVDYAEWEQVQLN-----LGRWDTEKSYWMAELAApLP-ILNLPLDFSRNRQSTNKGTVFEMKLDNEMKE 1311
Cdd:cd19538   157 APELAPLPVQYADYALWQQELLGdesdpDSLIARQLAYWKKQLAG-LPdEIELPTDYPRPAESSYEGGTLTFEIDSELHQ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1312 SLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVRE 1391
Cdd:cd19538   236 QLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1392 KCLNSFQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQ-----KDILQQHDAyKLQLLPNKQdiSKFDISLAVEEGLDY 1466
Cdd:cd19538   316 TNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQntpqpSLDLPGLEA-KLELRTVGS--AKFDLTFELREQYND 392

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 446581728 1467 V---GIS--FEYDINLFKEESINRFTQNLLNILDAFIHQ 1500
Cdd:cd19538   393 GtpnGIEgfIEYRTDLFDHETIEALAQRYLLLLESAVEN 431
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1080-1499 4.08e-85

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 286.58  E-value: 4.08e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFI-ERNGEPRQVILNSIAIDLIHdE 1158
Cdd:cd19539     4 LSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVrDDGGVPRQEILPPGPAPLEV-R 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1159 IEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRN 1238
Cdd:cd19539    83 DLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1239 PELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAApLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCE 1318
Cdd:cd19539   163 APLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1319 QENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQ 1398
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1399 NQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDILQQHDAYKLQLLPNKQDIS---KFDISLAVEEGLDYVGISFEYDI 1475
Cdd:cd19539   322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPdgaKFDLNLTVTEEGTGLRGSLGYAT 401

                         410       420
                  ....*....|....*....|....
gi 446581728 1476 NLFKEESINRFTQNLLNILDAFIH 1499
Cdd:cd19539   402 SLFDEETIQGFLADYLQVLRQLLA 425
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
475-962 1.11e-76

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 264.84  E-value: 1.11e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFP 554
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  555 EKRIEYILKDSESQMIITKKEYrgLVERFAIHTIYLEDFHYANSIENIAS-THTIE--DAAYIIYTSGSTGLPKGVVVPH 631
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATEEL--PLEILGIPVITLDELKDIFATGNPYDfDHAVKgdDNYYIIFTSGTTGKPKGVQISH 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  632 KGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLIS-EIEKRSAEEFINVsQKYGItNVVLPTAF 710
Cdd:PRK04813  166 DNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPkDMTANFKQLFETL-PQLPI-NVWVSTPS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  711 FkliADMPkeMLL------KLNSVKRLFVGGETLPAESVRKwqskLGLKIP---VLNAYGPTETTVCATMYEVNGEIQKE 781
Cdd:PRK04813  244 F---ADMC--LLDpsfneeHLPNLTHFLFCGEELPHKTAKK----LLERFPsatIYNTYGPTEATVAVTSIEITDEMLDQ 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  782 ISNIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDKsynrdKKMYCTGDLVRlLAN 861
Cdd:PRK04813  315 YKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDG-----QPAYHTGDAGY-LED 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  862 GNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQ-NDKIVcfYL-----SKDNT---ELK-QEALKTFLS 931
Cdd:PRK04813  389 GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNkDHKVQ--YLiayvvPKEEDferEFElTKAIKKELK 466

                         490       500       510
                  ....*....|....*....|....*....|.
gi 446581728  932 ESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK04813  467 ERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 475-962 6.31e-75

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 259.69  E-value: 6.31e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   475 IDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFP 554
Cdd:TIGR01734    6 IQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   555 EKRIEYILKDSESQMIITKKEYRGLVERFAIHTIYLEDfHYANSIENIASTHTI--EDAAYIIYTSGSTGLPKGVVVPHK 632
Cdd:TIGR01734   86 SERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALE-QAETSGGPVSFDHAVkgDDNYYIIYTSGSTGNPKGVQISHD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   633 GVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGItNVVLPTAFFk 712
Cdd:TIGR01734  165 NLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGL-NVWVSTPSF- 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   713 liADMPkeMLL------KLNSVKRLFVGGETLPaesvRKWQSKLGLKIP---VLNAYGPTETTVCATMYEVNGEIQKEIS 783
Cdd:TIGR01734  243 --VDMC--LLDpnfnqeNYPHLTHFLFCGEELP----VKTAKALLERFPkatIYNTYGPTEATVAVTSVKITQEILDQYP 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   784 NIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDksynrDKKMYCTGDLVRlLANGN 863
Cdd:TIGR01734  315 RLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSHE-----GQPAYRTGDAGT-ITDGQ 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   864 LEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF--TYQNDKI---VCFYLSKDNTELKQE----ALKTFLSESL 934
Cdd:TIGR01734  389 LFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVpkYNKDHKVeylIAAIVPETEDFEKEFqltkAIKKELKKSL 468

                          490       500
                   ....*....|....*....|....*...
gi 446581728   935 PDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:TIGR01734  469 PAYMIPRKFIYRDQLPLTANGKIDRKAL 496
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1077-1498 2.45e-74

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 255.32  E-value: 2.45e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1077 SYQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIH 1156
Cdd:cd20484     1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1157 DEIEHMSKKEQQEYIRTTINQtdhtPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKR 1236
Cdd:cd20484    81 EDISSLKESEIIAYLREKAKE----PFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1237 RNPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQV 1316
Cdd:cd20484   157 KQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSF 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1317 CEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNS 1396
Cdd:cd20484   237 ARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDG 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1397 FQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKdiLQQHDAYKlQLLPNKQDIS------------KFDISLAVEEGL 1464
Cdd:cd20484   317 LDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQN--FLQSTSLQ-QFLAEYQDVLsiefvegihqegEYELVLEVYEQE 393

                         410       420       430
                  ....*....|....*....|....*....|....
gi 446581728 1465 DYVGISFEYDINLFKEESINRFTQNLLNILDAFI 1498
Cdd:cd20484   394 DRFTLNIKYNPDLFDASTIERMMEHYVKLAEELI 427
SDR_e1 cd05235
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ...
 2163-2455 7.95e-74

extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187546 [Multi-domain]  Cd Length: 290  Bit Score: 248.72  E-value: 7.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLP-STTIYCLVRENEDQVIGAKLKERMEFYFGKEILQKLKERVELIEGDLSLMNLGLDS 2241
Cdd:cd05235     1 TVLLTGATGFLGAYLLRELLKRKnVSKIYCLVRAKDEEAALERLIDNLKEYGLNLWDELELSRIKVVVGDLSKPNLGLSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKEFEFFESDFDR 2320
Cdd:cd05235    81 DDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLkPLHFVSTLSVFSAEEYNALDDEESDDMLES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 GQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGkfqYNINENAFYRLLKGICLSSIAPDVNTYVDLTPV 2400
Cdd:cd05235   161 QNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETG---IGNTDDFFWRLLKGCLQLGIYPISGAPLDLSPV 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 2401 DYGSLAITELSYKANTVNKTMHICNPNQLKWDQFINSLQAFGYDillMKQEKYIE 2455
Cdd:cd05235   238 DWVARAIVKLALNESNEFSIYHLLNPPLISLNDLLDALEEKGYS---IKEVSYEE 289
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 20-451 8.10e-72

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 249.17  E-value: 8.10e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728    20 QEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIF-KKRDEKIKQLIQKNVEFDIPIKDLTAF 98
Cdd:pfam00668   11 QKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEPVQVILEERPFELEIIDISDL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728    99 KNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKSNVEF 178
Cdd:pfam00668   91 SESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGEPLPLP 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   179 E-SPYKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFAKKNNIS 257
Cdd:pfam00668  171 PkTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGTT 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   258 IYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAITYKHNS 337
Cdd:pfam00668  251 LNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGYP 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   338 YSHIVKDLNLNTNTNHNMVYSTAFNT------MKIPELKIPD-IESTVLTDCKRVNPFNMTwrIMRYEGETENKIEVDYN 410
Cdd:pfam00668  331 FGDLVNDLRLPRDLSRHPLFDPMFSFqnylgqDSQEEEFQLSeLDLSVSSVIEEEAKYDLS--LTASERGGGLTIKIDYN 408

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 446581728   411 SALYKPESISDLVERYIYLLQKLMKNVNEPIHSLDLLLEKD 451
Cdd:pfam00668  409 TSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE 449
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 610-958 9.39e-72

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 244.50  E-value: 9.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLIseiEKRSA 689
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL---PKFDP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  690 EEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCA 769
Cdd:cd04433    78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTETGGTV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  770 TMYEVNGEIQKEISnipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKkM 849
Cdd:cd04433   156 ATGPPDDDARKPGS---VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDG-W 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  850 YCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYLSKDNTELKQEA 925
Cdd:cd04433   224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgvpdPEWGERVVAVVVLRPGADLDAEE 303

                         330       340       350
                  ....*....|....*....|....*....|...
gi 446581728  926 LKTFLSESLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:cd04433   304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 492-962 1.05e-70

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 245.46  E-value: 1.05e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  492 DQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII 571
Cdd:cd17654    14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  572 TKKEYRGLVERFAIHTiyledfhyansiENIASTHTiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKED 651
Cdd:cd17654    94 QNKELDNAPLSFTPEH------------RHFNIRTD-ECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  652 VFLQFATIIFDASIMEIFPILLCGGRMhLISEIEKRSAEEFI--NVSQKYGITNVVL-PTAFFKLIADMPKEMLL-KLNS 727
Cdd:cd17654   161 ILFLTSPLTFDPSVVEIFLSLSSGATL-LIVPTSVKVLPSKLadILFKRHRITVLQAtPTLFRRFGSQSIKSTVLsATSS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  728 VKRLFVGGETLPAESVRKWQSKLGLKIPVLNAYGPTETTVCATMYEVngeiQKEISNIPIGKPIANSEVFVIspfnTLCP 807
Cdd:cd17654   240 LRVLALGGEPFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKV----PEEDSPVQLGSPLLGTVIEVR----DQNG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  808 SGVVGELFIGGD---GVANGYLNQKEKTegafisldksynrdkkMYCTGDLVRLlANGNLEFIGRKDNQVKIRGYRIELD 884
Cdd:cd17654   312 SEGTGQVFLGGLnrvCILDDEVTVPKGT----------------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLD 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  885 EIEGTLFKHPEVRDAVVFTYQNDKIVCFYLSKDNTELKQEALKTFLSES--LPDFMmpNYIfhlESFPVSPSGKLDRKKL 962
Cdd:cd17654   375 LIQQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSRIHKELQLTLLSShaIPDTF--VQI---DKLPLTSHGKVDKSEL 449
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1080-1496 1.71e-70

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 244.25  E-value: 1.71e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVIL--NSIAIDLihd 1157
Cdd:cd19540     4 LSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLpaAEARPDL--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1158 EIEHMSKKEQQEYIRTTINqtdhTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRR 1237
Cdd:cd19540    81 TVVDVTEDELAARLAEAAR----RGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1238 NPELPTISNRYVDYAEWeQVQLnLGRWDTEKS-------YWMAELAApLP-ILNLPLDFSRNRQSTNKGTVFEMKLDNEM 1309
Cdd:cd19540   157 APDWAPLPVQYADYALW-QREL-LGDEDDPDSlaarqlaYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAEL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1310 KESLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVV 1389
Cdd:cd19540   234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1390 REKCLNSFQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSyqkdiLQQHDAYKLQL-------LPNKQDISKFDISLAVEE 1462
Cdd:cd19540   314 RETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLA-----FQNTAAATLELpgltvepVPVDTGVAKFDLSFTLTE 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 446581728 1463 GLDYVG------ISFEYDINLFKEESINRFTQNLLNILDA 1496
Cdd:cd19540   389 RRDADGapagltGELEYATDLFDRSTAERLADRFVRVLEA 428
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 205-1055 6.79e-70

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 260.77  E-value: 6.79e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   205 WKDYLQGeLTPTEFPIDFNKMNEKRYTDKNISKNINSDLFyqiqcfAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGip 284
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLG-- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   285 intrpyTEERNTFGYFVntlpIRITIEKGETFKGILNKVNKSIHLAITYKHNSYSHIVKDLNLNTNTNHN-MVYSTAFnt 363
Cdd:TIGR03443   73 ------TSSNKSGRPFV----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTpPLFRLAF-- 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   364 MKIPELKIPDIESTVLTDCKrvnpfnmtwrIMRYEGETENKIEVDYNSALYKPESISDLVERYIYLLQKLMKNVNEPIHS 443
Cdd:TIGR03443  141 QDAPDNQQTTYSTGSTTDLT----------VFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGK 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   444 LDLLLE----------KD----------HRLYKEmnsNALTYPNlKTLdqlidlqALKSPNQIAISMGDQSITYYELQQR 503
Cdd:TIGR03443  211 VSLITPsqksllpdptKDldwsgfrgaiHDIFAD---NAEKHPD-RTC-------VVETPSFLDPSSKTRSFTYKQINEA 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   504 SNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKR-IEYILKDSESQMIITKK--EYRGLV 580
Cdd:TIGR03443  280 SNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqTIYLSVAKPRALIVIEKagTLDQLV 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   581 ERF---------AIHTIYLED-------FHYANSIENIAS-THTIEDAAYII----------YTSGSTGLPKGVVVPHkg 633
Cdd:TIGR03443  360 RDYidkelelrtEIPALALQDdgslvggSLEGGETDVLAPyQALKDTPTGVVvgpdsnptlsFTSGSEGIPKGVLGRH-- 437

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   634 vVNLSYS---VINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISE----IEKRSAEEFinvsQKYGITNVVL 706
Cdd:TIGR03443  438 -FSLAYYfpwMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTAddigTPGRLAEWM----AKYGATVTHL 512

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   707 PTAFFKLIADMPKEMLLKLNSVkrLFVGgETLPAESVRKWQSkLGLKIPVLNAYGPTETTVCATMYEVNG--------EI 778
Cdd:TIGR03443  513 TPAMGQLLSAQATTPIPSLHHA--FFVG-DILTKRDCLRLQT-LAENVCIVNMYGTTETQRAVSYFEIPSrssdstflKN 588

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   779 QKEIsnIPIGKPIANSEVFVISPF--NTLCPSGVVGELFIGGDGVANGYLN----QKEK-------TEGAFISLDKSYN- 844
Cdd:TIGR03443  589 LKDV--MPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGlpelNAEKfvnnwfvDPSHWIDLDKENNk 666

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   845 ---------RDKkMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTyQNDK-----IV 910
Cdd:TIGR03443  667 perefwlgpRDR-LYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLV-RRDKdeeptLV 744

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   911 CFYLSKDNT----ELKQEA----------------------LKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLEL 964
Cdd:TIGR03443  745 SYIVPQDKSdeleEFKSEVddeessdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPF 824

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   965 QIPSLLENMQKQYVPPI-----SETEKRLAKTWAEILNLGKYRIGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDI 1039
Cdd:TIGR03443  825 PDTAQLAAVAKNRSASAadeefTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLI 904

                          970
                   ....*....|....*.
gi 446581728  1040 FEHTTIASLSAYIDKL 1055
Cdd:TIGR03443  905 FKSPTIKGFAKEVDRL 920
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1533-2030 1.46e-69

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 244.03  E-value: 1.46e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1533 QNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIP 1612
Cdd:PRK04813    2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1613 IDVKYPEDRINYIVRDSEACRIITSNKFK-SHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGT 1691
Cdd:PRK04813   82 VDVSSPAERIEMIIEVAKPSLIIATEELPlEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1692 LLTHKGVLNLVEWRNEVFQISPNDkvtQFYSH---SFDSSVSEIFSTLLNGAELYLLSDE------QRYSTVEyAQAIQE 1762
Cdd:PRK04813  162 QISHDNLVSFTNWMLEDFALPEGP---QFLNQapySFDLSVMDLYPTLASGGTLVALPKDmtanfkQLFETLP-QLPINV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1763 TQATISdlptvfFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFkNQVQLVNEYGPTEATV--SAMYYFIP 1840
Cdd:PRK04813  238 WVSTPS------FADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERF-PSATIYNTYGPTEATVavTSIEITDE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1841 VLEGENNLlgsvPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFIsnpfsEDNSKRLYRTG 1920
Cdd:PRK04813  311 MLDQYKRL----PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF-----TFDGQPAYHTG 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1921 DLVRwLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAV---------VTQteggmlLQAYYKTVDGiGIEK 1991
Cdd:PRK04813  382 DAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVvvpynkdhkVQY------LIAYVVPKEE-DFER 453

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 446581728 1992 N-KL--AI--HLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKL 2030
Cdd:PRK04813  454 EfELtkAIkkELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1080-1325 1.78e-67

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 228.38  E-value: 1.78e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKRIWFLNKYNAinrVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDEI 1159
Cdd:COG4908     1 LSPAQKRFLFLEPGSN---AYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1160 EHMSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNP 1239
Cdd:COG4908    78 SALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1240 ELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQ 1319
Cdd:COG4908   158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237


                  ....*.
gi 446581728 1320 ENISMY 1325
Cdd:COG4908   238 HGATVN 243
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 1534-2030 3.40e-65

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 231.19  E-value: 3.40e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1534 NIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPI 1613
Cdd:TIGR01734    1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1614 DVKYPEDRINYIVRDSEACRIITSNKFKshLNVSDYKV---SIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKG 1690
Cdd:TIGR01734   81 DTSIPSERIEMIIEAAGPELVIHTAELS--IDAVGTQIitlSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1691 TLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQrysTVEYAQAIQETQATISDL 1770
Cdd:TIGR01734  159 VQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDI---TNNFKLLFEELPKTGLNV 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1771 --PTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVqLVNEYGPTEATVSamyyfIPVLEGENNL 1848
Cdd:TIGR01734  236 wvSTPSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKAT-IYNTYGPTEATVA-----VTSVKITQEI 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1849 LG---SVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpFSEDNsKRLYRTGDLVRw 1925
Cdd:TIGR01734  310 LDqypRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHEG-QPAYRTGDAGT- 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1926 LPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV---TQTEG---GMLLQAYYKTVDGIGIEKNKLAI--H 1997
Cdd:TIGR01734  384 ITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVvpkYNKDHkveYLIAAIVPETEDFEKEFQLTKAIkkE 463

                          490       500       510
                   ....*....|....*....|....*....|...
gi 446581728  1998 LSNVLPEYMVPKYYSHVLEIPITANGKIDFEKL 2030
Cdd:TIGR01734  464 LKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1078-1498 1.70e-63

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 223.83  E-value: 1.70e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1078 YQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIA------ 1151
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVrfriei 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1152 IDLIHDEIEHMSKKEQqeyirttINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYS 1231
Cdd:cd19066    82 IDLRNLADPEARLLEL-------IDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1232 AfAKRRNPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKE 1311
Cdd:cd19066   155 A-AERQKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1312 SLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVRE 1391
Cdd:cd19066   234 RLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1392 KCLNSFQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDilQQHDAYKLQLLPNKQDIS-----KFDISL-AVEEGLD 1465
Cdd:cd19066   314 QSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNN--QQQLGKTGGFIFTTPVYTssegtVFDLDLeASEDPDG 391

                         410       420       430
                  ....*....|....*....|....*....|...
gi 446581728 1466 YVGISFEYDINLFKEESINRFTQNLLNILDAFI 1498
Cdd:cd19066   392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLI 424
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
474-972 1.45e-60

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 219.60  E-value: 1.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  474 LIDLQALKSPNQIAI-----SMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVP 548
Cdd:COG0365    14 CLDRHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  549 IDPKFPEKRIEYILKDSESQMIITKKEYR------GLVERFAI---------HTIYLE----------DFHYANSIENIA 603
Cdd:COG0365    94 VFPGFGAEALADRIEDAEAKVLITADGGLrggkviDLKEKVDEaleelpsleHVIVVGrtgadvpmegDLDWDELLAAAS 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  604 STHTIE-----DAAYIIYTSGSTGLPKGVVVPHKG-VVNLSYSVINTFHLGKEDVFLQFATI--IFDASIMEIFPiLLCG 675
Cdd:COG0365   174 AEFEPEptdadDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIgwATGHSYIVYGP-LLNG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  676 GRMhLISE--IEKRSAEEFINVSQKYGITnvVL---PTAFFKLIADMPKemLLK---LNSVKRLFVGGETLPAESVRKWQ 747
Cdd:COG0365   253 ATV-VLYEgrPDFPDPGRLWELIEKYGVT--VFftaPTAIRALMKAGDE--PLKkydLSSLRLLGSAGEPLNPEVWEWWY 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  748 SKLGlkIPVLNAYGPTETTVCAtmyevngeiqkeISNIP--------IGKPIANSEVFVISPFNTLCPSGVVGELFIGGD 819
Cdd:COG0365   328 EAVG--VPIVDGWGQTETGGIF------------ISNLPglpvkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGP 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  820 --GVANGYLNQKEKTEGAFisldksYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVR 897
Cdd:COG0365   394 wpGMFRGYWNDPERYRETY------FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA 467

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  898 DAVVFTYQND----KIVCFYLSKDNT----ELKQEaLKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL------- 962
Cdd:COG0365   468 EAAVVGVPDEirgqVVKAFVVLKPGVepsdELAKE-LQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLrkiaegr 546

                         570
                  ....*....|
gi 446581728  963 ELQIPSLLEN 972
Cdd:COG0365   547 PLGDTSTLED 556
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 470-962 4.03e-59

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 213.88  E-value: 4.03e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   470 TLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPI 549
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   550 DPKFPEKRIEYILKDSESQMIITKKE-----YRGLVERFAIHT-IYLEDFHYANSIENIASTHTIE-------------- 609
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSErldllHPALPGCHDLRTlIIVGDPAHASEGHPGEEPASWPkllalgdadpphpv 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   610 ---DAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEK 686
Cdd:TIGR03098  161 idsDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   687 RsaeEFINVSQKYGITNV-VLPTAFFKLIADMPKEMLLKlnSVKRLFVGGETLPAESVRKWQSKLGLKIPVLnAYGPTET 765
Cdd:TIGR03098  241 R---DVLKALEKHGITGLaAVPPLWAQLAQLDWPESAAP--SLRYLTNSGGAMPRATLSRLRSFLPNARLFL-MYGLTEA 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   766 TvcATMYEVNGEIQKEISNipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISL----DK 841
Cdd:TIGR03098  315 F--RSTYLPPEEVDRRPDS--IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLppfpGE 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   842 SYNRDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKD 917
Cdd:TIGR03098  391 LHLPELAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTlgqaIVLVVTPPG 469

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 446581728   918 NTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:TIGR03098  470 GEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 1547-2031 5.72e-59

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 213.53  E-value: 5.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAI-------ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPE 1619
Cdd:cd17647     2 PERTCVvetpslnSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1620 DRINYivrdseacriitsnkfksHLNVSDYKVSIIEDiyrttindDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVL 1699
Cdd:cd17647    82 ARQNI------------------YLGVAKPRGLIVIR--------AAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1700 NLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLpTVFFNELs 1779
Cdd:cd17647   136 YYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHL-TPAMGQL- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1780 tsLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQnTFKNQVQLVNEYGPTEATVSAMYYFIPVLEGE----NNLLGSVPIG 1855
Cdd:cd17647   214 --LTAQATTPFPKLHHAFFVGDILTKRDCLRLQ-TLAENVRIVNMYGTTETQRAVSYFEVPSRSSDptflKNLKDVMPAG 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1856 IPISNTKVHILNSY--MQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISN--------------------PFSEDNS 1913
Cdd:cd17647   291 RGMLNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGPR 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1914 KRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQ----LEGISqAVVTQTEGGMLLQAYY-------- 1981
Cdd:cd17647   371 DRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQhplvRENIT-LVRRDKDEEPTLVSYIvprfdkpd 449

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728 1982 ------------KTVDGI--GIEKNKLAI-----HLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLP 2031
Cdd:cd17647   450 desfaqedvpkeVSTDPIvkGLIGYRKLIkdireFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 1554-2030 6.58e-58

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 208.48  E-value: 6.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1554 TATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACR 1633
Cdd:cd17654    12 TSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1634 IITsNKFkshlnvSDYKVSIIEDIYRTtinddvKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISP 1713
Cdd:cd17654    92 LLQ-NKE------LDNAPLSFTPEHRH------FNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1714 NDkVTQFYS-HSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYA------QAIQETQATisdlPTVFFNELSTSLTKLD 1786
Cdd:cd17654   159 ED-ILFLTSpLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLAdilfkrHRITVLQAT----PTLFRRFGSQSIKSTV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1787 SEKIRSLRFIIMGGEA-ASTNAIRSWQNTFkNQVQLVNEYGPTEATVSAMYYFIPVLEgennllGSVPIGIPISNTKVHI 1865
Cdd:cd17654   234 LSATSSLRVLALGGEPfPSLVILSSWRGKG-NRTRIFNIYGITEVSCWALAYKVPEED------SPVQLGSPLLGTVIEV 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1866 lnsyMQYCPVGCMGELYIEslGLAQGYWKQKEKTKqafisnPFSEdnskrLYRTGDLVRwLPNGNIEFMGRKDKQVKIRG 1945
Cdd:cd17654   307 ----RDQNGSEGTGQVFLG--GLNRVCILDDEVTV------PKGT-----MRATGDFVT-VKDGELFFLGRKDSQIKRRG 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1946 HRIELGEIEDAMLQLEGISQAVVTQTEGGMLLQAYyktVDgigiEKNKLAIHLS---NVLPEYMVPKYYSHVLEIPITAN 2022
Cdd:cd17654   369 KRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFI---VG----ESSSSRIHKElqlTLLSSHAIPDTFVQIDKLPLTSH 441


                  ....*...
gi 446581728 2023 GKIDFEKL 2030
Cdd:cd17654   442 GKVDKSEL 449
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 471-962 1.12e-57

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 208.19  E-value: 1.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  471 LDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPID 550
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  551 PKFPEKRIEYILKDSESQMIITKKEYRGLVERFAIHTIYLEDfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVP 630
Cdd:cd05936    81 PLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVAL--------------TPEDVAVLQYTSGTTGVPKGAMLT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  631 HKGVVNLSYSVINTF--HLGKEDVFLqfATI----IFDASIMEIFPILLcGGRMHLISeieKRSAEEFINVSQKYGITNV 704
Cdd:cd05936   147 HRNLVANALQIKAWLedLLEGDDVVL--AALplfhVFGLTVALLLPLAL-GATIVLIP---RFRPIGVLKEIRKHRVTIF 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  705 V-LPTAFFKLIAdMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLkiPVLNAYGPTETTVCATMYEVNGEiQKEIS 783
Cdd:cd05936   221 PgVPTMYIALLN-APEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGV--PIVEGYGLTETSPVVAVNPLDGP-RKPGS 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  784 nipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMYcTGDLVRLLANGN 863
Cdd:cd05936   297 ---IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF--------VDGWLR-TGDIGYMDEDGY 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  864 LEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMM 939
Cdd:cd05936   365 FFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgvpdPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKV 444

                         490       500
                  ....*....|....*....|...
gi 446581728  940 PNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05936   445 PRQVEFRDELPKSAVGKILRREL 467
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 479-959 2.24e-57

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 206.31  E-value: 2.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRI 558
Cdd:cd17631     5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  559 EYILKDSESQMIItkkeyrglverfaihtiyledfhyansieniasthtiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLS 638
Cdd:cd17631    85 AYILADSGAKVLF-------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  639 YSVINTFHLGKEDVFLQFATII-FDASIMEIFPILLCGGRMHLISEIEkrsAEEFINVSQKYGITNVVLPTAFFKLIADM 717
Cdd:cd17631   128 VNALAALDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVILRKFD---PETVLDLIERHRVTSFFLVPTMIQALLQH 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  718 PKEMLLKLNSVKRLFVGGETLPAESVRKWQSKlglKIPVLNAYGPTETTVCATMYEVNGEIQKEISnipIGKPIANSEVF 797
Cdd:cd17631   205 PRFATTDLSSLRAVIYGGAPMPERLLRALQAR---GVKFVQGYGMTETSPGVTFLSPEDHRRKLGS---AGRPVFFVEVR 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  798 VISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDkKMYCTGDLVRLLANGNLEFIGRKDNQVKIR 877
Cdd:cd17631   279 IVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF--------RD-GWFHTGDLGRLDEDGYLYIVDRKKDMIISG 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  878 GYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSP 953
Cdd:cd17631   350 GENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwgeaVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNA 429


                  ....*.
gi 446581728  954 SGKLDR 959
Cdd:cd17631   430 TGKILK 435
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 465-962 3.20e-57

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 208.50  E-value: 3.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  465 YPNLKTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSitmereidTIVW--------I 536
Cdd:PRK06187    2 QDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVA--------VFDWnsheyleaY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  537 LGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKEYRGLVERFA-----IHTIYLED-----------FHYANSIE 600
Cdd:PRK06187   74 FAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILpqlptVRTVIVEGdgpaaplapevGEYEELLA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  601 NIASTH-----TIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLqfatiifdaSIMEIFPI---- 671
Cdd:PRK06187  154 AASDTFdfpdiDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYL---------VIVPMFHVhawg 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  672 -----LLCGGRMHLISEIEKRSAEEFInvsQKYGITnvVL---PTAFfkliadmpkEMLLK--------LNSVKRLFVGG 735
Cdd:PRK06187  225 lpylaLMAGAKQVIPRRFDPENLLDLI---ETERVT--FFfavPTIW---------QMLLKaprayfvdFSSLRLVIYGG 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  736 ETLPAESVRKWQSKLGlkIPVLNAYGPTET--TVCATMYE--VNGEIQKEISnipIGKPIANSEVFVISP-FNTLCPSGV 810
Cdd:PRK06187  291 AALPPALLREFKEKFG--IDLVQGYGMTETspVVSVLPPEdqLPGQWTKRRS---AGRPLPGVEARIVDDdGDELPPDGG 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  811 -VGELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGT 889
Cdd:PRK06187  366 eVGEIIVRGPWLMQGYWNRPEATAETI---------DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDA 436

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728  890 LFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK06187  437 LYGHPAVAEVAVIGVPDEKwgerPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 15-436 2.69e-56

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 202.93  E-value: 2.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   15 DVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIPIKD 94
Cdd:cd20484     3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   95 LTAFKNTEqksILKnFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKS 174
Cdd:cd20484    83 ISSLKESE---IIA-YLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  175 NVEFESP--YKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFAK 252
Cdd:cd20484   159 PTLASSPasYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFAR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  253 KNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPytEER--NTFGYFVNTLPIRITIEKGETFKGILNKVNksIHLA 330
Cdd:cd20484   239 SQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRP--EERfdSLIGYFINMLPIRSRILGEETFSDFIRKLQ--LTVL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  331 ITYKHNSY--SHIVKDLNLNTNTNHNMVYSTAF---NTMKIPELKipdiesTVLTDCKRVNPFNMTWRImRYEGETENKI 405
Cdd:cd20484   315 DGLDHAAYpfPAMVRDLNIPRSQANSPVFQVAFfyqNFLQSTSLQ------QFLAEYQDVLSIEFVEGI-HQEGEYELVL 387

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 446581728  406 EV-----------DYNSALYKPESISDLVERYIYLLQKLMKN 436
Cdd:cd20484   388 EVyeqedrftlniKYNPDLFDASTIERMMEHYVKLAEELIAN 429
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1080-1429 5.21e-56

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 201.92  E-value: 5.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKRIWFLNKYnainrvYDTP------LHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIER--NGEPRQVILNSIA 1151
Cdd:cd19532     4 MSFGQSRFWFLQQY------LEDPttfnvtFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDpeDGEPMQGVLASSP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1152 IDLIHDEIEHmskkeqQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYs 1231
Cdd:cd19532    78 LRLEHVQISD------EAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1232 afakrRNPELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELA---APLPILNLPLdfSRNRQSTNK-GTV-FEMKLD 1306
Cdd:cd19532   151 -----NGQPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFStlpEPLPLLPFAK--VKSRPPLTRyDTHtAERRLD 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1307 NEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLL 1386
Cdd:cd19532   224 AALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVL 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 446581728 1387 QVVREKCLNSFQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSY 1429
Cdd:cd19532   304 KETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINY 346
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 19-323 2.33e-55

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 200.27  E-value: 2.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   19 GQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIPIKDLTAF 98
Cdd:cd19531     7 AQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVDLSGL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   99 KNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKsnvef 178
Cdd:cd19531    87 PEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGR----- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  179 ESP-------YKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFA 251
Cdd:cd19531   162 PSPlpplpiqYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRALA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728  252 KKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKV 323
Cdd:cd19531   242 RREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARV 313
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1674-2026 1.65e-54

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 194.81  E-value: 1.65e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1674 DLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLsdeQRYST 1753
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL---PKFDP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1754 VEYAQAIQETQATISDLPTVFFNELsTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTEATVS 1833
Cdd:cd04433    78 EAALELIEREKVTILLGVPTLLARL-LKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTETGGT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1834 AMYYFipvLEGENNLLGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpfsEDNs 1913
Cdd:cd04433   155 VATGP---PDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD------EDG- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1914 krLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIE 1990
Cdd:cd04433   223 --WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgvpDPEWGERVVAVVVLRPGADLD 300

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 446581728 1991 KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:cd04433   301 AEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
 2163-2451 8.76e-54

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 193.79  E-value: 8.76e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2163 TVFLTGATGYLGAHILERLL-QLPSTTIYCLVRENEDQVIGAKLKERMEFYFGKEiLQKLKERVELIEGDLSLMNLGLDS 2241
Cdd:TIGR01746    1 TVLLTGATGFLGAYLLEELLrRSTRAKVICLVRADSEEHAMERLREALRSYRLWH-ENLAMERIEVVAGDLSKPRLGLSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2242 KQLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSvVGQAERDPKEFEFFESDFDR 2320
Cdd:TIGR01746   80 AEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKpLHYVSTIS-VGAAIDLSTGVTEDDATVTP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2321 GQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGKFQYNineNAFYRLLKGiCLS-SIAPDVN-TYVDLT 2398
Cdd:TIGR01746  159 YPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSS---DILWRMVKG-CLAlGAYPQSPeLTEDLT 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728  2399 PVDYGSLAITELS--YKANTVNKTMHICNPNQLKWDQFINSLQAFGYDILLMKQE 2451
Cdd:TIGR01746  235 PVDFVARAIVALSsrPAASAGGIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFD 289
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 492-962 1.90e-53

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 194.43  E-value: 1.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  492 DQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII 571
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  572 TkkeyrglverfaihtiyledfhyansieniasthtieDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKED 651
Cdd:cd05934    81 V-------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  652 VFLQfATIIF--DASIMEIFPILLCGGRMHLiseIEKRSAEEFINVSQKYGITnvvlptaFFKLIADMPKeMLLKL---- 725
Cdd:cd05934   124 VYLT-VLPLFhiNAQAVSVLAALSVGATLVL---LPRFSASRFWSDVRRYGAT-------VTNYLGAMLS-YLLAQppsp 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  726 ----NSVkRLFVGGETLPAESvRKWQSKLGlkIPVLNAYGPTETTVCatmyeVNGEIQKEISNIPIGKPIANSEVFVISP 801
Cdd:cd05934   192 ddraHRL-RAAYGAPNPPELH-EEFEERFG--VRLLEGYGMTETIVG-----VIGPRDEPRRPGSIGRPAPGYEVRIVDD 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  802 FNTLCPSGVVGELFI---GGDGVANGYLNQKEKTEGAFISLdksynrdkkMYCTGDLVRLLANGNLEFIGRKDNQVKIRG 878
Cdd:cd05934   263 DGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAMRNG---------WFHTGDLGYRDADGFFYFVDRKKDMIRRRG 333

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  879 YRIELDEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPS 954
Cdd:cd05934   334 ENISSAEVERAILRHPAVREAAVVavpdEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPT 413


                  ....*...
gi 446581728  955 GKLDRKKL 962
Cdd:cd05934   414 EKVAKAQL 421
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1080-1500 3.08e-53

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 194.02  E-value: 3.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAIDLIHDEI 1159
Cdd:cd20483     4 MSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVIDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1160 EhmSKKEQQEYIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNP 1239
Cdd:cd20483    84 S--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1240 -ELPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELA-APLPILNLPldFSRNRQSTNK----GTVfEMKLDNEMKESL 1313
Cdd:cd20483   162 aTVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEgIPDASKLLP--FAKAERPPVKdyerSTV-EATLDKELLARM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1314 KQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKC 1393
Cdd:cd20483   239 KRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1394 LNSFQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQK------------DILQ-QHDayklqllpnkqDI-SKFDISLA 1459
Cdd:cd20483   319 LEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVhgkfpeydtgdfKFTDyDHY-----------DIpTACDIALE 387

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 446581728 1460 VEE----GLDyvgISFEYDINLFKEESINRFTQNLLNILDAFIHQ 1500
Cdd:cd20483   388 AEEdpdgGLD---LRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
 2166-2407 1.31e-51

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 183.58  E-value: 1.31e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2166 LTGATGYLGAHILERLLQLPS--TTIYCLVRENEDQVIGAKLKERMEFYF-GKEILQKLKERVELIEGDLSLMNLGLDSK 2242
Cdd:pfam07993    1 LTGATGFLGKVLLEKLLRSTPdvKKIYLLVRAKDGESALERLRQELEKYPlFDALLKEALERIVPVAGDLSEPNLGLSEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2243 QLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNT--NVRFHYISTlSVVGQAERDPKEFEFFES---- 2316
Cdd:pfam07993   81 DFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGkqLKPFHHVST-AYVNGERGGLVEEKPYPEgedd 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2317 ------DFDRGQNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVGNSKTGKFQyniNENAFYRLLKGIC----LSS 2386
Cdd:pfam07993  160 mlldedEPALLGGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWIN---NFDFGPRGLLGGIgkgvLPS 236

                          250       260
                   ....*....|....*....|.
gi 446581728  2387 IAPDVNTYVDLTPVDYGSLAI 2407
Cdd:pfam07993  237 ILGDPDAVLDLVPVDYVANAI 257
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 20-259 2.17e-51

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 182.16  E-value: 2.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   20 QEALWIahqMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIPIKDLTAFK 99
Cdd:COG4908     5 QKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDLSALP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  100 NTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKSNV--E 177
Cdd:COG4908    82 EPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPPPlpE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  178 FESPYKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFAKKNNIS 257
Cdd:COG4908   162 LPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKAHGAT 241


                  ..
gi 446581728  258 IY 259
Cdd:COG4908   242 VN 243
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 1542-2026 2.81e-51

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 189.70  E-value: 2.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1542 QVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDR 1621
Cdd:cd05936     8 AARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1622 INYIVRDSEACRIITSNKFkshlnvsdykvsiiEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKgvlNL 1701
Cdd:cd05936    88 LEHILNDSGAKALIVAVSF--------------TDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHR---NL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1702 V-------EWRNEVfqISPNDKVTQF--YSHSFDSSVSeIFSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATI-SDLP 1771
Cdd:cd05936   151 VanalqikAWLEDL--LEGDDVVLAAlpLFHVFGLTVA-LLLPLALGATIVLIP---RFRPIGVLKEIRKHRVTIfPGVP 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1772 TVfFNELSTS--LTKLDsekIRSLRFIIMGGEAASTNAIRSWQNTFknQVQLVNEYGPTEATvsamyyfiPV-----LEG 1844
Cdd:cd05936   225 TM-YIALLNApeFKKRD---FSSLRLCISGGAPLPVEVAERFEELT--GVPIVEGYGLTETS--------PVvavnpLDG 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1845 ENNlLGSvpIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlyRTGDLVR 1924
Cdd:cd05936   291 PRK-PGS--IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL---------RTGDIGY 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1925 WLPNGNIEFMGRKdKQVKIR-GHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNKLAIHLSN 2000
Cdd:cd05936   359 MDEDGYFFIVDRK-KDMIIVgGFNVYPREVEEVLYEHPAVAEAAVVgvpDPYSGEAVKAFVVLKEGASLTEEEIIAFCRE 437

                         490       500
                  ....*....|....*....|....*.
gi 446581728 2001 VLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:cd05936   438 QLAGYKVPRQVEFRDELPKSAVGKIL 463
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 493-963 2.17e-50

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 188.50  E-value: 2.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRieyilkdsesqmiit 572
Cdd:cd17647    19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--------------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  573 kkeyrglverfaiHTIYLedfhyanSIENIASTHTIEDAAYII---------YTSGSTGLPKGVVVPHkgvVNLSYS--- 640
Cdd:cd17647    84 -------------QNIYL-------GVAKPRGLIVIRAAGVVVgpdsnptlsFTSGSEGIPKGVLGRH---FSLAYYfpw 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  641 VINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKE 720
Cdd:cd17647   141 MAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATT 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  721 MLLKLnsvKRLFVGGETLPAESVRKWQSkLGLKIPVLNAYGPTETTVCATMYEVN------GEIQKEISNIPIGKPIANS 794
Cdd:cd17647   221 PFPKL---HHAFFVGDILTKRDCLRLQT-LAENVRIVNMYGTTETQRAVSYFEVPsrssdpTFLKNLKDVMPAGRGMLNV 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  795 EVFVISPFNT--LCPSGVVGELFIGGDGVANGYLN----QKEK-------TEGAFISLDKSYN----------RDKkMYC 851
Cdd:cd17647   297 QLLVVNRNDRtqICGIGEVGEIYVRAGGLAEGYRGlpelNKEKfvnnwfvEPDHWNYLDKDNNepwrqfwlgpRDR-LYR 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  852 TGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTyQNDK---------IVCFYLSKDNTELK 922
Cdd:cd17647   376 TGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLV-RRDKdeeptlvsyIVPRFDKPDDESFA 454

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581728  923 QEA-----------------------LKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLE 963
Cdd:cd17647   455 QEDvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 1544-2026 9.70e-50

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 186.53  E-value: 9.70e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1544 DRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRIN 1623
Cdd:TIGR03098   11 ARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1624 YIVRDSEACRIIT-SNKFKS------------HLNVSDYKVSIIEDIYRTTINDDVKILNK----------PDDLAYVIY 1680
Cdd:TIGR03098   91 HILADCNVRLLVTsSERLDLlhpalpgchdlrTLIIVGDPAHASEGHPGEEPASWPKLLALgdadpphpviDSDMAAILY 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1681 TSGSTGKPKGTLLTHKgvlNLVEWRNEV---FQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSdeqrYSTV-EY 1756
Cdd:TIGR03098  171 TSGSTGRPKGVVLSHR---NLVAGAQSVatyLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD----YLLPrDV 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1757 AQAIQETQAT-ISDLPTvffneLSTSLTKLD--SEKIRSLRFIIMGGEA---ASTNAIRSwqntFKNQVQLVNEYGPTEA 1830
Cdd:TIGR03098  244 LKALEKHGITgLAAVPP-----LWAQLAQLDwpESAAPSLRYLTNSGGAmprATLSRLRS----FLPNARLFLMYGLTEA 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1831 TVSAmyYFIPvlegenNLLGSVP--IGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPF 1908
Cdd:TIGR03098  315 FRST--YLPP------EEVDRRPdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPP 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1909 SEDNSKR---LYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAV---VTQTEGGMLLQAYYK 1982
Cdd:TIGR03098  387 FPGELHLpelAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVafgVPDPTLGQAIVLVVT 466

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 446581728  1983 TVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:TIGR03098  467 PPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKID 510
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1543-2041 2.04e-48

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 183.77  E-value: 2.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDR----QPERIAI-----ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPI 1613
Cdd:COG0365    15 LDRhaegRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1614 DVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKvSIIEDI------YRTTI-----NDDVKILN------------ 1670
Cdd:COG0365    95 FPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLK-EKVDEAleelpsLEHVIvvgrtGADVPMEGdldwdellaaas 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1671 --------KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNE-VFQISPNDKVtqFYS--------HSfdssvSEIF 1733
Cdd:COG0365   174 aefepeptDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVF--WCTadigwatgHS-----YIVY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1734 STLLNGAELYLLSDEQRYSTVE-YAQAIQETQATIsdL---PTVFfnelsTSLTKLDSEKIR-----SLRFIIMGGEAAS 1804
Cdd:COG0365   247 GPLLNGATVVLYEGRPDFPDPGrLWELIEKYGVTV--FftaPTAI-----RALMKAGDEPLKkydlsSLRLLGSAGEPLN 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1805 TNAIRSWQNTFKnqVQLVNEYGPTEaTVSAM---YYFIPVLEGEnnllgsvpIGIPISNTKVHILNSYMQYCPVGCMGEL 1881
Cdd:COG0365   320 PEVWEWWYEAVG--VPIVDGWGQTE-TGGIFisnLPGLPVKPGS--------MGKPVPGYDVAVVDEDGNPVPPGEEGEL 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1882 YIES--LGLAQGYWKQKEKTKQAFisnpFSEDnsKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQ 1959
Cdd:COG0365   389 VIKGpwPGMFRGYWNDPERYRETY----FGRF--PGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVS 462

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1960 LEGISQAVVT---QTEGGMLLQAYYKTVDGIGIE---KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKI 2033
Cdd:COG0365   463 HPAVAEAAVVgvpDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542


                  ....*...
gi 446581728 2034 EFGHEQKD 2041
Cdd:COG0365   543 AEGRPLGD 550
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 486-962 2.51e-48

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 181.74  E-value: 2.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  486 IAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDS 565
Cdd:cd05926     6 LVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  566 ESQMIITKKEYRGLVERFAIHT-IYLEDFHY----------ANSIENIASTHTI---------EDAAYIIYTSGSTGLPK 625
Cdd:cd05926    86 GSKLVLTPKGELGPASRAASKLgLAILELALdvgvlirapsAESLSNLLADKKNaksegvplpDDLALILHTSGTTGRPK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  626 GVVVPHKGVVNLSYSVINTFHLGKEDvflqfATIIfdasIMEIF----------PILLCGGRMHLiseIEKRSAEEFINV 695
Cdd:cd05926   166 GVPLTHRNLAASATNITNTYKLTPDD-----RTLV----VMPLFhvhglvasllSTLAAGGSVVL---PPRFSASTFWPD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  696 SQKYGIT--NVVlPTAFFKLIADMPKEMLLKLNSVKrlFV--GGETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCATM 771
Cdd:cd05926   234 VRDYNATwyTAV-PTIHQILLNRPEPNPESPPPKLR--FIrsCSASLPPAVLEALEATFG--APVLEAYGMTEAAHQMTS 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  772 YEVNGEIQKEISnipIGKPiANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTegafisldKSYNRDKKMYC 851
Cdd:cd05926   309 NPLPPGPRKPGS---VGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEAN--------AEAAFKDGWFR 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  852 TGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALK 927
Cdd:cd05926   377 TGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKygeeVAAAVVLREGASVTEEELR 456

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 446581728  928 TFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05926   457 AFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 1533-2025 3.51e-48

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 181.64  E-value: 3.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1533 QNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIP 1612
Cdd:PRK07656    5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1613 IDVKYPEDRINYIVRDSEACRIITSNKF-------KSHLNVSDYKVSI------IEDIYRTTINDDVKILN--------K 1671
Cdd:PRK07656   85 LNTRYTADEAAYILARGDAKALFVLGLFlgvdysaTTRLPALEHVVICeteeddPHTEKMKTFTDFLAAGDpaerapevD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 PDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQF--YSHSFDSSVSeIFSTLLNGAELYLLSdeq 1749
Cdd:PRK07656  165 PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAAnpFFHVFGYKAG-VNAPLMRGATILPLP--- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1750 RYSTVEYAQAIQETQATI-SDLPTVFFNELSTslTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFknQVQLVNE-YGP 1827
Cdd:PRK07656  241 VFDPDEVFRLIETERITVlPGPPTMYNSLLQH--PDRSAEDLSSLRLAVTGAASMPVALLERFESEL--GVDIVLTgYGL 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1828 TEAtvSAMYYFIPVLEGENNLLGSvpIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnp 1907
Cdd:PRK07656  317 SEA--SGVTTFNRLDDDRKTVAGT--IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI---- 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1908 fseDNSKRLYrTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTV 1984
Cdd:PRK07656  389 ---DADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgvpDERLGEVGKAYVVLK 464

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 446581728 1985 DGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK07656  465 PGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKV 505
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 492-957 1.25e-47

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 179.33  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  492 DQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII 571
Cdd:cd05911     8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  572 TKKE----YRGLVERFAIHT-IYLEDFH--YANSIENIASTH--------------TIEDAAYIIYTSGSTGLPKGVVVP 630
Cdd:cd05911    88 TDPDglekVKEAAKELGPKDkIIVLDDKpdGVLSIEDLLSPTlgeededlppplkdGKDDTAAILYSSGTTGLPKGVCLS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  631 HKGVVNLSYSVINTF--HLGKEDVFLQFATI--IFDASIMEIFPilLCGGRMHLISeieKRSAEEFINVSQKYGITNVVL 706
Cdd:cd05911   168 HRNLIANLSQVQTFLygNDGSNDVILGFLPLyhIYGLFTTLASL--LNGATVIIMP---KFDSELFLDLIEKYKITFLYL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  707 PTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKIpVLNAYGPTETTVCATMYevngeiqKEISNIP 786
Cdd:cd05911   243 VPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNAT-IKQGYGMTETGGILTVN-------PDGDDKP 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  787 --IGKPIANSEVFVISP-FNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKM-YCTGDLVRLLANG 862
Cdd:cd05911   315 gsVGRLLPNVEAKIVDDdGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF---------DEDGwLHTGDIGYFDEDG 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  863 NLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFm 938
Cdd:cd05911   386 YLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIgipdEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASY- 464

                         490       500
                  ....*....|....*....|....
gi 446581728  939 mpnY-----IFHLESFPVSPSGKL 957
Cdd:cd05911   465 ---KqlrggVVFVDEIPKSASGKI 485
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 486-962 6.44e-47

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 175.94  E-value: 6.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  486 IAISMGDQSITYYELQQRSNQIVNYL-RENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKD 564
Cdd:cd05941     3 IAIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  565 SESQMIItkkeyrglverfaihtiyledfhyansieniasthtieDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINT 644
Cdd:cd05941    83 SEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  645 FHLGKEDVFLQFATI-----IFDASIMEifpiLLCGGRMHLISeieKRSAEEFINVSQKYGITnvVL---PTAFFKLIAD 716
Cdd:cd05941   125 WRWTEDDVLLHVLPLhhvhgLVNALLCP----LFAGASVEFLP---KFDPKEVAISRLMPSIT--VFmgvPTIYTRLLQY 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  717 ---MPKEMLLKLNSVK---RLFVGGET-LPAESVRKWQSKLGLkiPVLNAYGPTETTVcATMYEVNGEiqkeisNIP--I 787
Cdd:cd05941   196 yeaHFTDPQFARAAAAerlRLMVSGSAaLPVPTLEEWEAITGH--TLLERYGMTEIGM-ALSNPLDGE------RRPgtV 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  788 GKPIANSEVFVISPFNT-LCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMYCTGDLVRLLANGNLEF 866
Cdd:cd05941   267 GMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF--------TDDGWFKTGDLGVVDEDGYYWI 338

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  867 IGR-KDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND---KIVCFY--LSKDNTELKQEALKTFLSESLPDFMMP 940
Cdd:cd05941   339 LGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPdwgERVVAVvvLRAGAAALSLEELKEWAKQRLAPYKRP 418

                         490       500
                  ....*....|....*....|..
gi 446581728  941 NYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05941   419 RRLILVDELPRNAMGKVNKKEL 440
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 496-962 9.00e-47

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 175.70  E-value: 9.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  496 TYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKE 575
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDGS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  576 yrglverfaihtiyledfhyansieniasthtiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQ 655
Cdd:cd05971    88 ---------------------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLY 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  656 FATI-------IFDAsimeIFPILLCGgrMHLIS-EIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNS 727
Cdd:cd05971   135 WTPAdwawiggLLDV----LLPSLYFG--VPVLAhRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  728 VKRLFVGGETLPAESVrKWqSKLGLKIPVLNAYGPTETTVCATmyevNGEIQKEISNIPIGKPIANSEVFVISPFNTLCP 807
Cdd:cd05971   209 LRAIATGGESLGEELL-GW-AREQFGVEVNEFYGQTECNLVIG----NCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLP 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  808 SGVVGELFIG-GDGVAN-GYLNQKEKTEGAFISldksynrdkKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDE 885
Cdd:cd05971   283 PGEVGEIAVElPDPVAFlGYWNNPSATEKKMAG---------DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAE 353

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  886 IEGTLFKHPEVRDAVVFTYQND---KIVCFYLSKDNTELKQEALKTFLSE----SLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:cd05971   354 IEECLLKHPAVLMAAVVGIPDPirgEIVKAFVVLNPGETPSDALAREIQElvktRLAAHEYPREIEFVNELPRTATGKIR 433


                  ....
gi 446581728  959 RKKL 962
Cdd:cd05971   434 RREL 437
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 470-962 1.56e-46

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 177.02  E-value: 1.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  470 TLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPI 549
Cdd:PRK07656    6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  550 DPKFPEKRIEYILKDSESQMIITKKEYRGL----------VER-----------FAIHTIYLEDFHYANSIENIASTHTI 608
Cdd:PRK07656   86 NTRYTADEAAYILARGDAKALFVLGLFLGVdysattrlpaLEHvviceteeddpHTEKMKTFTDFLAAGDPAERAPEVDP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKED-------VFLQFA-TIIFDASIME---IFPILlcggr 677
Cdd:PRK07656  166 DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylaanpFFHVFGyKAGVNAPLMRgatILPLP----- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  678 mhliseieKRSAEEFINVSQKYGITnvVL---PTAFFKLIaDMPKEMLLKLNSVkRLFV-GGETLPAESVRKWQSKLGLK 753
Cdd:PRK07656  241 --------VFDPDEVFRLIETERIT--VLpgpPTMYNSLL-QHPDRSAEDLSSL-RLAVtGAASMPVALLERFESELGVD 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  754 IpVLNAYGPTETTVCATMYEVNGEiQKEISNiPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTE 833
Cdd:PRK07656  309 I-VLTGYGLSEASGVTTFNRLDDD-RKTVAG-TIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATA 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  834 GAfisLDKsynrDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI---- 909
Cdd:PRK07656  386 AA---IDA----DGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLgevg 457

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446581728  910 VCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK07656  458 KAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 503-963 4.45e-46

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 174.17  E-value: 4.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  503 RSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGG----VYVPIDPKFPEKRIEYILKDSESQMIITKKeyrG 578
Cdd:cd05922     2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADA---G 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  579 LVERFAIHTIYLEDFHYANSIENI------ASTHTI--EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKE 650
Cdd:cd05922    79 AADRLRDALPASPDPGTVLDADGIraarasAPAHEVshEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  651 DVFLQFATIIFDASIMEIFPILLCGGRmhLISEIEKRSAEEFINVSQKYGITNV--VLPTAFFKLIADMPKEmllKLNSV 728
Cdd:cd05922   159 DRALTVLPLSYDYGLSVLNTHLLRGAT--LVLTNDGVLDDAFWEDLREHGATGLagVPSTYAMLTRLGFDPA---KLPSL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  729 KRLFVGGETLPAESVRKWQSKL-GLKIPVLnaYGPTETTvcATMYEVNGEiqkEISNIP--IGKPIANSEVFVISPFNTL 805
Cdd:cd05922   234 RYLTQAGGRLPQETIARLRELLpGAQVYVM--YGQTEAT--RRMTYLPPE---RILEKPgsIGLAIPGGEFEILDDDGTP 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  806 CPSGVVGELFIGGDGVANGYLN--QKEKTEGAFISLdksynrdkkMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIEL 883
Cdd:cd05922   307 TPPGEPGEIVHRGPNVMKGYWNdpPYRRKEGRGGGV---------LH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISP 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  884 DEIEGTLFKHPEVRDAVVF---TYQNDKIVCFYLSKDNTELKqeALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRK 960
Cdd:cd05922   377 TEIEAAARSIGLIIEAAAVglpDPLGEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYA 454


                  ...
gi 446581728  961 KLE 963
Cdd:cd05922   455 ALR 457
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1099-1498 6.33e-46

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 172.77  E-value: 6.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1099 VYDTPLHIYIEPS-------LNKDILQDTIRFLVERHEMLRTVFI-ERNGEPRQVILNSIAIDLIHDEIEHMSKKEQQEY 1170
Cdd:cd19543    16 LLDPGSGAYVEQMvitlegpLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWRELDLSHLSEAEQEAE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1171 IRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTIsNRYVD 1250
Cdd:cd19543    96 LEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPV-RPYRD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1251 YAEWeqvqlnLGRWDTE--KSYW---MAELAAPLPILNLPLDfsRNRQSTNKGTVFEmKLDNEMKESLKQVCEQENISMY 1325
Cdd:cd19543   175 YIAW------LQRQDKEaaEAYWreyLAGFEEPTPLPKELPA--DADGSYEPGEVSF-ELSAELTARLQELARQHGVTLN 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1326 MLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQ--EFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYP 1403
Cdd:cd19543   246 TVVQGAWALLLSRYSGRDDVVFGTTVSGRPAElpGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHEYVP 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1404 FdkvieqinPD---RSFGNNPIFSTMFSYQ-----KDILQQHDAYKLQLLP-NKQDISKFDISLAVEEGlDYVGISFEYD 1474
Cdd:cd19543   326 L--------YEiqaWSEGKQALFDHLLVFEnypvdESLEEEQDEDGLRITDvSAEEQTNYPLTVVAIPG-EELTIKLSYD 396

                         410       420
                  ....*....|....*....|....
gi 446581728 1475 INLFKEESINRFTQNLLNILDAFI 1498
Cdd:cd19543   397 AEVFDEATIERLLGHLRRVLEQVA 420
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 17-437 6.43e-46

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 172.59  E-value: 6.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   17 TVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVE-FDIPIKDL 95
Cdd:cd19066     5 SPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVrFRIEIIDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   96 TafKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKSN 175
Cdd:cd19066    85 R--NLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKPT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  176 V-EFESPYKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFAKKN 254
Cdd:cd19066   163 LpPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARES 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  255 NISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAITYK 334
Cdd:cd19066   243 GTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEHQ 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  335 HNSYSHIVKDLNLNTNTNHNMVYSTAFNTMKIPE--LKIPD---IESTVLTDCKRVNPFNmtwrIMRYEGET-ENKIEVD 408
Cdd:cd19066   323 RVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQqlGKTGGfifTTPVYTSSEGTVFDLD----LEASEDPDgDLLLRLE 398

                         410       420
                  ....*....|....*....|....*....
gi 446581728  409 YNSALYKPESISDLVERYIYLLQKLMKNV 437
Cdd:cd19066   399 YSRGVYDERTIDRFAERYMTALRQLIENP 427
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 19-436 2.21e-45

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 171.29  E-value: 2.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   19 GQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIPIkdltaf 98
Cdd:cd19538     7 AQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL------ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   99 kntEQKSILKNFLESIVNE----KFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKS 174
Cdd:cd19538    81 ---EIKEVDEEELESEINEavryPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  175 NVEFESPYK------------NLVKHEESFIDSAIykegsSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSD 242
Cdd:cd19538   158 PELAPLPVQyadyalwqqellGDESDPDSLIARQL-----AYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  243 LFYQIQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNK 322
Cdd:cd19538   233 LHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLER 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  323 VNKSIHLAITYKHNSYSHIVKdlnlNTNTNHNMVYSTAFNTMKI------PELKIPDIESTVL----TDCKrvnpFNMTW 392
Cdd:cd19538   313 VKETNLEAYEHQDIPFERLVE----ALNPTRSRSRHPLFQIMLAlqntpqPSLDLPGLEAKLElrtvGSAK----FDLTF 384

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 446581728  393 RIM-RYEGETENKIE--VDYNSALYKPESISDLVERYIYLLQKLMKN 436
Cdd:cd19538   385 ELReQYNDGTPNGIEgfIEYRTDLFDHETIEALAQRYLLLLESAVEN 431
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 496-962 6.87e-45

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 169.83  E-value: 6.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  496 TYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITkke 575
Cdd:cd05972     2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  576 yrglverfaihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVPHK---GVVNLSYSVINtfhLGKEDV 652
Cdd:cd05972    79 -------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLG---LRPDDI 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  653 FLQFATI--IFDASIMEIFPILLcgGRMHLISEIEKRSAEEFINVSQKYGITNVVL-PTAFFKLIADMPKEmlLKLNSVK 729
Cdd:cd05972   125 HWNIADPgwAKGAWSSFFGPWLL--GATVFVYEGPRFDAERILELLERYGVTSFCGpPTAYRMLIKQDLSS--YKFSHLR 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  730 RLFVGGETLPAESVRKWQSKLGLkiPVLNAYGPTETTVCATMYevngeiqkeiSNIPI-----GKPIANSEVFVISPFNT 804
Cdd:cd05972   201 LVVSAGEPLNPEVIEWWRAATGL--PIRDGYGQTETGLTVGNF----------PDMPVkpgsmGRPTPGYDVAIIDDDGR 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  805 LCPSGVVGELFI--GGDGVANGYLNQKEKTEgAFISLDksynrdkkMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIE 882
Cdd:cd05972   269 ELPPGEEGDIAIklPPPGLFLGYVGDPEKTE-ASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIG 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  883 LDEIEGTLFKHPEVRDAVVFTYQND---KIVCFYLS-----KDNTELKQEaLKTFLSESLPDFMMPNYIFHLESFPVSPS 954
Cdd:cd05972   340 PFEVESALLEHPAVAEAAVVGSPDPvrgEVVKAFVVltsgyEPSEELAEE-LQGHVKKVLAPYKYPREIEFVEELPKTIS 418


                  ....*...
gi 446581728  955 GKLDRKKL 962
Cdd:cd05972   419 GKIRRVEL 426
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 483-962 1.27e-44

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 171.01  E-value: 1.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITKKEyrgLVERFAI------HTIY----------------LEDFHYANS-IENIASTHTiEDAAYIIYTSG 619
Cdd:cd05959    98 EDSRARVVVVSGE---LAPVLAAaltkseHTLVvlivsggagpeagallLAELVAAEAeQLKPAATHA-DDPAFWLYSSG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  620 STGLPKGVVVPHKgvvNLSYS----VINTFHLGKEDVFLQFATIIF-----DASImeiFPiLLCGGRMHLISE------I 684
Cdd:cd05959   174 STGRPKGVVHLHA---DIYWTaelyARNVLGIREDDVCFSAAKLFFayglgNSLT---FP-LSVGATTVLMPErptpaaV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  685 EKRSAEEfiNVSQKYGitnvvLPTAFFKLIAD--MPKEMLLKLnsvkRLFV-GGETLPAESVRKWQSKLGLKIpvLNAYG 761
Cdd:cd05959   247 FKRIRRY--RPTVFFG-----VPTLYAAMLAApnLPSRDLSSL----RLCVsAGEALPAEVGERWKARFGLDI--LDGIG 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  762 PTEttvcatMYEVNgeiqkeISNIP-------IGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEG 834
Cdd:cd05959   314 STE------MLHIF------LSNRPgrvrygtTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRD 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  835 AFISldkSYNRdkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND----KIV 910
Cdd:cd05959   382 TFQG---EWTR------TGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEdgltKPK 452

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728  911 CFYLSK---DNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05959   453 AFVVLRpgyEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 496-962 1.88e-44

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 168.78  E-value: 1.88e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   496 TYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKe 575
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   576 yrgLVERFAIHTIYLEDFHYANSIE-NIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFL 654
Cdd:TIGR01923   80 ---LLEEKDFQADSLDRIEAAGRYEtSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   655 qFATIIFDASIMEI-FPILLCGGRMHLISEIEkrsaeEFINVSQKYGITNVVL-PTAFFKLI-ADMPKEMLlklnsvKRL 731
Cdd:TIGR01923  157 -LSLPLYHISGLSIlFRWLIEGATLRIVDKFN-----QLLEMIANERVTHISLvPTQLNRLLdEGGHNENL------RKI 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   732 FVGGETLPAESVRKWQSKlglKIPVLNAYGPTETtvCATMYEVNGEIQKEISNIpiGKPIANSEVFVISPfntlcPSGVV 811
Cdd:TIGR01923  225 LLGGSAIPAPLIEEAQQY---GLPIYLSYGMTET--CSQVTTATPEMLHARPDV--GRPLAGREIKIKVD-----NKEGH 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   812 GELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLF 891
Cdd:TIGR01923  293 GEIMVKGANLMKGYLYQGELTPAFE---------QQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLY 363

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728   892 KHPEVRDAVVFTYQNDKI----VCFYLSkdNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:TIGR01923  364 QHPGIQEAVVVPKPDAEWgqvpVAYIVS--ESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 1545-2026 3.78e-44

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 167.79  E-value: 3.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:cd17631     7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEAcriitsnkfkshlnvsdyKVSIiediyrttinddvkilnkpDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEW 1704
Cdd:cd17631    87 ILADSGA------------------KVLF-------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVN 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1705 RNEVFQISPNDK--VTQFYSHSFDSSVSeIFSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATISDLPTVFFNELSTSl 1782
Cdd:cd17631   130 ALAALDLGPDDVllVVAPLFHIGGLGVF-TLPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTMIQALLQH- 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1783 TKLDSEKIRSLRFIIMGGEAASTNAIRSWQntfKNQVQLVNEYGPTEatvsaMYYFIPVLEGENNL--LGSVpiGIPISN 1860
Cdd:cd17631   205 PRFATTDLSSLRAVIYGGAPMPERLLRALQ---ARGVKFVQGYGMTE-----TSPGVTFLSPEDHRrkLGSA--GRPVFF 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1861 TKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpfsednSKRLYRTGDLVRWLPNGNIEFMGRKDKQ 1940
Cdd:cd17631   275 VEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF---------RDGWFHTGDLGRLDEDGYLYIVDRKKDM 345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1941 VKIRGHRIELGEIEDAMLQLEGISQAVV------TQTEGGMllqAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHV 2014
Cdd:cd17631   346 IISGGENVYPAEVEDVLYEHPAVAEVAVigvpdeKWGEAVV---AVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFV 422

                         490
                  ....*....|..
gi 446581728 2015 LEIPITANGKID 2026
Cdd:cd17631   423 DALPRNATGKIL 434
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
475-962 4.09e-44

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 169.27  E-value: 4.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLR-ENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKF 553
Cdd:PRK06839    8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  554 PEKRIEYILKDSESQMIITKKEYRGLVER-----FAIHTIYLEDFHYANSIENIASTHTIEDAAYII-YTSGSTGLPKGV 627
Cdd:PRK06839   88 TENELIFQLKDSGTTVLFVEKTFQNMALSmqkvsYVQRVISITSLKEIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  628 VVPHkgvVNLSYSVIN---TFHLGKEDVFLQFATIIFDASI-MEIFPILLCGGRMHLISEIEKRSAEEFInvsQKYGITN 703
Cdd:PRK06839  168 VLTQ---ENMFWNALNntfAIDLTMHDRSIVLLPLFHIGGIgLFAFPTLFAGGVIIVPRKFEPTKALSMI---EKHKVTV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  704 VVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKlGLkiPVLNAYGPTETTVCATMYEVNGEIQKEIS 783
Cdd:PRK06839  242 VMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GF--LFGQGFGMTETSPTVFMLSEEDARRKVGS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  784 nipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDkKMYCTGDLVRLLANGN 863
Cdd:PRK06839  319 ---IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI--------QD-GWLCTGDLARVDEDGF 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  864 LEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLPDFMM 939
Cdd:PRK06839  387 VYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKwgeiPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKI 466

                         490       500
                  ....*....|....*....|...
gi 446581728  940 PNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK06839  467 PKEIVFLKELPKNATGKIQKAQL 489
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
 2164-2428 3.17e-43

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 160.61  E-value: 3.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2164 VFLTGATGYLGAHILERLLQLPSTtIYCLVRENEDqvigAKLKERMEFyfgkeiLQKLKERVELIEGDLSLMNLGLDSKQ 2243
Cdd:cd05263     1 VFVTGGTGFLGRHLVKRLLENGFK-VLVLVRSESL----GEAHERIEE------AGLEADRVRVLEGDLTQPNLGLSAAA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2244 LDHLKKNVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGqaerdPKEFEFFESDFDRGQ 2322
Cdd:cd05263    70 SRELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIqRFHYVSTAYVAG-----NREGNIRETELNPGQ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2323 NLDNLYLESKFQGEKMVREAMEKgVRATIYRVGNLVGNSKTG---KFQYninenaFYRLLKGICLSSIAP----DVNTYV 2395
Cdd:cd05263   145 NFKNPYEQSKAEAEQLVRAAATQ-IPLTVYRPSIVVGDSKTGrieKIDG------LYELLNLLAKLGRWLpmpgNKGARL 217

                         250       260       270
                  ....*....|....*....|....*....|...
gi 446581728 2396 DLTPVDYGSLAITELSYKANTVNKTMHICNPNQ 2428
Cdd:cd05263   218 NLVPVDYVADAIVYLSKKPEANGQIFHLTDPTP 250
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 16-436 3.41e-43

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 164.86  E-value: 3.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   16 VTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKI-KQLIQKNVEFDIPIKD 94
Cdd:cd19539     4 LSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVpRQEILPPGPAPLEVRD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   95 LTAfKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGK- 173
Cdd:cd19539    84 LSD-PDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPa 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  174 SNV-EFESPYKNLVKHEESFIDSAIYKEGSSYWKDYLQGeLTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFAK 252
Cdd:cd19539   163 APLpELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  253 KNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAIT 332
Cdd:cd19539   242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  333 YKHNSYSHIVKDLNLNTNTNHNMVYSTAFNTMKIPELKIP-----------DIESTVLTDckrvnpFNMTWRimryEGET 401
Cdd:cd19539   322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELElagglsytegsDIPDGAKFD------LNLTVT----EEGT 391

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 446581728  402 ENKIEVDYNSALYKPESISDLVERYIYLLQKLMKN 436
Cdd:cd19539   392 GLRGSLGYATSLFDEETIQGFLADYLQVLRQLLAN 426
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 494-962 8.50e-43

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 163.71  E-value: 8.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  494 SITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITK 573
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  574 KEYRGlverfaihtiyledfhyaNSIENIAsthtiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVF 653
Cdd:cd05903    81 ERFRQ------------------FDPAAMP-----DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  654 LQFATII-FDASIMEIFPILLCGGRMHLISEIEKRSAEEFINvsqKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLF 732
Cdd:cd05903   138 LVASPMAhQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMR---EHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFV 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  733 VGGETLPAESVRKWQSKLGLKipVLNAYGPTETTVCATMYEVNGEIQKEISNipiGKPIANSEVFVISPFNTLCPSGVVG 812
Cdd:cd05903   215 CGGATVPRSLARRAAELLGAK--VCSAYGSTECPGAVTSITPAPEDRRLYTD---GRPLPGVEIKVVDDTGATLAPGVEG 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  813 ELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKMYCTGDLVRLLANGNLEFIGR-KDnqVKIR-GYRIELDEIEGTL 890
Cdd:cd05903   290 ELLSRGPSVFLGYLDRPDLTADAA---------PEGWFRTGDLARLDEDGYLRITGRsKD--IIIRgGENIPVLEVEDLL 358

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728  891 FKHPEVRDAVVFTYQNDKI---VCFYLS-KDNTELKQEALKTFLS-ESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05903   359 LGHPGVIEAAVVALPDERLgerACAVVVtKSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1568-2030 3.82e-42

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 162.61  E-value: 3.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1568 SNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAA----YIPIDVKYPEDRINYIVRDSEACRIITSNKFKSH 1643
Cdd:cd05922     3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1644 LNV-----SDYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVT 1718
Cdd:cd05922    83 LRDalpasPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1719 QFYSHSFDSSVSEIFSTLLNGAEL-----YLLSDeqrystvEYAQAIQETQAT-ISDLPTVFfnELSTSLTkLDSEKIRS 1792
Cdd:cd05922   163 TVLPLSYDYGLSVLNTHLLRGATLvltndGVLDD-------AFWEDLREHGATgLAGVPSTY--AMLTRLG-FDPAKLPS 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1793 LRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATvSAMYYFIPVLEGENnlLGSvpIGIPISNTKVHILNSYMQY 1872
Cdd:cd05922   233 LRYLTQAGGRLPQETIARLRELLPG-AQVYVMYGQTEAT-RRMTYLPPERILEK--PGS--IGLAIPGGEFEILDDDGTP 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1873 CPVGCMGELYIESLGLAQGYWKQKektkqafiSNPFSEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGE 1952
Cdd:cd05922   307 TPPGEPGEIVHRGPNVMKGYWNDP--------PYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTE 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1953 IEDAMLQLEGISQAVVTQTE--GGMLLQAYYKTVDgiGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKL 2030
Cdd:cd05922   379 IEAAARSIGLIIEAAAVGLPdpLGEKLALFVTAPD--KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1529-2026 5.04e-42

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 163.43  E-value: 5.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1529 YPYFQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGA 1608
Cdd:PRK06187    2 QDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1609 AYIPIDVKYPEDRINYIVRDSEACRIITSNKFKSHL--------NVSDY-------------KVSIIEDIYRTTINDDVK 1667
Cdd:PRK06187   82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLaailpqlpTVRTVivegdgpaaplapEVGEYEELLAAASDTFDF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1668 ILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK----VTQFysHSFDSSVSeiFSTLLNGAELY 1743
Cdd:PRK06187  162 PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVylviVPMF--HVHAWGLP--YLALMAGAKQV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1744 LLsdeQRYSTVEYAQAIQETQATISDL-PTVFfNELSTSLTKlDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKnqVQLV 1822
Cdd:PRK06187  238 IP---RRFDPENLLDLIETERVTFFFAvPTIW-QMLLKAPRA-YFVDFSSLRLVIYGGAALPPALLREFKEKFG--IDLV 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1823 NEYGPTEAT-VSAMYYFIPVLEGENNLLGSVpiGIPISNTKVHILNSYMQYCPV--GCMGELYIESLGLAQGYWKQKEKT 1899
Cdd:PRK06187  311 QGYGMTETSpVVSVLPPEDQLPGQWTKRRSA--GRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEAT 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1900 KQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT----QTEGGM 1975
Cdd:PRK06187  389 AETIDGG---------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgvpdEKWGER 459

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446581728 1976 LLqAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:PRK06187  460 PV-AVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKIL 509
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 1549-2030 7.68e-42

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 161.09  E-value: 7.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1549 RIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRD 1628
Cdd:cd05919     1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1629 SEACRIITSNkfkshlnvsdykvsiiediyrttinddvkilnkpDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVE-WRNE 1707
Cdd:cd05919    81 CEARLVVTSA----------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADaMARE 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1708 VFQISPNDKV----TQFYSHSFDSSVseiFSTLLNGAELYLlsdeqrYSTVEYAQAIQETQATISdlPTVFFNELSTSLT 1783
Cdd:cd05919   127 ALGLTPGDRVfssaKMFFGYGLGNSL---WFPLAVGASAVL------NPGWPTAERVLATLARFR--PTVLYGVPTFYAN 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1784 KLDS-----EKIRSLRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTEatvsAMYYFIPVLEGENNlLGSVpiGIPI 1858
Cdd:cd05919   196 LLDScagspDALRSLRLCVSAGEALPRGLGERWMEHFG--GPILDGIGATE----VGHIFLSNRPGAWR-LGST--GRPV 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1859 SNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKD 1938
Cdd:cd05919   267 PGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG---------WYRTGDKFCRDADGWYTHAGRAD 337

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1939 KQVKIRGHRIELGEIEDAMLQLEGISQAVVTQT---EGGMLLQAYYKTVDGIGIEK---NKLAIHLSNVLPEYMVPKYYS 2012
Cdd:cd05919   338 DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVpesTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIA 417

                         490
                  ....*....|....*...
gi 446581728 2013 HVLEIPITANGKIDFEKL 2030
Cdd:cd05919   418 FVDELPRTATGKLQRFKL 435
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1078-1501 8.79e-42

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 160.23  E-value: 8.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1078 YQLSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIA-----I 1152
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPvpirhI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1153 DLIHDEIEHmskKEQQEYIRTTINQtdhtPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSA 1232
Cdd:cd19533    82 DLSGDPDPE---GAAQQWMQEDLRK----PLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1233 FAKRRNPElPTISNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPilnlPLDFSRNRQST-NKGTVFEMKLDNEMKE 1311
Cdd:cd19533   155 LLKGRPAP-PAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPE----PVSLARRAPGRsLAFLRRTAELPPELTR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1312 SLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVRE 1391
Cdd:cd19533   230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1392 KCLNSFQNQSYPFDKVIEQINpdRSFGNNPIFSTMFSYQKDILQQHDAYKLQLLPNKQDISKFDISLAVEEGLDYVGISF 1471
Cdd:cd19533   310 ELRSLLRHQRYRYEDLRRDLG--LTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSIFVYDRDDESGLRI 387

                         410       420       430
                  ....*....|....*....|....*....|..
gi 446581728 1472 EYDIN--LFKEESINRFTQNLLNILDAFIHQR 1501
Cdd:cd19533   388 DFDANpaLYSGEDLARHQERLLRLLEEAAADP 419
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 1548-2026 2.97e-41

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 159.38  E-value: 2.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1548 ERIAIATATESLTYRQLNMSSNQVAQHLLEKG-IKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIItsnkfkshlnvsdykvsiiediyrttinddvkilnkpdDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRN 1706
Cdd:cd05941    81 TDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKVTQ----FYSHSFdssVSEIFSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATI-SDLPTVF------F 1775
Cdd:cd05941   123 DAWRWTEDDVLLHvlplHHVHGL---VNALLCPLFAGASVEFLP---KFDPKEVAISRLMPSITVfMGVPTIYtrllqyY 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1776 NELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqvQLVNEYGPTEatvSAMYYFIPvLEGEnNLLGSVpiG 1855
Cdd:cd05941   197 EAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGH--TLLERYGMTE---IGMALSNP-LDGE-RRPGTV--G 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1856 IPISNTKVHIL-NSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFM 1934
Cdd:cd05941   268 MPLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTGDLGVVDEDGYYWIL 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1935 GR-KDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIG-IEKNKLAIHLSNVLPEYMVPK 2009
Cdd:cd05941   340 GRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIgvpDPDWGERVVAVVVLRAGAAaLSLEELKEWAKQRLAPYKRPR 419

                         490
                  ....*....|....*..
gi 446581728 2010 YYSHVLEIPITANGKID 2026
Cdd:cd05941   420 RLILVDELPRNAMGKVN 436
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 492-962 9.12e-41

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 158.01  E-value: 9.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  492 DQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII 571
Cdd:cd05919     8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  572 TKKEyrglverfaihtiyledfhyansieniasthtieDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSV-INTFHLGKE 650
Cdd:cd05919    88 TSAD----------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  651 DVFLQFATIIFDASIME--IFPiLLCGGRMHLISEieKRSAEEFINVSQKYGITnvVL---PTAFFKLI--ADMPKEMLL 723
Cdd:cd05919   134 DRVFSSAKMFFGYGLGNslWFP-LAVGASAVLNPG--WPTAERVLATLARFRPT--VLygvPTFYANLLdsCAGSPDALR 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  724 KLnsvkRLFV-GGETLPAESVRKWQSKLGlkIPVLNAYGPTETtvcatmyevngeIQKEISNIP-------IGKPIANSE 795
Cdd:cd05919   209 SL----RLCVsAGEALPRGLGERWMEHFG--GPILDGIGATEV------------GHIFLSNRPgawrlgsTGRPVPGYE 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  796 VFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVK 875
Cdd:cd05919   271 IRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF---------NGGWYRTGDKFCRDADGWYTHAGRADDMLK 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  876 IRGYRIELDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKD---NTELKQEALKTFLSESLPDFMMPNYIFHLES 948
Cdd:cd05919   342 VGGQWVSPVEVESLIIQHPAVAEAAVVAVPEStglsRLTAFVVLKSpaaPQESLARDIHRHLLERLSAHKVPRRIAFVDE 421

                         490
                  ....*....|....
gi 446581728  949 FPVSPSGKLDRKKL 962
Cdd:cd05919   422 LPRTATGKLQRFKL 435
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 40-340 2.13e-40

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 156.21  E-value: 2.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   40 IIIKLKGNLQIEVLKKALTTIVQSHPALRTIF-KKRDEKIKQLIQKNVEFDIPIKDLTAFKNTEQKSILKNFLESIVNEK 118
Cdd:cd19543    28 MVITLEGPLDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLQVVLKDRKLPWRELDLSHLSEAEQEAELEALAEEDRERG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  119 FSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGK-SNVEFESPYKNLVK------HEES 191
Cdd:cd19543   108 FDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQpPSLPPVRPYRDYIAwlqrqdKEAA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  192 fidsaiykegSSYWKDYLQGELTPTEFPIDFNKMNEKRYTDKNISKNINSDLFYQIQCFAKKNNISIYRVMLSTYCTLLH 271
Cdd:cd19543   188 ----------EAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLS 257

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446581728  272 QMTNAEEIIVGIPINTRPyTE----ERnTFGYFVNTLPIRITIEKGETFKGILNKVNKSiHLAItykhNSYSH 340
Cdd:cd19543   258 RYSGRDDVVFGTTVSGRP-AElpgiET-MVGLFINTLPVRVRLDPDQTVLELLKDLQAQ-QLEL----REHEY 323
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1078-1498 5.68e-40

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 154.91  E-value: 5.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1078 YQLSSAQKRIWFLNKYNAINRVYdtpLHIY---IEPSLNKDILQDTIRFLVERHEMLRTVFIERN-GEPRQVILNSIAID 1153
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVY---LHNYtytVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1154 LIHDEIEHMSKKEQQeyIRTTINQTDHTPFDLEKGPLFRIRIFNLNKKKSYLY-INLHHIITDEWSVRNLLDELMKVYSA 1232
Cdd:cd19536    79 VTELDLTPLEEQLDP--LRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1233 FAKRRNPELPTISNrYVDYAEWEQVQLnlgrwDTEKS--YWMAELA----APLPILNLPLDFSRNRQStnkgtvfEMKLD 1306
Cdd:cd19536   157 LLEYKPLSLPPAQP-YRDFVAHERASI-----QQAASerYWREYLAgatlATLPALSEAVGGGPEQDS-------ELLVS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1307 NEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNhQEF---EKIQGFFVNTLAIRTQLNDvKNLT 1383
Cdd:cd19536   224 VPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRS-EETtgaERLLGLFLNTLPLRVTLSE-ETVE 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1384 QLLQVVREKCLNSFQNQSYPfdkvIEQINPDRSfgNNPIFSTMFSYQKDILQQ------HDAYKLQLLPNKQDISKFDIS 1457
Cdd:cd19536   302 DLLKRAQEQELESLSHEQVP----LADIQRCSE--GEPLFDSIVNFRHFDLDFglpewgSDEGMRRGLLFSEFKSNYDVN 375

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 446581728 1458 LAVEEGLDYVGISFEYDINLFKEESINRFTQNLLNILDAFI 1498
Cdd:cd19536   376 LSVLPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELA 416
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1560-2025 1.03e-39

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 154.37  E-value: 1.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1560 TYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITsnk 1639
Cdd:cd05934     5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1640 fkshlnvsdykvsiiediyrttinddvkilnkpdDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK--V 1717
Cdd:cd05934    82 ----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVylT 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1718 TQFYSHSfDSSVSEIFSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATIsdlptvfFNELSTSLTKL----DSEKIRSL 1793
Cdd:cd05934   128 VLPLFHI-NAQAVSVLAALSVGATLVLLP---RFSASRFWSDVRRYGATV-------TNYLGAMLSYLlaqpPSPDDRAH 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1794 RFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTEATVsamyyfiPVL--EGENNLLGSvpIGIPISNTKVHILNSYMQ 1871
Cdd:cd05934   197 RLRAAYGAPNPPELHEEFEERFG--VRLLEGYGMTETIV-------GVIgpRDEPRRPGS--IGRPAPGYEVRIVDDDGQ 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1872 YCPVGCMGELYIESL---GLAQGYWKQKEKTKQAFiSNPFsednskrlYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRI 1948
Cdd:cd05934   266 ELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM-RNGW--------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENI 336

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1949 ELGEIEDAMLQLEGISQAVVTQT---EGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05934   337 SSAEVERAILRHPAVREAAVVAVpdeVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 1559-2055 3.71e-39

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 154.05  E-value: 3.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEAcriitsn 1638
Cdd:cd17640     6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1639 kfkshlnvsdyKVSIIEdiyrttinddvkilNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVT 1718
Cdd:cd17640    79 -----------VALVVE--------------NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1719 QFYS--HSFDSSVsEIFSTLLNGAELY-----LLSDEQRYSTVEYAQA--IQET-----QATISDLPTVFFNELSTSLTk 1784
Cdd:cd17640   134 SILPiwHSYERSA-EYFIFACGCSQAYtsirtLKDDLKRVKPHYIVSVprLWESlysgiQKQVSKSSPIKQFLFLFFLS- 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1785 ldsekIRSLRFIIMGGeaastNAIRSWQNTFKNQ--VQLVNEYGPTEATvsamyyfiPVL---EGENNLLGSVpiGIPIS 1859
Cdd:cd17640   212 -----GGIFKFGISGG-----GALPPHVDTFFEAigIEVLNGYGLTETS--------PVVsarRLKCNVRGSV--GRPLP 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1860 NTKVHILNSYMQ-YCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpfsedNSKRLYRTGDLVRWLPNGNIEFMGR-K 1937
Cdd:cd17640   272 GTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVL--------DSDGWFNTGDLGWLTCGGELVLTGRaK 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1938 DKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGML-------LQAYYKTVdgigieKNKLAIHLSNVLPEYMV 2007
Cdd:cd17640   344 DTIVLSNGENVEPQPIEEALMRSPFIEQIMVVgqdQKRLGALivpnfeeLEKWAKES------GVKLANDRSQLLASKKV 417

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 446581728 2008 PKYYS-HVLEIPITANGKIDFEKLPKIEFGHEQKDECKLKPQT-KVQKDI 2055
Cdd:cd17640   418 LKLYKnEIKDEISNRPGFKSFEQIAPFALLEEPFIENGEMTQTmKIKRNV 467
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 496-962 4.57e-39

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 153.04  E-value: 4.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  496 TYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKE 575
Cdd:cd05969     2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  576 yrgLVERfaihtiyledfhyansieniastHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFL- 654
Cdd:cd05969    82 ---LYER-----------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWc 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  655 ---------QFATIIfdASIMEIFPILLCGGRMhliseiekrSAEEFINVSQKYGITN-VVLPTAfFKLIADMPKEMLLK 724
Cdd:cd05969   136 tadpgwvtgTVYGIW--APWLNGVTNVVYEGRF---------DAESWYGIIERVKVTVwYTAPTA-IRMLMKEGDELARK 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  725 --LNSVKRLFVGGETLPAESVRkWQSKLgLKIPVLNAYGPTETtvcatmyevnGEIQkeISNIP--------IGKPIANS 794
Cdd:cd05969   204 ydLSSLRFIHSVGEPLNPEAIR-WGMEV-FGVPIHDTWWQTET----------GSIM--IANYPcmpikpgsMGKPLPGV 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  795 EVFVISPFNTLCPSGVVGELFIGGD--GVANGYLNQKEKTEGAFISldksynrdkKMYCTGDLVRLLANGNLEFIGRKDN 872
Cdd:cd05969   270 KAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFID---------GWYLTGDLAYRDEDGYFWFVGRADD 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  873 QVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN----DKIVCFY-LSKD---NTELKQEaLKTFLSESLPDFMMPNYIF 944
Cdd:cd05969   341 IIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDplrgEIIKAFIsLKEGfepSDELKEE-IINFVRQKLGAHVAPREIE 419

                         490
                  ....*....|....*...
gi 446581728  945 HLESFPVSPSGKLDRKKL 962
Cdd:cd05969   420 FVDNLPKTRSGKIMRRVL 437
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 1559-2025 1.06e-38

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 151.89  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSn 1638
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1639 kfkshlnvsdykvsiiEDIYRTTinddvkilnKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKvt 1718
Cdd:cd05969    80 ----------------EELYERT---------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDI-- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1719 qfYSHSFD-----SSVSEIFSTLLNGAELYllSDEQRYSTVEYAQAIQETQATI-SDLPTVFFNELSTSLTKLDSEKIRS 1792
Cdd:cd05969   133 --YWCTADpgwvtGTVYGIWAPWLNGVTNV--VYEGRFDAESWYGIIERVKVTVwYTAPTAIRMLMKEGDELARKYDLSS 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1793 LRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTE--ATVSAMYYFIPVLEGEnnllgsvpIGIPISNTKVHILNSYM 1870
Cdd:cd05969   209 LRFIHSVGEPLNPEAIRWGMEVFG--VPIHDTWWQTEtgSIMIANYPCMPIKPGS--------MGKPLPGVKAAVVDENG 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1871 QYCPVGCMGELYIES--LGLAQGYWKQKEKTKQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRI 1948
Cdd:cd05969   279 NELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDG---------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRV 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1949 ELGEIEDAMLQLEGISQAVVTQTEG---GMLLQAY------YKTVDGIGIE-----KNKLAIHLsnvlpeymVPKYYSHV 2014
Cdd:cd05969   350 GPFEVESALMEHPAVAEAGVIGKPDplrGEIIKAFislkegFEPSDELKEEiinfvRQKLGAHV--------APREIEFV 421

                         490
                  ....*....|.
gi 446581728 2015 LEIPITANGKI 2025
Cdd:cd05969   422 DNLPKTRSGKI 432
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 1553-2025 1.41e-38

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 152.37  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1553 ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEAC 1632
Cdd:cd05911     5 ADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1633 RIITSNKF----KSHLNVSDYKVSII-------EDIYRTTINDDVKILNK----------PDDLAYVIYTSGSTGKPKGT 1691
Cdd:cd05911    85 VIFTDPDGlekvKEAAKELGPKDKIIvlddkpdGVLSIEDLLSPTLGEEDedlppplkdgKDDTAAILYSSGTTGLPKGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1692 LLTHKgvlNLVE-----WRNEVFQISPNDK---VTQFYsHSFDssvseIFSTL---LNGAELYLLSdeqRYSTVEYAQAI 1760
Cdd:cd05911   165 CLSHR---NLIAnlsqvQTFLYGNDGSNDVilgFLPLY-HIYG-----LFTTLaslLNGATVIIMP---KFDSELFLDLI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1761 QETQATISDLPTVFFNELSTSlTKLDSEKIRSLRFIIMGGeAASTNAIRSWQNTFKNQVQLVNEYGPTEATVSAMYYFip 1840
Cdd:cd05911   233 EKYKITFLYLVPPIAAALAKS-PLLDKYDLSSLRVILSGG-APLSKELQELLAKRFPNATIKQGYGMTETGGILTVNP-- 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1841 vleGENNLLGSVpiGIPISNTKVHILNS-YMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAfisnpFSEDNskrLYRT 1919
Cdd:cd05911   309 ---DGDDKPGSV--GRLLPNVEAKIVDDdGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKET-----FDEDG---WLHT 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1920 GDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVtqteggmllqayyktvdgIGIEKnklaiHLS 1999
Cdd:cd05911   376 GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAV------------------IGIPD-----EVS 432

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446581728 2000 NVLP------------------EYM---VPKYYSH------VLEIPITANGKI 2025
Cdd:cd05911   433 GELPrayvvrkpgekltekevkDYVakkVASYKQLrggvvfVDEIPKSASGKI 485
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 470-965 1.51e-38

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 153.16  E-value: 1.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  470 TLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPI 549
Cdd:PRK08316   12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  550 DPKFPEKRIEYILKDSESQMIITKKEYRGLVERfAIHTIYLEDFHYAN------------SIENIASTH---------TI 608
Cdd:PRK08316   92 NFMLTGEELAYILDHSGARAFLVDPALAPTAEA-ALALLPVDTLILSLvlggreapggwlDFADWAEAGsvaepdvelAD 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQfATIIFDASIMEIF--PILLCGGRMHLiseIEK 686
Cdd:PRK08316  171 DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLH-ALPLYHCAQLDVFlgPYLYVGATNVI---LDA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  687 RSAEEFINVSQKYGITNVVL-PTAFFKLI--ADMPKEmllKLNSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPT 763
Cdd:PRK08316  247 PDPELILRTIEAERITSFFApPTVWISLLrhPDFDTR---DLSSLRKGYYGASIMPVEVLKELRERLP-GLRFYNCYGQT 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  764 ETTVCATMYEVNGEIQKEISnipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksy 843
Cdd:PRK08316  323 EIAPLATVLGPEEHLRRPGS---AGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF------- 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  844 nRDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNT 919
Cdd:PRK08316  393 -RGGWFH-SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKwieaVTAVVVPKAGA 470

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 446581728  920 ELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQ 965
Cdd:PRK08316  471 TVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1525-1968 2.59e-38

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 154.10  E-value: 2.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1525 TERPYPYFQNIQEQFYMQVDRQPERIAIATAT----ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSM 1600
Cdd:COG1022     3 EFSDVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1601 LGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSN-----KFKSHLNvsdyKVSIIEDIY---RTTINDDVKILN-- 1670
Cdd:COG1022    83 LAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqeqldKLLEVRD----ELPSLRHIVvldPRGLRDDPRLLSld 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1671 ----------------------KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQF--YSHSFD 1726
Cdd:COG1022   159 ellalgrevadpaelearraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlpLAHVFE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1727 SSVSeiFSTLLNGAELYLLSDEQrysTVeyAQAIQETQatisdlPTVFF-----------------NELST--------- 1780
Cdd:COG1022   239 RTVS--YYALAAGATVAFAESPD---TL--AEDLREVK------PTFMLavprvwekvyagiqakaEEAGGlkrklfrwa 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1781 -------SLTKLDSE-------------------KIRS-----LRFIIMGGEAAST------NAIRswqntfknqVQLVN 1823
Cdd:COG1022   306 lavgrryARARLAGKspslllrlkhaladklvfsKLREalggrLRFAVSGGAALGPelarffRALG---------IPVLE 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1824 EYGPTEAT-VSAMYYFipvlegENNLLGSVpiGIPISNTKVHIlnsymqycpvGCMGELYIESLGLAQGYWKQKEKTKQA 1902
Cdd:COG1022   377 GYGLTETSpVITVNRP------GDNRIGTV--GPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEA 438

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728 1903 FISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKdKQVkIR---GHRIELGEIEDAMLQLEGISQAVV 1968
Cdd:COG1022   439 FDADGW--------LHTGDIGELDEDGFLRITGRK-KDL-IVtsgGKNVAPQPIENALKASPLIEQAVV 497
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1098-1500 2.89e-38

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 149.38  E-value: 2.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1098 RVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPR--QVILNSIAIdlihdEIEHMSKKEQQEYIRTTI 1175
Cdd:cd19542    20 GLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTflQVVLKSLDP-----PIEEVETDEDSLDALTRD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1176 NQTDHTPFdleKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAfakrrnpELPTISNRYVDYAE-- 1253
Cdd:cd19542    95 LLDDPTLF---GQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-------QLLPPAPPFSDYISyl 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1254 WEQVQlnlgrwDTEKSYWMAELAAPLPILnLPlDFSRNRQSTNKGTVFEMKLDnemkeSLKQVCEQENISMYMLFLAAYI 1333
Cdd:cd19542   165 QSQSQ------EESLQYWRKYLQGASPCA-FP-SLSPKRPAERSLSSTRRSLA-----KLEAFCASLGVTLASLFQAAWA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1334 QLLHYLTDQKDIIVGTPVVGRN--HQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVIEQI 1411
Cdd:cd19542   232 LVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRAL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1412 NPDRSfgnNPIFSTMFSYQKDILQQHDAYKLQLLPNK---QDISKFDISLAVEEGLDYVGISFEYDINLFKEESINRFTQ 1488
Cdd:cd19542   312 GLWPS---GTLFNTLVSYQNFEASPESELSGSSVFELsaaEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLE 388

                         410
                  ....*....|..
gi 446581728 1489 NLLNILDAFIHQ 1500
Cdd:cd19542   389 QFDDILEALLAN 400
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
478-962 3.07e-38

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 151.65  E-value: 3.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  478 QALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKR 557
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  558 IEYILKDSESQMIITKKEYRGlvERFAIHTIYLEDF-HYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKgvvN 636
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEA--KLIPGISVKFAELmNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYG---N 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  637 LSYSVINT-FHLG--KEDVFLqFATIIFDASIMEI-FPILLCGGRMHLiseIEKRSAEEFINVSQKYGITNV-VLPTAFF 711
Cdd:PRK03640  166 HWWSAVGSaLNLGltEDDCWL-AAVPIFHISGLSIlMRSVIYGMRVVL---VEKFDAEKINKLLQTGGVTIIsVVSTMLQ 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  712 KLIADMPKEMLlkLNSVKRLFVGGETLPAESVRKWQSKlglKIPVLNAYGPTETT--VCATMYEvngEIQKEISNipIGK 789
Cdd:PRK03640  242 RLLERLGEGTY--PSSFRCMLLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETAsqIVTLSPE---DALTKLGS--AGK 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  790 PIANSEVfVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMYcTGDLVRLLANGNLEFIGR 869
Cdd:PRK03640  312 PLFPCEL-KIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF--------QDGWFK-TGDIGYLDEEGFLYVLDR 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  870 KDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK---IVCFYLSKDnTELKQEALKTFLSESLPDFMMPNYIFHL 946
Cdd:PRK03640  382 RSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwgqVPVAFVVKS-GEVTEEELRHFCEEKLAKYKVPKRFYFV 460

                         490
                  ....*....|....*.
gi 446581728  947 ESFPVSPSGKLDRKKL 962
Cdd:PRK03640  461 EELPRNASGKLLRHEL 476
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 1558-2030 5.70e-38

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 150.94  E-value: 5.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQhLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGaaYIPIDVKYP--EDRINYIVRDSEACRII 1635
Cdd:cd05909     7 SLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIKTVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1636 TSNKFKSHLNV-------SDYKVSIIEDIyRTTIN--DDVKIL------------------NKPDDLAYVIYTSGSTGKP 1688
Cdd:cd05909    84 TSKQFIEKLKLhhlfdveYDARIVYLEDL-RAKISkaDKCKAFlagkfppkwllrifgvapVQPDDPAVILFTSGSEGLP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1689 KGTLLTHKGVLNLVEWRNEVFQISPNDKVTQF--YSHSFDSSVSeIFSTLLNGAELYLLSDEQRYSTVeyAQAIQETQAT 1766
Cdd:cd05909   163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGAlpFFHSFGLTGC-LWLPLLSGIKVVFHPNPLDYKKI--PELIYDKKAT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1767 ISDLPTVFFNELstsLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFknQVQLVNEYGPTEATvsamyyfiPVLE--- 1843
Cdd:cd05909   240 ILLGTPTFLRGY---ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF--GIRILEGYGTTECS--------PVISvnt 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1844 -GENNLLGSVpiGIPISNTKVHILnSYMQYCPV--GCMGELYIESLGLAQGYWKQKEKTKQAFisnpfsednSKRLYRTG 1920
Cdd:cd05909   307 pQSPNKEGTV--GRPLPGMEVKIV-SVETHEEVpiGEGGLLLVRGPNVMLGYLNEPELTSFAF---------GDGWYDTG 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1921 DLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAV----VTQTEGGMLLQAYYKTVDgigIEKNKLAI 1996
Cdd:cd05909   375 DIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVavvsVPDGRKGEKIVLLTTTTD---TDPSSLND 451

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 446581728 1997 HLSNV-LPEYMVPKYYSHVLEIPITANGKIDFEKL 2030
Cdd:cd05909   452 ILKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 1547-2030 5.84e-38

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 151.37  E-value: 5.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSNKF--------------KSHLNVS-----DYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGK 1687
Cdd:cd05959    98 EDSRARVVVVSGELapvlaaaltksehtLVVLIVSggagpEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGR 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1688 PKGTLLTHKGVLNLVE-WRNEVFQISPNDKVTQ----FYSHSFDSSVSEIFStllNGAELYLLSDEQRYSTVeyAQAIQE 1762
Cdd:cd05959   178 PKGVVHLHADIYWTAElYARNVLGIREDDVCFSaaklFFAYGLGNSLTFPLS---VGATTVLMPERPTPAAV--FKRIRR 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1763 TQatisdlPTVFFN--ELSTSLTKLDSEKIR---SLRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTEatvsAMYY 1837
Cdd:cd05959   253 YR------PTVFFGvpTLYAAMLAAPNLPSRdlsSLRLCVSAGEALPAEVGERWKARFG--LDILDGIGSTE----MLHI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1838 FIPVLEGENNlLGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNpfsednskrLY 1917
Cdd:cd05959   321 FLSNRPGRVR-YGTT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE---------WT 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1918 RTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGI---GIEK 1991
Cdd:cd05959   389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVgveDEDGLTKPKAFVVLRPGYedsEALE 468

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 446581728 1992 NKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKL 2030
Cdd:cd05959   469 EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 1559-2025 8.50e-38

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 149.02  E-value: 8.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSN 1638
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1639 kfkshlnvsdykvsiiediyrttinddvkilnkpDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDkvt 1718
Cdd:cd05972    81 ----------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD--- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1719 QFYSHSfDSS-----VSEIFSTLLNGAELyLLSDEQRYSTVEYAQAIQETQAT-ISDLPTVFfnelsTSLTKLDSE--KI 1790
Cdd:cd05972   124 IHWNIA-DPGwakgaWSSFFGPWLLGATV-FVYEGPRFDAERILELLERYGVTsFCGPPTAY-----RMLIKQDLSsyKF 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1791 RSLRFIIMGGEAASTNAIRSWQNTFKNQVQlvNEYGPTEATVS-AMYYFIPVLEGEnnllgsvpIGIPISNTKVHILNSY 1869
Cdd:cd05972   197 SHLRLVVSAGEPLNPEVIEWWRAATGLPIR--DGYGQTETGLTvGNFPDMPVKPGS--------MGRPTPGYDVAIIDDD 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1870 MQYCPVGCMGELYIE--SLGLAQGYWKQKEKTKQAFisnpfSEDnskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHR 1947
Cdd:cd05972   267 GRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-----RGD----YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1948 IELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIE---KNKLAIHLSNVLPEYMVPKYYSHVLEIPITA 2021
Cdd:cd05972   338 IGPFEVESALLEHPAVAEAAVVgspDPVRGEVVKAFVVLTSGYEPSeelAEELQGHVKKVLAPYKYPREIEFVEELPKTI 417


                  ....
gi 446581728 2022 NGKI 2025
Cdd:cd05972   418 SGKI 421
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 493-902 1.49e-37

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 148.90  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIIT 572
Cdd:cd05907     4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  573 KkeyrglverfaihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDV 652
Cdd:cd05907    84 E---------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDR 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  653 FLQF--ATIIFdASIMEIFPILLCGGRMHLISEIEKrsaeefinvsqkyGITN--VVLPTAFF-------KLIADMPKE- 720
Cdd:cd05907   131 HLSFlpLAHVF-ERRAGLYVPLLAGARIYFASSAET-------------LLDDlsEVRPTVFLavprvweKVYAAIKVKa 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  721 ---------MLLKLNSVKRLFVGGETLPAESVRKWQsklGLKIPVLNAYGPTETTVCATMyeVNGEIQKEISnipIGKPI 791
Cdd:cd05907   197 vpglkrklfDLAVGGRLRFAASGGAPLPAELLHFFR---ALGIPVYEGYGLTETSAVVTL--NPPGDNRIGT---VGKPL 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  792 ANSEVFVispfntlcpsGVVGELFIGGDGVANGYLNQKEKTEGAFIsldksynrDKKMYCTGDLVRLLANGNLEFIGR-K 870
Cdd:cd05907   269 PGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALD--------ADGWLHTGDLGEIDEDGFLHITGRkK 330

                         410       420       430
                  ....*....|....*....|....*....|..
gi 446581728  871 DNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF 902
Cdd:cd05907   331 DLIITSGGKNISPEPIENALKASPLISQAVVI 362
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 466-962 7.01e-37

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 148.75  E-value: 7.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  466 PNLKTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGV 545
Cdd:PRK06155   18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  546 YVPIDPKFPEKRIEYILKDSESQMIITKKEYRGLVE-----RFAIHTIYLEDFHYANSIEniASTHTIE----------- 609
Cdd:PRK06155   98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALEaadpgDLPLPAVWLLDAPASVSVP--AGWSTAPlppldapapaa 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 -----DAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLIsei 684
Cdd:PRK06155  176 avqpgDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLE--- 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  685 EKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGetLPAESVRKWQSKLGlkIPVLNAYGPTE 764
Cdd:PRK06155  253 PRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG--VPAALHAAFRERFG--VDLLDGYGSTE 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  765 TtvcatmyevngeiqkeisNIPIGKPIANS------------EVFVISPFNTLCPSGVVGELFIGGD---GVANGYLNQK 829
Cdd:PRK06155  329 T------------------NFVIAVTHGSQrpgsmgrlapgfEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMP 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  830 EKTEGAFISLdksynrdkkMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN--- 906
Cdd:PRK06155  391 EKTVEAWRNL---------WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSelg 461

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728  907 -DKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK06155  462 eDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 494-962 9.34e-37

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 145.70  E-value: 9.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  494 SITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITK 573
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  574 KEyrglverfaihtiyledfhyansieniasthtIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVF 653
Cdd:cd05935    81 SE--------------------------------LDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  654 LQ----FATIIFDASIMEIFPIllcGGRMHLISEIEKRSAEEFInvsQKYGITN-VVLPTAFFKLIADmPKEMLLKLNSV 728
Cdd:cd05935   129 LAclplFHVTGFVGSLNTAVYV---GGTYVLMARWDRETALELI---EKYKVTFwTNIPTMLVDLLAT-PEFKTRDLSSL 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  729 KRLFVGGETLPAESVRKWQSKLGLKIpvLNAYGPTETTVCATMyevngeiqkeisNIP-------IGKPIANSEVFVISP 801
Cdd:cd05935   202 KVLTGGGAPMPPAVAEKLLKLTGLRF--VEGYGLTETMSQTHT------------NPPlrpklqcLGIP*FGVDARVIDI 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  802 fNTL--CPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGY 879
Cdd:cd05935   268 -ETGreLPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK-----GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGF 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  880 RIELDEIEGTLFKHPEVRDAVVFTYQNDKIV----CFYLSKDNTELK--QEALKTFLSESLPDFMMPNYIFHLESFPVSP 953
Cdd:cd05935   342 KVWPAEVEAKLYKHPAI*EVCVISVPDERVGeevkAFIVLRPEYRGKvtEEDIIEWAREQMAAYKYPREVEFVDELPRSA 421


                  ....*....
gi 446581728  954 SGKLDRKKL 962
Cdd:cd05935   422 SGKILWRLL 430
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 1558-1968 1.49e-36

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 145.82  E-value: 1.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIdvkYP---EDRINYIVRDSEAcri 1634
Cdd:cd05907     5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI---YPtssAEQIAYILNDSEA--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1635 itsnkfkshlnvsdyKVSIIEDiyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPN 1714
Cdd:cd05907    79 ---------------KALFVED---------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1715 DKVTQF--YSHSFDsSVSEIFSTLLNGAELYLLSDEQRYStveyaQAIQETQatisdlPTVFFN--------------EL 1778
Cdd:cd05907   129 DRHLSFlpLAHVFE-RRAGLYVPLLAGARIYFASSAETLL-----DDLSEVR------PTVFLAvprvwekvyaaikvKA 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1779 STSLTK--LDSEKIRSLRFIIMGGEAASTNAIRSWQntfKNQVQLVNEYGPTE--ATVSAMyyfipvlEGENNLLGSVpi 1854
Cdd:cd05907   197 VPGLKRklFDLAVGGRLRFAASGGAPLPAELLHFFR---ALGIPVYEGYGLTEtsAVVTLN-------PPGDNRIGTV-- 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1855 GIPISNTKVHILNSymqycpvgcmGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFM 1934
Cdd:cd05907   265 GKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW--------LHTGDLGEIDEDGFLHIT 326

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 446581728 1935 GR-KDKQVKIRGHRIELGEIEDAMLQLEGISQAVV 1968
Cdd:cd05907   327 GRkKDLIITSGGKNISPEPIENALKASPLISQAVV 361
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 17-435 8.09e-36

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 142.89  E-value: 8.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   17 TVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIPIKDLT 96
Cdd:cd19533     5 TSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHIDLS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   97 AFKNTEqkSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKSNV 176
Cdd:cd19533    85 GDPDPE--GAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  177 EFES-PYKNLVKHEESFIDSAIYKEGSSYWKDYLQGELTPTEF---PIDFNKMNEKRytdkniSKNINSDLFYQIQCFAK 252
Cdd:cd19533   163 PAPFgSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLarrAPGRSLAFLRR------TAELPPELTRTLLEAAE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  253 KNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSihLAIT 332
Cdd:cd19533   237 AHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRE--LRSL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  333 YKHNSYSH--IVKDLNLNTNTNHnmVYSTAFNTMK-IPELKIPDIESTVLTDCK-RVNPFNmtwrIMRYEGETENKIEVD 408
Cdd:cd19533   315 LRHQRYRYedLRRDLGLTGELHP--LFGPTVNYMPfDYGLDFGGVVGLTHNLSSgPTNDLS----IFVYDRDDESGLRID 388

                         410       420
                  ....*....|....*....|....*....
gi 446581728  409 --YNSALYKPESISDLVERYIYLLQKLMK 435
Cdd:cd19533   389 fdANPALYSGEDLARHQERLLRLLEEAAA 417
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 1547-2026 6.86e-35

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 141.68  E-value: 6.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd05926     3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSN-------KFKSHLNVS------DYKVSIIEDIYRT---TINDDVKI----LNKPDDLAYVIYTSGSTG 1686
Cdd:cd05926    83 ADLGSKLVLTPKgelgpasRAASKLGLAilelalDVGVLIRAPSAESlsnLLADKKNAksegVPLPDDLALILHTSGTTG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1687 KPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQ----FYSHSFdssVSEIFSTLLNGAELYLlsdEQRYSTVEYAQAIQE 1762
Cdd:cd05926   163 RPKGVPLTHRNLAASATNITNTYKLTPDDRTLVvmplFHVHGL---VASLLSTLAAGGSVVL---PPRFSASTFWPDVRD 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1763 TQAT-ISDLPTVFFNELSTSLTKLDSEKIrSLRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTEATvSAMyyFIPV 1841
Cdd:cd05926   237 YNATwYTAVPTIHQILLNRPEPNPESPPP-KLRFIRSCSASLPPAVLEALEATFG--APVLEAYGMTEAA-HQM--TSNP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1842 LEGENNLLGSVPIGipiSNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGD 1921
Cdd:cd05926   311 LPPGPRKPGSVGKP---VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW--------FRTGD 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1922 LVRWLPNGNIEFMGRKdKQVKIR-GHRIELGEIEDAMLQLEGISQAV---VTQTEGGMLLQAYYKTVDGIGIEKNKLAIH 1997
Cdd:cd05926   380 LGYLDADGYLFLTGRI-KELINRgGEKISPLEVDGVLLSHPAVLEAVafgVPDEKYGEEVAAAVVLREGASVTEEELRAF 458

                         490       500
                  ....*....|....*....|....*....
gi 446581728 1998 LSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:cd05926   459 CRKHLAAFKVPKKVYFVDELPKTATGKIQ 487
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1555-2025 9.33e-35

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 140.26  E-value: 9.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1555 ATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRI 1634
Cdd:cd05971     3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1635 ITsnkfkshlnvsdykvsiiediyrttinddvkilNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPN 1714
Cdd:cd05971    83 VT---------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPR 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1715 DKvTQFYSHSFDSSVSEIFSTLLngAELY-----LLSDEQRYStveyAQAIQETQATISdLPTVFfneLSTSLTKL---- 1785
Cdd:cd05971   130 DG-DLYWTPADWAWIGGLLDVLL--PSLYfgvpvLAHRMTKFD----PKAALDLMSRYG-VTTAF---LPPTALKMmrqq 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1786 ---DSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVqlvNE-YGPTEATVsamyyfipvLEGENNLLGSV---PIGIPI 1858
Cdd:cd05971   199 geqLKHAQVKLRAIATGGESLGEELLGWAREQFGVEV---NEfYGQTECNL---------VIGNCSALFPIkpgSMGKPI 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1859 SNTKVHILNSYMQYCPVGCMGELYIESLGLAQ--GYWKQKEKTKQAFISNPFsednskrlyRTGDLVRWLPNGNIEFMGR 1936
Cdd:cd05971   267 PGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAflGYWNNPSATEKKMAGDWL---------LTGDLGRKDSDGYFWYVGR 337

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1937 KDKQVKIRGHRIELGEIEDAMLQLEGISQAVV---------TQTEGGMLLQAYYKTVDGIgieKNKLAIHLSNVLPEYMV 2007
Cdd:cd05971   338 DDDVITSSGYRIGPAEIEECLLKHPAVLMAAVvgipdpirgEIVKAFVVLNPGETPSDAL---AREIQELVKTRLAAHEY 414

                         490
                  ....*....|....*...
gi 446581728 2008 PKYYSHVLEIPITANGKI 2025
Cdd:cd05971   415 PREIEFVNELPRTATGKI 432
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 465-962 2.67e-34

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 139.77  E-value: 2.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  465 YPNLKTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGG 544
Cdd:cd05920    11 YWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  545 VYVPIDPKFPEKRIEYILKDSESQMIITKKEYRGlverfaihtiyleDFHYANSIEniaSTHTIEDAAYIIYTSGSTGLP 624
Cdd:cd05920    91 VPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAG-------------FDHRALARE---LAESIPEVALFLLSGGTTGTP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  625 KGVVVPHKGvvnLSYSVINTF---HLGKEDVFL-------QFATiifdaSIMEIFPILLCGGRMHLISEIEKRSAEEFIn 694
Cdd:cd05920   155 KLIPRTHND---YAYNVRASAevcGLDQDTVYLavlpaahNFPL-----ACPGVLGTLLAGGRVVLAPDPSPDAAFPLI- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  695 vsQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKipVLNAYGPTETTVCATMYEV 774
Cdd:cd05920   226 --EREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT--LQQVFGMAEGLLNYTRLDD 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  775 NGEIqkeISNIPiGKPI-ANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMYCTG 853
Cdd:cd05920   302 PDEV---IIHTQ-GRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF--------TPDGFYRTG 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  854 DLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYLSKDnTELKQEALKTF 929
Cdd:cd05920   370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVampdELLGERSCAFVVLRD-PPPSAAQLRRF 448

                         490       500       510
                  ....*....|....*....|....*....|....
gi 446581728  930 LSE-SLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05920   449 LRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 1558-2025 3.08e-34

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 138.67  E-value: 3.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITS 1637
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1638 NKFKSHlnvsdykvsiiediyrttinddvKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK- 1716
Cdd:cd05903    81 ERFRQF-----------------------DPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVf 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1717 -VTQFYSHsFDSSVSEIFSTLLNGAELYLLsdeQRYSTVEYAQAIQETQATISDLPTVFFNELSTSLTKLDsEKIRSLRF 1795
Cdd:cd05903   138 lVASPMAH-QTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAG-EPLSRLRT 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1796 IIMGGEAASTNAIRSWQNTFKNQVqlVNEYGPTEaTVSAMYYFIPVLEGennlLGSVPIGIPISNTKVHILNSYMQYCPV 1875
Cdd:cd05903   213 FVCGGATVPRSLARRAAELLGAKV--CSAYGSTE-CPGAVTSITPAPED----RRLYTDGRPLPGVEIKVVDDTGATLAP 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1876 GCMGELYIESLGLAQGYWKQKEKTKQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKdKQVKIR-GHRIELGEIE 1954
Cdd:cd05903   286 GVEGELLSRGPSVFLGYLDRPDLTADAAPEG---------WFRTGDLARLDEDGYLRITGRS-KDIIIRgGENIPVLEVE 355

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1955 DAMLQLEGISQAVVTQTEGGMLLQ---AYYKTVDGIGIEKNKLAIHLSNV-LPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05903   356 DLLLGHPGVIEAAVVALPDERLGEracAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 495-959 3.56e-34

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 138.42  E-value: 3.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  495 ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITkk 574
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  575 eyrglverfaihtiyledfhyansieNIASTHTIEDAAYI-IYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVF 653
Cdd:cd05973    79 --------------------------DAANRHKLDSDPFVmMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  654 LQFA---------TIIFDASIMEIFPILLCGGRmhliseiekrSAEEFINVSQKYGITNVV-LPTAFFKLIAD-MPKEML 722
Cdd:cd05973   133 WNAAdpgwayglyYAITGPLALGHPTILLEGGF----------SVESTWRVIERLGVTNLAgSPTAYRLLMAAgAEVPAR 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  723 LKLnSVKRLFVGGETLPAESVRKWQSKLGLkiPVLNAYGPTETTVCATMYEVNGEIQKEISnipIGKPIANSEVFVISPF 802
Cdd:cd05973   203 PKG-RLRRVSSAGEPLTPEVIRWFDAALGV--PIHDHYGQTELGMVLANHHALEHPVHAGS---AGRAMPGWRVAVLDDD 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  803 NTLCPSGVVGELFIGGDGVA----NGYLNQKEKTEgafisldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRG 878
Cdd:cd05973   277 GDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPAI------------DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSG 344

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  879 YRIELDEIEGTLFKHPEVRDAVVFTYQND---KIVCFYL----SKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPV 951
Cdd:cd05973   345 YRIGPFDVESALIEHPAVAEAAVIGVPDPertEVVKAFVvlrgGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPK 424


                  ....*...
gi 446581728  952 SPSGKLDR 959
Cdd:cd05973   425 TPSGKIQR 432
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 609-962 4.36e-34

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 135.87  E-value: 4.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDV-------FLQF-------------ATIIFDASIMEI 668
Cdd:cd05917     2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlcipvplFHCFgsvlgvlaclthgATMVFPSPSFDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  669 FPILlcggrmHLISEiEKRSAeefinvsqKYGItnvvlPTAFFKLIaDMPKEMLLKLNSVKRLFVGGETLPAESVRKWQS 748
Cdd:cd05917    82 LAVL------EAIEK-EKCTA--------LHGV-----PTMFIAEL-EHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIE 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  749 KLGLKiPVLNAYGPTETTVCATMYEVNGEIQKEISNIpiGKPIANSEVFVISPF-NTLCPSGVVGELFIGGDGVANGYLN 827
Cdd:cd05917   141 VMNMK-DVTIAYGMTETSPVSTQTRTDDSIEKRVNTV--GRIMPHTEAKIVDPEgGIVPPVGVPGELCIRGYSVMKGYWN 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  828 QKEKTEgafisldKSYNRDKKMYcTGDLVRLLANGNLEFIGR-KDnqVKIRG-YRIELDEIEGTLFKHPEVRDAVVFTYQ 905
Cdd:cd05917   218 DPEKTA-------EAIDGDGWLH-TGDLAVMDEDGYCRIVGRiKD--MIIRGgENIYPREIEEFLHTHPKVSDVQVVGVP 287

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728  906 NDK---IVCFYLS-KDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05917   288 DERygeEVCAWIRlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1080-1495 5.50e-34

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 138.00  E-value: 5.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKRIWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSiaiDLIHDEI 1159
Cdd:cd19546     7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDA---DAARPEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1160 EHMSKKEQqEYIRTTINQTDHtPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNP 1239
Cdd:cd19546    84 PVVPATEE-ELPALLADRAAH-LFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1240 ELPTISNRYVDYAEWEQVQLNLGR------WDtEKSYWMAELAAPLPILNLPLDFSRNRQSTNKGTVFEMKLDNEMKESL 1313
Cdd:cd19546   162 ERAPLPLQFADYALWERELLAGEDdrdsliGD-QIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1314 KQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNHQ-EFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREK 1392
Cdd:cd19546   241 MEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1393 CLNSFQNQSYPFDKVIEQINPDRSFGNNPIFSTMFSYQKDILQQHDAYKL-----QLLPNKQDISKFDISLAVEE----- 1462
Cdd:cd19546   321 VREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPELpglrtSPVPLGTEAMELDLSLALTErrndd 400

                         410       420       430
                  ....*....|....*....|....*....|....
gi 446581728 1463 -GLDYVGISFEYDINLFKEESINRFTQNLLNILD 1495
Cdd:cd19546   401 gDPDGLDGSLRYAADLFDRATAAALARRLVRVLE 434
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 1560-2030 1.49e-33

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 136.42  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1560 TYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNK 1639
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1640 FKSHLNVSDYKVSI-IEDIYRTTINDDVKIlnkpDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK-- 1716
Cdd:TIGR01923   81 LEEKDFQADSLDRIeAAGRYETSLSASFNM----DQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNwl 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1717 -VTQFYsHSfdSSVSEIFSTLLNGAELYLLsdeQRYSTVeyAQAIQETQAT-ISDLPTVFFNELSTSLTKLdsekirSLR 1794
Cdd:TIGR01923  157 lSLPLY-HI--SGLSILFRWLIEGATLRIV---DKFNQL--LEMIANERVThISLVPTQLNRLLDEGGHNE------NLR 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1795 FIIMGGEAASTNAIRSWQntfKNQVQLVNEYGPTEATVSAMYYFIPVLEGENNllgsvpIGIPISNTKVHILNSYMQYcp 1874
Cdd:TIGR01923  223 KILLGGSAIPAPLIEEAQ---QYGLPIYLSYGMTETCSQVTTATPEMLHARPD------VGRPLAGREIKIKVDNKEG-- 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1875 vgcMGELYIESLGLAQGYWKQKEktkqafiSNPFSEDNSkrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIE 1954
Cdd:TIGR01923  292 ---HGEIMVKGANLMKGYLYQGE-------LTPAFEQQG--WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIE 359

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  1955 DAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDgiGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKL 2030
Cdd:TIGR01923  360 TVLYQHPGIQEAVVVpkpDAEWGQVPVAYIVSES--DISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
460-902 3.21e-33

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 138.31  E-value: 3.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  460 SNALTYPNLKTLDQLIDLQALKSPNQIAIS---MGD-QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMereiDTIV- 534
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALRekeDGIwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILS----DNRPe 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  535 WI---LGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII--TKKEYR-------------------GLVERFAIHTIYL 590
Cdd:COG1022    78 WViadLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDkllevrdelpslrhivvldPRGLRDDPRLLSL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  591 EDF-------HYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQF------- 656
Cdd:COG1022   158 DELlalgrevADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplahvf 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  657 ------------ATIIFDASI-------MEIFPILLCGG-----RMHliSEIEKRSAEE----------FINVSQKYGIT 702
Cdd:COG1022   238 ertvsyyalaagATVAFAESPdtlaedlREVKPTFMLAVprvweKVY--AGIQAKAEEAgglkrklfrwALAVGRRYARA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  703 -----NVVLPTAFFKLIADmpkemLLKLNSVKRLF--------VGGETLPAESVRKWQsklGLKIPVLNAYGPTETTVCA 769
Cdd:COG1022   316 rlagkSPSLLLRLKHALAD-----KLVFSKLREALggrlrfavSGGAALGPELARFFR---ALGIPVLEGYGLTETSPVI 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  770 TMYEVNGeiqkeisNIP--IGKPIANSEVFVispfntlcpsGVVGELFIGGDGVANGYLNQKEKTEGAFisldksyNRDK 847
Cdd:COG1022   388 TVNRPGD-------NRIgtVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAF-------DADG 443

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  848 KMYcTGDLVRLLANGNLEFIGRKDNQVKIR-GYRIELDEIEGTLFKHPEVRDAVVF 902
Cdd:COG1022   444 WLH-TGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 493-962 1.09e-32

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 135.44  E-value: 1.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIIT 572
Cdd:cd05904    31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  573 KKEYRGLVERFAIHTIYLED--FHYANSIENIASTHTIE---------DAAYIIYTSGSTGLPKGVVVPHKGVVNLSySV 641
Cdd:cd05904   111 TAELAEKLASLALPVVLLDSaeFDSLSFSDLLFEADEAEppvvvikqdDVAALLYSSGTTGRSKGVMLTHRNLIAMV-AQ 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  642 INTF---HLGKEDVFLQFatiifdasiMEIFPI----LLCGGRMHLISEI---EKRSAEEFINVSQKYGITN--VVLPta 709
Cdd:cd05904   190 FVAGegsNSDSEDVFLCV---------LPMFHIyglsSFALGLLRLGATVvvmPRFDLEELLAAIERYKVTHlpVVPP-- 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  710 FFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMYEVNGEIQKEISNipIGK 789
Cdd:cd05904   259 IVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFP-NVDLGQGYGMTESTGVVAMCFAPEKDRAKYGS--VGR 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  790 PIANSEVFVISPfNT--LCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKMY-CTGDLVRLLANGNLEF 866
Cdd:cd05904   336 LVPNVEAKIVDP-ETgeSLPPNQTGELWIRGPSIMKGYLNNPEATAATI---------DKEGWlHTGDLCYIDEDGYLFI 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  867 IGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI----VCFYLSKDNTELKQEALKTFLSESLPDFMMPNY 942
Cdd:cd05904   406 VDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAgevpMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRK 485

                         490       500
                  ....*....|....*....|
gi 446581728  943 IFHLESFPVSPSGKLDRKKL 962
Cdd:cd05904   486 VAFVDAIPKSPSGKILRKEL 505
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 494-962 1.35e-32

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 134.77  E-value: 1.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  494 SITYYELQQRSNQIVNYLRENDlKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITK 573
Cdd:cd05909     7 SLTYRKLLTGAIALARKLAKMT-KEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  574 K---EYRGLVERFAIHT----IYLED------------------FHYANSIENIASTHT-IEDAAYIIYTSGSTGLPKGV 627
Cdd:cd05909    86 KqfiEKLKLHHLFDVEYdariVYLEDlrakiskadkckaflagkFPPKWLLRIFGVAPVqPDDPAVILFTSGSEGLPKGV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  628 VVPHKGVVNLSYSVINTFHLGKEDVFLQFATII--FDASIMEIFPILLCGGRMHLISEIEKRSAEEFInvsQKYGITnVV 705
Cdd:cd05909   166 VLSHKNLLANVEQITAIFDPNPEDVVFGALPFFhsFGLTGCLWLPLLSGIKVVFHPNPLDYKKIPELI---YDKKAT-IL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  706 LPT-AFFKLIADMPKEMLLKlnSVKRLFVGGETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCATMyevngeiqkeisN 784
Cdd:cd05909   242 LGTpTFLRGYARAAHPEDFS--SLRLVVAGAEKLKDTLRQEFQEKFG--IRILEGYGTTECSPVISV------------N 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  785 IP--------IGKPIANSEVFVISPfNTLCP--SGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKMYCTGD 854
Cdd:cd05909   306 TPqspnkegtVGRPLPGMEVKIVSV-ETHEEvpIGEGGLLLVRGPNVMLGYLNEPELTSFAF---------GDGWYDTGD 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  855 LVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKH--PEVRDAVVFT---YQNDKIVCFYLSKDNTelkQEALKTF 929
Cdd:cd05909   376 IGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVpdgRKGEKIVLLTTTTDTD---PSSLNDI 452

                         490       500       510
                  ....*....|....*....|....*....|....
gi 446581728  930 LSES-LPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05909   453 LKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 1558-2025 4.15e-32

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 132.22  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEAcriits 1637
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGA------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1638 nkfkshlnvsdyKVSIiediyrttinddvkILNKPDDLAYVIYTSGSTGKPKGTLLTHKG----VLNLVEWRNevfqISP 1713
Cdd:cd05935    75 ------------KVAV--------------VGSELDDLALIPYTSGTTGLPKGCMHTHFSaaanALQSAVWTG----LTP 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1714 NDKVTQ----FYSHSFDSSVSeifSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATIS-DLPTVFFNELSTslTKLDSE 1788
Cdd:cd05935   125 SDVILAclplFHVTGFVGSLN---TAVYVGGTYVLMA---RWDRETALELIEKYKVTFWtNIPTMLVDLLAT--PEFKTR 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1789 KIRSLRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTEATvsAMYYFIPVLEGENNLLgsvpiGIPISNTKVHILN- 1867
Cdd:cd05935   197 DLSSLKVLTGGGAPMPPAVAEKLLKLTG--LRFVEGYGLTETM--SQTHTNPPLRPKLQCL-----GIP*FGVDARVIDi 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1868 SYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFIsnpfsEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHR 1947
Cdd:cd05935   268 ETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI-----EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1948 IELGEIEDAMLQLEGISQAVVTQT---EGG-------MLLQAYYKTVDGIGIEKnklaiHLSNVLPEYMVPKYYSHVLEI 2017
Cdd:cd05935   343 VWPAEVEAKLYKHPAI*EVCVISVpdeRVGeevkafiVLRPEYRGKVTEEDIIE-----WAREQMAAYKYPREVEFVDEL 417


                  ....*...
gi 446581728 2018 PITANGKI 2025
Cdd:cd05935   418 PRSASGKI 425
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 494-962 8.98e-32

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 130.54  E-value: 8.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  494 SITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMiitk 573
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  574 keyrglverfaihtiyledfhyansieniasthtiEDAAYIIYTSGSTGLPKGVVVPHKgvvNLSYSVINT--------- 644
Cdd:cd05912    77 -----------------------------------DDIATIMYTSGTTGKPKGVQQTFG---NHWWSAIGSalnlglted 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  645 ---------FHLGKEDVFLQfatiifdaSIMEIFPILLcggrmhliseIEKRSAEEFINVSQKYGITNV-VLPTAFFKLI 714
Cdd:cd05912   119 dnwlcalplFHISGLSILMR--------SVIYGMTVYL----------VDKFDAEQVLHLINSGKVTIIsVVPTMLQRLL 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  715 ADMPKEMllkLNSVKRLFVGGETLPAESVRKWQSKlglKIPVLNAYGPTETT--VCATMYEvngEIQKEISNipIGKPIA 792
Cdd:cd05912   181 EILGEGY---PNNLRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETCsqIVTLSPE---DALNKIGS--AGKPLF 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  793 NSEVFVISPFNtlcPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKMYCTGDLVRLLANGNLEFIGRKDN 872
Cdd:cd05912   250 PVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESF---------ENGWFKTGDIGYLDEEGFLYVLDRRSD 317

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  873 QVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK---IVCFYLSKdNTELKQEALKTFLSESLPDFMMPNYIFHLESF 949
Cdd:cd05912   318 LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKwgqVPVAFVVS-ERPISEEELIAYCSEKLAKYKVPKKIYFVDEL 396

                         490
                  ....*....|...
gi 446581728  950 PVSPSGKLDRKKL 962
Cdd:cd05912   397 PRTASGKLLRHEL 409
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1108-1496 1.01e-31

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 130.00  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1108 IEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVIL-NSIAIDlihdEIEHMSkkeqqeyIRTTINqtdhTPFDLE 1186
Cdd:cd19537    32 LSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSsSPPRVQ----RVDTLD-------VWKEIN----RPFDLE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1187 KGPLFRIRIfnlnkKKSYLYINLHHIITDEWSVRNLLDELMKVYsafakrRNPELPTISNRYVDYAEWEQVQLnlgrwDT 1266
Cdd:cd19537    97 REDPIRVFI-----SPDTLLVVMSHIICDLTTLQLLLREVSAAY------NGKLLPPVRREYLDSTAWSRPAS-----PE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1267 EKSYWMAELAaPLPILNLPldfSRNRQSTNKGTVFEMKLDNEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDII 1346
Cdd:cd19537   161 DLDFWSEYLS-GLPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1347 VGTPVVGRNHQEFEKIQGFFVNTLAIRTQLNDVKNLT--QLLQVVREkclnSFQN---QSYPFDKVIEQINPDRSFGNNP 1421
Cdd:cd19537   237 LGAPYLNRTSEEDMETVGLFLEPLPIRIRFPSSSDASaaDFLRAVRR----SSQAalaHAIPWHQLLEHLGLPPDSPNHP 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1422 IFSTMFSYqkdilqqHDAYKLQLLPNKQDI---------SKFdiSLAVE---EGLDYVGISFEYDINLFKEESINRFTQN 1489
Cdd:cd19537   313 LFDVMVTF-------HDDRGVSLALPIPGVeplytwaegAKF--PLMFEftaLSDDSLLLRLEYDTDCFSEEEIDRIESL 383


                  ....*..
gi 446581728 1490 LLNILDA 1496
Cdd:cd19537   384 ILAALEL 390
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 469-962 2.28e-31

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 131.09  E-value: 2.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAISM--GDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVY 546
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  547 VPIDPKFPEKRIEYILKDSESQMII---TKKEYRGLVERFAiHTIYLED-------FHYANSIEniASTHTIEDAAYIIY 616
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAViavDAQVMDAIFQSGV-RVLALSDlvglgepESAGPLIE--DPPREPEQPAFVFY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  617 TSGSTGLPKGVVVPHKG----VVNLSYSVINTFhlGKEDVFLQFATIIfdaSIMEIFPILLC----GGRMHLISEIEKRS 688
Cdd:cd05923   158 TSGTTGLPKGAVIPQRAaesrVLFMSTQAGLRH--GRHNVVLGLMPLY---HVIGFFAVLVAalalDGTYVVVEEFDPAD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  689 AEEFInvsQKYGITNVVL-PTAFFKLIADMpKEMLLKLNSVKRLFVGGETLPAESVRKWQSKlgLKIPVLNAYGPTETtv 767
Cdd:cd05923   233 ALKLI---EQERVTSLFAtPTHLDALAAAA-EFAGLKLSSLRHVTFAGATMPDAVLERVNQH--LPGEKVNIYGTTEA-- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  768 catmyeVNGEIQKEISNIPIGKPIANSEVFVIS---PFNTLCPSGVVGELFI--GGDGVANGYLNQKEKTEGAFisldks 842
Cdd:cd05923   305 ------MNSLYMRDARTGTEMRPGFFSEVRIVRiggSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKL------ 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  843 ynRDKKmYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK---IVCFYLSKDNT 919
Cdd:cd05923   373 --QDGW-YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwgqSVTACVVPREG 449

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 446581728  920 ELKQEALKTF-LSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05923   450 TLSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 20-336 4.29e-31

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 128.92  E-value: 4.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   20 QEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVEFDIPIKDLTAFK 99
Cdd:cd20483     8 QRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVIDLSEAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  100 NTEQKsiLKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKSNVEFE 179
Cdd:cd20483    88 DPEAA--LDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLATVP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  180 SP---YKNLVKHEESFIDSAIYKEGSSYWKDYLQG-----ELTPtefpidFNK---MNEKRYTDKNISKNINSDLFYQIQ 248
Cdd:cd20483   166 PPpvqYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipdasKLLP------FAKaerPPVKDYERSTVEATLDKELLARMK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  249 CFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIH 328
Cdd:cd20483   240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319


                  ....*...
gi 446581728  329 LAitYKHN 336
Cdd:cd20483   320 EA--YEHS 325
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 474-959 8.28e-31

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 130.31  E-value: 8.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  474 LIDLQALKSPNQIAISMGDQS-----ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVP 548
Cdd:cd05970    22 VVDAMAKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  549 IDPKFPEKRIEYILKDSESQMIITKKEyRGLVERF--AIHTIYL---------------EDFH--YANSIENIASTHTI- 608
Cdd:cd05970   102 ATHQLTAKDIVYRIESADIKMIVAIAE-DNIPEEIekAAPECPSkpklvwvgdpvpegwIDFRklIKNASPDFERPTANs 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 ----EDAAYIIYTSGSTGLPKgvVVPHKGVVNLSYSVINTF--HLGKEDVFLQFATIIFDASIM-EIFPILLCGGRMhLI 681
Cdd:cd05970   181 ypcgEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYwqNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAV-FV 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  682 SEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIAdmpKEMLLK--LNSVKRLFVGGETLPAESVRKWQSKLGLKIpvLNA 759
Cdd:cd05970   258 YDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLI---REDLSRydLSSLRYCTTAGEALNPEVFNTFKEKTGIKL--MEG 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  760 YGPTETTVC-ATMYEVngeiqkEISNIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGD-----GVANGYLNQKEKTE 833
Cdd:cd05970   333 FGQTETTLTiATFPWM------EPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTA 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  834 GAFisldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----- 908
Cdd:cd05970   407 EVW---------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIrgqvv 477

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728  909 ---IVcfyLSKDNT---ELKQEaLKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDR 959
Cdd:cd05970   478 katIV---LAKGYEpseELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
PRK07201 PRK07201
SDR family oxidoreductase;
2163-2426 8.97e-31

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 131.61  E-value: 8.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQL-PSTTIYCLVRENEDqvigAKLkERMEFYFGKEilqklkeRVELIEGDLSLMNLGLDS 2241
Cdd:PRK07201    2 RYFVTGGTGFIGRRLVSRLLDRrREATVHVLVRRQSL----SRL-EALAAYWGAD-------RVVPLVGDLTEPGLGLSE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHLKKnVESIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSVVGQAERdpkefEFFESDFDR 2320
Cdd:PRK07201   70 ADIAELGD-IDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAAtFHHVSSIAVAGDYEG-----VFREDDFDE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 GQNLDNLYLESKFQGEKMVREamEKGVRATIYRVGNLVGNSKTGKFQ------YninenaFYRLLKGIC-----LSSIAP 2389
Cdd:PRK07201  144 GQGLPTPYHRTKFEAEKLVRE--ECGLPWRVYRPAVVVGDSRTGEMDkidgpyY------FFKVLAKLAklpswLPMVGP 215

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 446581728 2390 DVNtYVDLTPVDYGSLAITELSYKANTVNKTMHICNP 2426
Cdd:PRK07201  216 DGG-RTNIVPVDYVADALDHLMHKDGRDGQTFHLTDP 251
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 612-960 1.54e-30

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 124.75  E-value: 1.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  612 AYIIYTSGSTGLPKGVVVPHKgvvNLSYS---VINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLIseiEKRS 688
Cdd:cd17630     3 ATVILTSGSTGTPKAVVHTAA---NLLASaagLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLL---ERNQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  689 AEEfiNVSQKYGITNVVL-PTAFFKLIADmpKEMLLKLNSVKRLFVGGETLPAESVRKwQSKLGlkIPVLNAYGPTETTV 767
Cdd:cd17630    77 ALA--EDLAPPGVTHVSLvPTQLQRLLDS--GQGPAALKSLRAVLLGGAPIPPELLER-AADRG--IPLYTTYGMTETAS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  768 CATMYEVNGEIQKEIsnipiGKPIANSEVFVISPfntlcpsgvvGELFIGGDGVANGYLNQKEKTEGAfisldksynrDK 847
Cdd:cd17630   150 QVATKRPDGFGRGGV-----GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPEFN----------ED 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  848 KMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSkdNTELKQ 923
Cdd:cd17630   205 GWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEelgqRPVAVIVG--RGPADP 282

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 446581728  924 EALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRK 960
Cdd:cd17630   283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 455-962 2.06e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 129.38  E-value: 2.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  455 YKEMNSNALTYpNLKTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIV 534
Cdd:PRK06710   11 YPEEIPSTISY-DIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  535 WILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII---------------TKKEYRgLVERFAIHTIYLEDFHY---- 595
Cdd:PRK06710   90 GYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsaTKIEHV-IVTRIADFLPFPKNLLYpfvq 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  596 ---ANSIENIASTHTIE---------------------DAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFH---LG 648
Cdd:PRK06710  169 kkqSNLVVKVSESETIHlwnsvekevntgvevpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYnckEG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  649 KEDVF--LQF-----ATIIFDASIMEifpillcGGRMHLISEIEKRSAEEFInvsQKYGITnvVLPTAFFKLIADMPKEM 721
Cdd:PRK06710  249 EEVVLgvLPFfhvygMTAVMNLSIMQ-------GYKMVLIPKFDMKMVFEAI---KKHKVT--LFPGAPTIYIALLNSPL 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  722 LLK--LNSVKRLFVGGETLPAESVRKWQSKLGLKIpvLNAYGPTETTvcaTMYEVNGEIQKEISNiPIGKPIANSEVFVI 799
Cdd:PRK06710  317 LKEydISSIRACISGSAPLPVEVQEKFETVTGGKL--VEGYGLTESS---PVTHSNFLWEKRVPG-SIGVPWPDTEAMIM 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  800 S-PFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRG 878
Cdd:PRK06710  391 SlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL--------QDGWLH-TGDVGYMDEDGFFYVKDRKKDMIVASG 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  879 YRIELDEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPS 954
Cdd:PRK06710  462 FNVYPREVEEVLYEHEKVQEVVTIgvpdPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTV 541


                  ....*...
gi 446581728  955 GKLDRKKL 962
Cdd:PRK06710  542 GKILRRVL 549
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
449-962 2.06e-30

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 129.10  E-value: 2.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  449 EKDHRLYKEMNsnaltYPNLKTLDQLIDLQALKSPNQIAISmGDQ--SITYYELQQRSNQIVNYLRENDLKKGQRVSITM 526
Cdd:PRK06087    8 EQRRAAYRQQG-----YWGDASLADYWQQTARAMPDKIAVV-DNHgaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  527 EREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKEYRG---------------------LVERFAI 585
Cdd:PRK06087   82 PGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQtrpvdlilplqnqlpqlqqivGVDKLAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  586 HTIYLEDFHYANSIENIASTHTI--EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVF-----LQFAT 658
Cdd:PRK06087  162 ATSSLSLSQIIADYEPLTTAITThgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFmmpapLGHAT 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  659 IIFDASIMeifPILLcGGRMHLISEIEKRSAEEFINvsqKYGITNVVLPTAFfklIADMPKEML---LKLNSVKRLFVGG 735
Cdd:PRK06087  242 GFLHGVTA---PFLI-GARSVLLDIFTPDACLALLE---QQRCTCMLGATPF---IYDLLNLLEkqpADLSALRFFLCGG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  736 ETLPAESVRKWQSKlGLKIpvLNAYGPTETtvCATMYeVNGEIQKEISNIPIGKPIANSEVFVISPFNTLCPSGVVGELF 815
Cdd:PRK06087  312 TTIPKKVARECQQR-GIKL--LSVYGSTES--SPHAV-VNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  816 IGGDGVANGYLNQKEKTEGAfisLDksynrDKKMYCTGDLVRLLANGNLEFIGRKdNQVKIR-GYRIELDEIEGTLFKHP 894
Cdd:PRK06087  386 SRGPNVFMGYLDEPELTARA---LD-----EEGWYYSGDLCRMDEAGYIKITGRK-KDIIVRgGENISSREVEDILLQHP 456

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581728  895 EVRDAVVFTYQNDKI---VCFY--LSKDNTELKQEALKTFLSES-LPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK06087  457 KIHDACVVAMPDERLgerSCAYvvLKAPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 479-977 2.32e-30

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 127.97  E-value: 2.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDlKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKF-PEKR 557
Cdd:PRK07638   11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWkQDEL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  558 IEYILKdSESQMIITKKEYRG-----------LVERFAIHTIYLEDFHYANSIENiasthtieDAAYIIYTSGSTGLPKG 626
Cdd:PRK07638   90 KERLAI-SNADMIVTERYKLNdlpdeegrvieIDEWKRMIEKYLPTYAPIENVQN--------APFYMGFTSGSTGKPKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  627 VVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFI---NVSQKYGItn 703
Cdd:PRK07638  161 FLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRKFIPNQVLDKLeteNISVMYTV-- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  704 vvlPTAFfkliadmpkEMLLKLN----SVKRLFVGGETLPAESVRKWQSKLgLKIPVLNAYGPTETTVCATMYEVNGEiQ 779
Cdd:PRK07638  239 ---PTML---------ESLYKENrvieNKMKIISSGAKWEAEAKEKIKNIF-PYAKLYEFYGASELSFVTALVDEESE-R 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  780 KEISnipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLN----QKEKTEGAFISLDKSYNRDKKmyctgdl 855
Cdd:PRK07638  305 RPNS---VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIggvlARELNADGWMTVRDVGYEDEE------- 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  856 vrllanGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYlsKDNTELKQeaLKTFLS 931
Cdd:PRK07638  375 ------GFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIgvpdSYWGEKPVAII--KGSATKQQ--LKSFCL 444

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 446581728  932 ESLPDFMMPNYIFHLESFPVSPSGKLDRKKLElqipSLLENMQKQY 977
Cdd:PRK07638  445 QRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK----SWIENQEKIY 486
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 469-962 2.48e-30

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 128.55  E-value: 2.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAISMGDQS----ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGG 544
Cdd:cd05906    10 RTLLELLLRAAERGPTKGITYIDADGseefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  545 VYVPIdPKFP--------EKRIEYILKDSESQMIITKK----EYRGL-----VERFAIHTIYLEDFHYANSIENIASTht 607
Cdd:cd05906    90 VPAPL-TVPPtydepnarLRKLRHIWQLLGSPVVLTDAelvaEFAGLetlsgLPGIRVLSIEELLDTAADHDLPQSRP-- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  608 iEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFatIIFD--ASIME--IFPILLCGGRMH-LIS 682
Cdd:cd05906   167 -DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNW--VPLDhvGGLVElhLRAVYLGCQQVHvPTE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  683 EIEKRSAeEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLK---LNSVKRLFVGGETLPAESVRKWQ---SKLGLKIPV 756
Cdd:cd05906   244 EILADPL-RWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGtwdLSSLRYLVNAGEAVVAKTIRRLLrllEPYGLPPDA 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  757 LN-AYGPTET----TVCATMYEvnGEIQKEISNIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEK 831
Cdd:cd05906   323 IRpAFGMTETcsgvIYSRSFPT--YDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  832 TEGAFISlDKSYNrdkkmycTGDLVrLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRD--AVVFTYQN--- 906
Cdd:cd05906   401 NAEAFTE-DGWFR-------TGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDpga 471

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  907 --DKIVCFY---------LSKDNTELKQEALKTFlseSLPdfmmPNYIFHL--ESFPVSPSGKLDRKKL 962
Cdd:cd05906   472 etEELAIFFvpeydlqdaLSETLRAIRSVVSREV---GVS----PAYLIPLpkEEIPKTSLGKIQRSKL 533
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 469-962 3.81e-30

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 128.25  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAI----SMGDQS--ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKS 542
Cdd:PRK13295   24 RTINDDLDACVASCPDKTAVtavrLGTGAPrrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  543 GGVYVPIDPKFPEKRIEYILKDSESQMIITKKEYRG-----LVERF-----AIHTIYLEDFHYANSIENIASTHTIE--- 609
Cdd:PRK13295  104 GAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGfdhaaMARRLrpelpALRHVVVVGGDGADSFEALLITPAWEqep 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 --------------DAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVflqfatiIFDASIME-------- 667
Cdd:PRK13295  184 dapailarlrpgpdDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDV-------ILMASPMAhqtgfmyg 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  668 -IFPILLcGGRMHLISEIEKRSAEEFInvsQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKW 746
Cdd:PRK13295  257 lMMPVML-GATAVLQDIWDPARAAELI---RTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERA 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  747 QSKLGLKIpvLNAYGPTETTVcATMYEVNGEIQKEISNipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYL 826
Cdd:PRK13295  333 RAALGAKI--VSAWGMTENGA-VTLTKLDDPDERASTT--DGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  827 NQKEKT----EGAFislDksynrdkkmycTGDLVRLLANGNLEFIGR-KDnqVKIRG-YRIELDEIEGTLFKHPEVRDAV 900
Cdd:PRK13295  408 KRPQLNgtdaDGWF---D-----------TGDLARIDADGYIRISGRsKD--VIIRGgENIPVVEIEALLYRHPAIAQVA 471

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728  901 VFTYQNDKI---VC-FYLSKDNTELKQEALKTFL-SESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK13295  472 IVAYPDERLgerACaFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 479-969 4.21e-30

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 128.24  E-value: 4.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRI 558
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  559 EYILKDSESQMIITKKEYRGLVE--------RFAIHTIY-----------LEDFHYANS------IENIASTHT------ 607
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAPVVEqvraetslRHVIVTSLadvlpaeptlpLPDSLRAPRlaaagaIDLLPALRActapvp 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  608 -----IEDAAYIIYTSGSTGLPKGVVVPHKGVVNL--SYSVInTFHLGKEDVFLQFATIIF----DASImeIFPiLLCGG 676
Cdd:PRK06178  203 lpppaLDALAALNYTGGTTGMPKGCEHTQRDMVYTaaAAYAV-AVVGGEDSVFLSFLPEFWiageNFGL--LFP-LFSGA 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  677 RMHLISeieKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRL----FVggETLPAESVRKWQSKLGl 752
Cdd:PRK06178  279 TLVLLA---RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVrvvsFV--KKLNPDYRQRWRALTG- 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  753 kiPVL--NAYGPTETTVCATMYEVNGEIQKEISNIPI--GKPIANSEvFVISPFNT--LCPSGVVGELFIGGDGVANGYL 826
Cdd:PRK06178  353 --SVLaeAAWGMTETHTCDTFTAGFQDDDFDLLSQPVfvGLPVPGTE-FKICDFETgeLLPLGAEGEIVVRTPSLLKGYW 429

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  827 NQKEKTEGAFisldksynRDKkMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEV-RDAVVFTYQ 905
Cdd:PRK06178  430 NKPEATAEAL--------RDG-WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVlGSAVVGRPD 500

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728  906 NDK---IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNyIFHLESFPVSPSGKLDRKKLELQIPSL 969
Cdd:PRK06178  501 PDKgqvPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQALAEEL 566
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 470-962 1.17e-29

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 126.15  E-value: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  470 TLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPI 549
Cdd:PRK06145    3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  550 DPKFPEKRIEYILKDSESQMIITKKEYRGLVErfAIHTIYLEDFHYANSIENIASTHTIEDAAY---------IIYTSGS 620
Cdd:PRK06145   83 NYRLAADEVAYILGDAGAKLLLVDEEFDAIVA--LETPKIVIDAAAQADSRRLAQGGLEIPPQAavaptdlvrLMYTSGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  621 TGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATII-FDASIMEIFPILLCGGRMHLISEIEKRSAEEFInvsQKY 699
Cdd:PRK06145  161 TDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYhVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAI---ERH 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  700 GITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWqSKLGLKIPVLNAYGPTETTVCATMYEVNGEIQ 779
Cdd:PRK06145  238 RLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDF-TRVFTRARYIDAYGLTETCSGDTLMEAGREIE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  780 KEISNipiGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldksynrdkKMYCTGDLVRLL 859
Cdd:PRK06145  317 KIGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG---------DWFRSGDVGYLD 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  860 ANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLP 935
Cdd:PRK06145  385 EEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwgerITAVVVLNPGATLTLEALDRHCRQRLA 464

                         490       500
                  ....*....|....*....|....*..
gi 446581728  936 DFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK06145  465 SFKVPRQLKVRDELPRNPSGKVLKRVL 491
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 610-957 1.34e-29

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 122.22  E-value: 1.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVVNLS--------------YSVINTFhlgkedvflqFATIIFDASIMeifPILLCG 675
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAaawadcadlteddrYLIINPF----------FHTFGYKAGIV---ACLLTG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  676 GRMHLISEIEKRSAEEFINVSQkygITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKIp 755
Cdd:cd17638    68 ATVVPVAVFDVDAILEAIERER---ITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFET- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  756 VLNAYGPTETtVCATMYEvNGEIQKEISNIpIGKPIANSEVFVISPfntlcpsgvvGELFIGGDGVANGYLNQKEKTEga 835
Cdd:cd17638   144 VLTAYGLTEA-GVATMCR-PGDDAETVATT-CGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATA-- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  836 fisldKSYNRDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI----VC 911
Cdd:cd17638   209 -----EAIDADGWLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgevgKA 282

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 446581728  912 FYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKL 957
Cdd:cd17638   283 FVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 1535-2033 1.53e-29

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 129.27  E-value: 1.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1535 IQEQFYMQVDRQPERIAIATAT-ESLTYRQLnMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAayIPI 1613
Cdd:PRK08633  617 LAEAWIDTAKRNWSRLAVADSTgGELSYGKA-LTGALALARLLKRELKDEENVGILLPPSVAGALANLALLLAGK--VPV 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1614 DVKYP--EDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSI--------IEDIyRTTINDDVKILN------------- 1670
Cdd:PRK08633  694 NLNYTasEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELpenvkviyLEDL-KAKISKVDKLTAllaarllparllk 772

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1671 -------KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQ---FYsHSFDSSVSeIFSTLLNGA 1740
Cdd:PRK08633  773 rlygptfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpFF-HSFGLTVT-LWLPLLEGI 850

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1741 ELYLLSDEQRYSTVeyAQAIQETQATISdLPTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKnqVQ 1820
Cdd:PRK08633  851 KVVYHPDPTDALGI--AKLVAKHRATIL-LGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFG--IR 925

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1821 LVNEYGPTE----ATVSamyyfIP-VLEGEN-----NLLGSVpiGIPISNTKVHILN-SYMQYCPVGCMGELYIESLGLA 1889
Cdd:PRK08633  926 ILEGYGATEtspvASVN-----LPdVLAADFkrqtgSKEGSV--GMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVM 998

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1890 QGYWKQKEKTKQAfisnpFSEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT 1969
Cdd:PRK08633  999 KGYLGDPEKTAEV-----IKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFA 1073

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1970 QT------EGGMLLQAYykTVDGIGIEKNKLAIHLSNvLPEYMVPKYYSHVLEIPITANGKIDFEKLPKI 2033
Cdd:PRK08633 1074 VTavpdekKGEKLVVLH--TCGAEDVEELKRAIKESG-LPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 475-971 1.70e-29

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 125.30  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKSPNQIAIS--MGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPK 552
Cdd:PRK09088    1 IAFHARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  553 FPEKRIEYILKDSESQMIITKKEyrglVERFAIHTIYLEDFHYANSIENIASTHTI--EDAAYIIYTSGSTGLPKGVVVP 630
Cdd:PRK09088   81 LSASELDALLQDAEPRLLLGDDA----VAAGRTDVEDLAAFIASADALEPADTPSIppERVSLILFTSGTSGQPKGVMLS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  631 HKgvvNLSYSVIN---TFHLGKEDVFL----QFATIifdASIMEIFPILLCGGRMHLISEIE-KRSAEEFINVSqkYGIT 702
Cdd:PRK09088  157 ER---NLQQTAHNfgvLGRVDAHSSFLcdapMFHII---GLITSVRPVLAVGGSILVSNGFEpKRTLGRLGDPA--LGIT 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  703 NVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWqskLGLKIPVLNAYGPTETTVCATMYEVNGEIQKEI 782
Cdd:PRK09088  229 HYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGW---LDDGIPMVDGFGMSEAGTVFGMSVDCDVIRAKA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  783 SNipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldksynrdKKMYCTGDLVRLLANG 862
Cdd:PRK09088  306 GA--AGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTG--------DGWFRTGDIARRDADG 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  863 NLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI----VCFYLSKDNTELKQEALKTFLSESLPDFM 938
Cdd:PRK09088  376 FFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgevgYLAIVPADGAPLDLERIRSHLSTRLAKYK 455

                         490       500       510
                  ....*....|....*....|....*....|...
gi 446581728  939 MPNYIFHLESFPVSPSGKLDRKKLELQIPSLLE 971
Cdd:PRK09088  456 VPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 469-969 1.79e-29

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 126.43  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAISMGDQSI--TYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVY 546
Cdd:PRK12583   18 QTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  547 VPIDPKFPEKRIEYILKDSESQMIITKKEYRG----------------------LVERFAI--HTIYL---EDFHYANSI 599
Cdd:PRK12583   98 VNINPAYRASELEYALGQSGVRWVICADAFKTsdyhamlqellpglaegqpgalACERLPElrGVVSLapaPPPGFLAWH 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  600 ENIASTHTIEDAAY--------------IIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDV-------FLQFAT 658
Cdd:PRK12583  178 ELQARGETVSREALaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRlcvpvplYHCFGM 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  659 IIFDASIME-----IFPIllcggrMHLISEIEKRSAEEFiNVSQKYGItnvvlPTAFfklIA--DMPKEMLLKLNSVKRL 731
Cdd:PRK12583  258 VLANLGCMTvgaclVYPN------EAFDPLATLQAVEEE-RCTALYGV-----PTMF---IAelDHPQRGNFDLSSLRTG 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  732 FVGGETLPAESVRKWQSKLGLKiPVLNAYGPTETTVCATMYEVNGEIQKEISNIpiGKPIANSEVFVISPFNTLCPSGVV 811
Cdd:PRK12583  323 IMAGAPCPIEVMRRVMDEMHMA-EVQIAYGMTETSPVSLQTTAADDLERRVETV--GRTQPHLEVKVVDPDGATVPRGEI 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  812 GELFIGGDGVANGYLNQKEKTEgafisldKSYNRDKKMYcTGDLVRLLANGNLEFIGRKDNQVkIRG-YRIELDEIEGTL 890
Cdd:PRK12583  400 GELCTRGYSVMKGYWNNPEATA-------ESIDEDGWMH-TGDLATMDEQGYVRIVGRSKDMI-IRGgENIYPREIEEFL 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  891 FKHPEVRDAVVF----TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL-ELQ 965
Cdd:PRK12583  471 FTHPAVADVQVFgvpdEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMrEIS 550


                  ....
gi 446581728  966 IPSL 969
Cdd:PRK12583  551 IEEL 554
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 496-962 2.60e-29

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 125.44  E-value: 2.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  496 TYYELQQRSNQIVNYLRENDLKKGQRVSitmereidTIVW--------ILGILKSGGVYVPIDPKFPEKRIEYILKDSES 567
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVA--------TLAWnthrhlelYYAVPGMGAVLHTINPRLFPEQIAYIINHAED 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  568 QMIITKKEYRGLVERFA------IHTIYLEDFHYANSIEN---------IASTHTIED--------AAYIIYTSGSTGLP 624
Cdd:cd12119    99 RVVFVDRDFLPLLEAIAprlptvEHVVVMTDDAAMPEPAGvgvlayeelLAAESPEYDwpdfdentAAAICYTSGTTGNP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  625 KGVVVPHKGVVNLSYSVINT--FHLGKEDVFLQFaTIIFDASIMEI-FPILLCGGRMHLISEieKRSAEEFINVSQKYGI 701
Cdd:cd12119   179 KGVVYSHRSLVLHAMAALLTdgLGLSESDVVLPV-VPMFHVNAWGLpYAAAMVGAKLVLPGP--YLDPASLAELIEREGV 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  702 TNVV-LPTaFFKLIADMPKEMLLKLNSVKRLFVGGETLPaESVRKWQSKLGlkIPVLNAYGPTETTVCATM-----YEVN 775
Cdd:cd12119   256 TFAAgVPT-VWQGLLDHLEANGRDLSSLRRVVIGGSAVP-RSLIEAFEERG--VRVIHAWGMTETSPLGTVarppsEHSN 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  776 GEIQKEIS-NIPIGKPIANSEVFVISPFNTLCPS--GVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMYcT 852
Cdd:cd12119   332 LSEDEQLAlRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALT--------EDGWLR-T 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  853 GDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI----VCFYLSKDNTELKQEALKT 928
Cdd:cd12119   403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWgerpLAVVVLKEGATVTAEELLE 482

                         490       500       510
                  ....*....|....*....|....*....|....
gi 446581728  929 FLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd12119   483 FLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 487-962 3.20e-29

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 123.74  E-value: 3.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  487 AISMGDQSITYYELQQRSNQIVNYLR-ENDLKKGQRVSItmeREIDTIVWI---LGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:cd05958     3 CLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLL---RGSNSPELVacwFGIQKAGAIAVATMPLLRPKELAYIL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIItkkeyrgLVERFAihtiyledfhyansieniasthTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLS--YS 640
Cdd:cd05958    80 DKARITVAL-------CAHALT----------------------ASDDICILAFTSGTTGAPKATMHFHRDPLASAdrYA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  641 ViNTFHLGKEDVFLQFATIIFDASI--MEIFPiLLCGGRMHLIseiEKRSAEEFINVSQKYGITNVV-LPTAFFKLIADM 717
Cdd:cd05958   131 V-NVLRLREDDRFVGSPPLAFTFGLggVLLFP-FGVGASGVLL---EEATPDLLLSAIARYKPTVLFtAPTAYRAMLAHP 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  718 PKEMLLkLNSVKRLFVGGETLPAESVRKWQSKLGlkIPVLNAYGPTEttvcatMYEVNgeiqkeISNIP-------IGKP 790
Cdd:cd05958   206 DAAGPD-LSSLRKCVSAGEALPAALHRAWKEATG--IPIIDGIGSTE------MFHIF------ISARPgdarpgaTGKP 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  791 IANSEVFVISPFNTLCPSGVVGELFIGGDgvaNGYLNQKEKTEgafisldKSYNRDKKMYcTGDLVRLLANGNLEFIGRK 870
Cdd:cd05958   271 VPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQ-------RTYVQGGWNI-TGDTYSRDPDGYFRHQGRS 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  871 DNQVKIRGYRIELDEIEGTLFKHPEVRD-AVVFTYQNDKIV---CFYLSKDN---TELKQEALKTFLSESLPDFMMPNYI 943
Cdd:cd05958   340 DDMIVSGGYNIAPPEVEDVLLQHPAVAEcAVVGHPDESRGVvvkAFVVLRPGvipGPVLARELQDHAKAHIAPYKYPRAI 419

                         490
                  ....*....|....*....
gi 446581728  944 FHLESFPVSPSGKLDRKKL 962
Cdd:cd05958   420 EFVTELPRTATGKLQRFAL 438
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 483-957 3.75e-29

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 125.77  E-value: 3.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAI----SMGDQS--ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEK 556
Cdd:cd17634    67 GDRTAIiyegDDTSQSrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  557 RIEYILKDSESQMIITKKE---------YRGLVERFA------IHTIYL-------------EDFHYANSIENIASTHT- 607
Cdd:cd17634   147 AVAGRIIDSSSRLLITADGgvragrsvpLKKNVDDALnpnvtsVEHVIVlkrtgsdidwqegRDLWWRDLIAKASPEHQp 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  608 ----IEDAAYIIYTSGSTGLPKGVVVPHKG-VVNLSYSVINTFHLGKEDVFLQFATI--IFDASIMeIFPILLCGGRMHL 680
Cdd:cd17634   227 eamnAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVgwVTGHSYL-LYGPLACGATTLL 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  681 ISEIEKR-SAEEFINVSQKYGITNVVL-PTAFFKLIADMPKEML-LKLNSVKRLFVGGETLPAESVRKWQSKLGL-KIPV 756
Cdd:cd17634   306 YEGVPNWpTPARMWQVVDKHGVNILYTaPTAIRALMAAGDDAIEgTDRSSLRILGSVGEPINPEAYEWYWKKIGKeKCPV 385

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  757 LNAYGPTETT-VCATMYEVNGEIQKEISNipigKPIANSEVFVISPFNTLCPSGVVGELFIGGD--GVANGYLNQKEKTE 833
Cdd:cd17634   386 VDTWWQTETGgFMITPLPGAIELKAGSAT----RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFE 461

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  834 GAFISldksynRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF----TYQNDKI 909
Cdd:cd17634   462 QTYFS------TFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgiphAIKGQAP 535

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446581728  910 VCFYLSK----DNTELKQEaLKTFLSESLPDFMMPNYIFHLESFPVSPSGKL 957
Cdd:cd17634   536 YAYVVLNhgvePSPELYAE-LRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1542-2032 6.84e-29

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 124.47  E-value: 6.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1542 QVDRQPERIAIATAT-ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPED 1620
Cdd:PRK06087   32 TARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1621 RINYIVRDSEACRIITSNKFKS---------------HLN-----------VSDYKVSIIEDIYrTTINDDVKIlnKPDD 1674
Cdd:PRK06087  112 ELVWVLNKCQAKMFFAPTLFKQtrpvdlilplqnqlpQLQqivgvdklapaTSSLSLSQIIADY-EPLTTAITT--HGDE 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1675 LAYVIYTSGSTGKPKGTLLTHK----------GVLNLVeWRNEVFQISPNDKVTQFYsHSfdssvseIFSTLLNGAELYL 1744
Cdd:PRK06087  189 LAAVLFTSGTEGLPKGVMLTHNnilaseraycARLNLT-WQDVFMMPAPLGHATGFL-HG-------VTAPFLIGARSVL 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1745 LsdeQRYSTVEYAQAIQETQATISDLPTVFFNELstsLTKLDSEKIR--SLRFIIMGGEAASTNAIR-SWQNTFKnqvqL 1821
Cdd:PRK06087  260 L---DIFTPDACLALLEQQRCTCMLGATPFIYDL---LNLLEKQPADlsALRFFLCGGTTIPKKVAReCQQRGIK----L 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1822 VNEYGPTEatvSAMYYFIPvLEGENNLLGSVPiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQ 1901
Cdd:PRK06087  330 LSVYGSTE---SSPHAVVN-LDDPLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTAR 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1902 AFisnpfseDNSKRLYrTGDLVRWLPNGNIEFMGRKdKQVKIR-GHRIELGEIEDAMLQLEGISQAVVTqtegGM----- 1975
Cdd:PRK06087  405 AL-------DEEGWYY-SGDLCRMDEAGYIKITGRK-KDIIVRgGENISSREVEDILLQHPKIHDACVV----AMpderl 471

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728 1976 --------LLQAYYKTvdgigIEKNKLAIHLSNV-LPEYMVPKYYSHVLEIPITANGKIDFEKLPK 2032
Cdd:PRK06087  472 gerscayvVLKAPHHS-----LTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 493-901 9.43e-29

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 122.85  E-value: 9.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIIt 572
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  573 kkeyrglverfaihtiyledfhyansIENiasthTIEDAAYIIYTSGSTGLPKGVVVPHKgvvNLSYSVINT---FHLGK 649
Cdd:cd17640    83 --------------------------VEN-----DSDDLATIIYTSGTTGNPKGVMLTHA---NLLHQIRSLsdiVPPQP 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  650 EDVFLQFATI--IFDASImEIFpILLCGGRM------HLISEIEKRSAEEFINVSQKYGItnvvLPTAFFKLIADMP--K 719
Cdd:cd17640   129 GDRFLSILPIwhSYERSA-EYF-IFACGCSQaytsirTLKDDLKRVKPHYIVSVPRLWES----LYSGIQKQVSKSSpiK 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  720 EMLLKL----NSVKRLFVGGETLPAESVRKWQSklgLKIPVLNAYGPTETTVCATMYEVNGEIQKEisnipIGKPIANSE 795
Cdd:cd17640   203 QFLFLFflsgGIFKFGISGGGALPPHVDTFFEA---IGIEVLNGYGLTETSPVVSARRLKCNVRGS-----VGRPLPGTE 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  796 VFVISPF-NTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAfISLDKSYNrdkkmycTGDLVRLLANGNLEFIGR-KDNQ 873
Cdd:cd17640   275 IKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGWFN-------TGDLGWLTCGGELVLTGRaKDTI 346

                         410       420
                  ....*....|....*....|....*...
gi 446581728  874 VKIRGYRIELDEIEGTLFKHPEVRDAVV 901
Cdd:cd17640   347 VLSNGENVEPQPIEEALMRSPFIEQIMV 374
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 482-962 1.36e-28

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 122.88  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  482 SPNQIAISMG--DQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIE 559
Cdd:PRK13391   10 TPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  560 YILKDSESQMIITKKEYRGLVERFAIHT-------IYLED------FHYANSIENIASThTIED---AAYIIYTSGSTGL 623
Cdd:PRK13391   90 YIVDDSGARALITSAAKLDVARALLKQCpgvrhrlVLDGDgelegfVGYAEAVAGLPAT-PIADeslGTDMLYSSGTTGR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  624 PKGVV--VPHKGVV---NLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGrMHLIseIEKRSAEEFINVSQK 698
Cdd:PRK13391  169 PKGIKrpLPEQPPDtplPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGG-TVIV--MEHFDAEQYLALIEE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  699 YGITNV-VLPTAFFKLIaDMPKEMLLK--LNSVKRLFVGGETLPA---ESVRKWqskLGlkiPVLNA-YGPTE---TTVC 768
Cdd:PRK13391  246 YGVTHTqLVPTMFSRML-KLPEEVRDKydLSSLEVAIHAAAPCPPqvkEQMIDW---WG---PIIHEyYAATEglgFTAC 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  769 ATMyevngeiQKEISNIPIGKPIAnSEVFVISPFNTLCPSGVVGELFIGGdGVANGYLNQKEKTegafislDKSYNRDKK 848
Cdd:PRK13391  319 DSE-------EWLAHPGTVGRAMF-GDLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKT-------AEARHPDGT 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  849 MYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK--------IVCFYLSKDNTE 920
Cdd:PRK13391  383 WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDlgeevkavVQPVDGVDPGPA 462

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 446581728  921 LKQEALKtFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK13391  463 LAAELIA-FCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 469-966 1.48e-28

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 123.33  E-value: 1.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVyvp 548
Cdd:COG1021    25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  549 idPKF--PEKR---IEYILKDSESQMIITKKE-----YRGLVERFAI------HTIYL---EDFH-----YANSIENIAS 604
Cdd:COG1021   102 --PVFalPAHRraeISHFAEQSEAVAYIIPDRhrgfdYRALARELQAevpslrHVLVVgdaGEFTsldalLAAPADLSEP 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  605 THTIEDAAYIIYTSGSTGLPKGVVVPHKG-VVNLSYSVINTfHLGKEDVFLQFATII--FDASIMEIFPILLCGGRMHLI 681
Cdd:COG1021   180 RPDPDDVAFFQLSGGTTGLPKLIPRTHDDyLYSVRASAEIC-GLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTVVLA 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  682 SEIEKRSAEEFInvsQKYGITNVVL-PTAFfKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKipVLNAY 760
Cdd:COG1021   259 PDPSPDTAFPLI---ERERVTVTALvPPLA-LLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCT--LQQVF 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  761 GPTETTVCATMYEVNGEI----QkeisnipiGKPI-ANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGA 835
Cdd:COG1021   333 GMAEGLVNYTRLDDPEEVilttQ--------GRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARA 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  836 FIsldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVkIR-GYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI---VC 911
Cdd:COG1021   405 FT--------PDGFYRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgerSC 475

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  912 FYLSKDNTELKQEALKTFLSES-LPDFMMPNYIFHLESFPVSPSGKLDRKKLELQI 966
Cdd:COG1021   476 AFVVPRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1535-2033 1.50e-28

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 122.66  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1535 IQEQFYMQvdrqPERIAIATATESLTYRQLNMSSNQVAQHLL-EKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPI 1613
Cdd:PRK06839    8 IEKRAYLH----PDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1614 DVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTIND--DVKILN---KPDDLAYVI-YTSGSTGK 1687
Cdd:PRK06839   84 NIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEieDRKIDNfveKNESASFIIcYTSGTTGK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1688 PKGTLLTHKGVL-NLVewrNEVFQISPNdkvtqfyshSFDSSVSEI------------FSTLLNGAELYLlsdEQRYSTV 1754
Cdd:PRK06839  164 PKGAVLTQENMFwNAL---NNTFAIDLT---------MHDRSIVLLplfhiggiglfaFPTLFAGGVIIV---PRKFEPT 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1755 EYAQAIQETQATIS-DLPTVffNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQntfKNQVQLVNEYGPTEATVS 1833
Cdd:PRK06839  229 KALSMIEKHKVTVVmGVPTI--HQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFI---DRGFLFGQGFGMTETSPT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1834 AmyyFIPVLEGENNLLGSvpIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAfISNPFsedns 1913
Cdd:PRK06839  304 V---FMLSEEDARRKVGS--IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW----- 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1914 krlYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIE 1990
Cdd:PRK06839  373 ---LCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVgrqHVKWGEIPIAFIVKKSSSVLI 449

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 446581728 1991 KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKI 2033
Cdd:PRK06839  450 EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 40-323 1.65e-28

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 121.02  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   40 IIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIK-QLIQKNVEFDIPIKDLTAFknTEQKSILKNFLESIVNEK 118
Cdd:cd19536    28 YTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPvQVVHRQAQVPVTELDLTPL--EEQLDPLRAYKEETKIRR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  119 FSLEEGPLFKFHIIKFSEDT-FILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKSNVEFE-SPYKNLVKHEESFIDSA 196
Cdd:cd19536   106 FDLGRAPLVRAALVRKDERErFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYKPLSLPPaQPYRDFVAHERASIQQA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  197 iykEGSSYWKDYLQG-ELTPTEFPIDfnKMNEKRYTDKNISKNINSDLfyQIQCFAKKNNISIYRVMLSTYCTLLHQMTN 275
Cdd:cd19536   186 ---ASERYWREYLAGaTLATLPALSE--AVGGGPEQDSELLVSVPLPV--RSRSLAKRSGIPLSTLLLAAWALVLSRHSG 258

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 446581728  276 AEEIIVGIPINTRP--YTEERNTFGYFVNTLPIRITIEkGETFKGILNKV 323
Cdd:cd19536   259 SDDVVFGTVVHGRSeeTTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRA 307
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 462-901 1.76e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 123.15  E-value: 1.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  462 ALTYPNLKTLDQLiDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYL-RENDLKKGQRVSITMEREIDTIVWILGIL 540
Cdd:PRK08314    4 SLTLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  541 KSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKEYRG----LVERFAI-HTI------------------YLEDFHYAN 597
Cdd:PRK08314   83 RANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPkvapAVGNLRLrHVIvaqysdylpaepeiavpaWLRAEPPLQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  598 SIENIASTH----------------TIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLqfatiif 661
Cdd:PRK08314  163 ALAPGGVVAwkealaaglappphtaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVL------- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  662 daSIMEIFPI----------LLCGGRMHLISEIEKRSAEEFInvsQKYGITN-VVLPTAFFKLIADmPKEMLLKLNSVKR 730
Cdd:PRK08314  236 --AVLPLFHVtgmvhsmnapIYAGATVVLMPRWDREAAARLI---ERYRVTHwTNIPTMVVDFLAS-PGLAERDLSSLRY 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  731 LFVGGETLPAESVRKWQSKLGLkiPVLNAYGPTETtvcatmyevngeIQKEISNIP-------IGKPIANSEVFVISPfN 803
Cdd:PRK08314  310 IGGGGAAMPEAVAERLKELTGL--DYVEGYGLTET------------MAQTHSNPPdrpklqcLGIPTFGVDARVIDP-E 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  804 TL--CPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLD-KSYNRdkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYR 880
Cdd:PRK08314  375 TLeeLPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEIDgKRFFR------TGDLGRMDEEGYFFITDRLKRMINASGFK 448

                         490       500
                  ....*....|....*....|.
gi 446581728  881 IELDEIEGTLFKHPEVRDAVV 901
Cdd:PRK08314  449 VWPAEVENLLYKHPAIQEACV 469
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 491-959 2.01e-28

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 121.78  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  491 GDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMI 570
Cdd:cd05914     4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  571 ITKKEyrglverfaihtiyledfhyansieniasthtiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKE 650
Cdd:cd05914    84 FVSDE---------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKG 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  651 DVFLQF--------------------ATIIF--DASIMEIFPILLCGGRMHLIS----EIEKRSAEEFINVSQ----KYG 700
Cdd:cd05914   131 DKILSIlplhhiypltftlllpllngAHVVFldKIPSAKIIALAFAQVTPTLGVpvplVIEKIFKMDIIPKLTlkkfKFK 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  701 ITNVVLPTAFFKLIAdmpKEMLLKLNSVKRLFV-GGETLPAEsVRKWQSKLGlkIPVLNAYGPTETT--VCATMYEvnge 777
Cdd:cd05914   211 LAKKINNRKIRKLAF---KKVHEAFGGNIKEFViGGAKINPD-VEEFLRTIG--FPYTIGYGMTETApiISYSPPN---- 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  778 iqkEISNIPIGKPIANSEVFVISPFntlcPSGVVGELFIGGDGVANGYLNQKEKTEGAFIsldksynRDKKMYcTGDLVR 857
Cdd:cd05914   281 ---RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFD-------KDGWFH-TGDLGK 345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  858 LLANGNLEFIGRKDNQ-VKIRGYRIELDEIEGTLFKHPEVRDAVVFTyQNDK----IVCFYLSKDNTELKQEALKTFLSE 932
Cdd:cd05914   346 IDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVV-QEKKlvalAYIDPDFLDVKALKQRNIIDAIKW 424

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 446581728  933 SLPDFM---MPNY------IFHLESFPVSPSGKLDR 959
Cdd:cd05914   425 EVRDKVnqkVPNYkkiskvKIVKEEFEKTPKGKIKR 460
PRK08315 PRK08315
AMP-binding domain protein; Validated
 469-962 4.50e-28

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 121.84  E-value: 4.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAISMGDQSI--TYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVY 546
Cdd:PRK08315   16 QTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  547 VPIDPKFPEKRIEYILKDSESQMIITKKEYRG---------LVERFAI---------------HTIYLEDFHYANSI--- 599
Cdd:PRK08315   96 VTINPAYRLSELEYALNQSGCKALIAADGFKDsdyvamlyeLAPELATcepgqlqsarlpelrRVIFLGDEKHPGMLnfd 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  600 ENIASTHTIEDAAY--------------IIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKED-------VFLQF-- 656
Cdd:PRK08315  176 ELLALGRAVDDAELaarqatldpddpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcipvpLYHCFgm 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  657 -----------ATIIFdasIMEIF-PILLcggrMHLISEiEKRSAeefinvsqKYGItnvvlPTAFfklIA--DMPKEML 722
Cdd:PRK08315  256 vlgnlacvthgATMVY---PGEGFdPLAT----LAAVEE-ERCTA--------LYGV-----PTMF---IAelDHPDFAR 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  723 LKLNSVKRLFVGGETLPAESVRKWQSKLGLKiPVLNAYGPTETTVCATMYEVNGEIQKEISNIpiGKPIANSEVFVISPF 802
Cdd:PRK08315  312 FDLSSLRTGIMAGSPCPIEVMKRVIDKMHMS-EVTIAYGMTETSPVSTQTRTDDPLEKRVTTV--GRALPHLEVKIVDPE 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  803 -NTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAfisLDKsynrDKKMYcTGDLVRLLANGNLEFIGR-KDnqVKIRG-- 878
Cdd:PRK08315  389 tGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA---IDA----DGWMH-TGDLAVMDEEGYVNIVGRiKD--MIIRGge 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  879 --Y-RieldEIEGTLFKHPEVRDAVVFTYQNDK---IVC-FYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPV 951
Cdd:PRK08315  459 niYpR----EIEEFLYTHPKIQDVQVVGVPDEKygeEVCaWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPM 534

                         570
                  ....*....|.
gi 446581728  952 SPSGKLDRKKL 962
Cdd:PRK08315  535 TVTGKIQKFKM 545
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 1557-2025 5.30e-28

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 120.24  E-value: 5.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1557 ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIIT 1636
Cdd:cd05914     6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1637 SNkfkshlnvsdykvsiiediyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK 1716
Cdd:cd05914    86 SD---------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDK 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1717 VTQF--YSHSFDSSVSEIFStLLNGAELYLLsDEQRYSTVEYAQAIQETQATISDLPTVFF----NELSTSLT------- 1783
Cdd:cd05914   133 ILSIlpLHHIYPLTFTLLLP-LLNGAHVVFL-DKIPSAKIIALAFAQVTPTLGVPVPLVIEkifkMDIIPKLTlkkfkfk 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1784 ---KLDSEKIRSL-------------RFIIMGGEAASTNAIRSWqntFKNQVQLVNEYGPTEATvsamyyfiPVLEG--- 1844
Cdd:cd05914   211 lakKINNRKIRKLafkkvheafggniKEFVIGGAKINPDVEEFL---RTIGFPYTIGYGMTETA--------PIISYspp 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1845 ENNLLGSVpiGIPISNTKVHILNSYmqycPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVR 1924
Cdd:cd05914   280 NRIRLGSA--GKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW--------FHTGDLGK 345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1925 WLPNGNIEFMGRKdKQVKI--RGHRIELGEIEDAMLQLEGISQAVVTQTEGGMLLQAY----YKTVDGIGIEKNKLAI-- 1996
Cdd:cd05914   346 IDAEGYLYIRGRK-KEMIVlsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYidpdFLDVKALKQRNIIDAIkw 424

                         490       500       510
                  ....*....|....*....|....*....|....
gi 446581728 1997 ----HLSNVLPEY-MVPKYYSHVLEIPITANGKI 2025
Cdd:cd05914   425 evrdKVNQKVPNYkKISKVKIVKEEFEKTPKGKI 458
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1547-2025 1.40e-27

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 119.30  E-value: 1.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:PRK03640   16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSNKFKSHLNVSdyKVSIIEDIYRTTINdDVKILNK--PDDLAYVIYTSGSTGKPKGTLLTHK-------- 1696
Cdd:PRK03640   96 DDAEVKCLITDDDFEAKLIPG--ISVKFAELMNGPKE-EAEIQEEfdLDEVATIMYTSGTTGKPKGVIQTYGnhwwsavg 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1697 GVLNLvewrnevfQISPNDK----VTQFYShsfdSSVSEIFSTLLNGAELYLlsdEQRYSTVEYAQAIQETQAT-ISDLP 1771
Cdd:PRK03640  173 SALNL--------GLTEDDCwlaaVPIFHI----SGLSILMRSVIYGMRVVL---VEKFDAEKINKLLQTGGVTiISVVS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1772 TVffneLSTSLTKLDSEKI-RSLRFIIMGGEAASTNAIRSWQntfKNQVQLVNEYGPTEaTVSAmyyfIPVLEGENNL-- 1848
Cdd:PRK03640  238 TM----LQRLLERLGEGTYpSSFRCMLLGGGPAPKPLLEQCK---EKGIPVYQSYGMTE-TASQ----IVTLSPEDALtk 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1849 LGSVpiGIPISNTKVHILNSyMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlyRTGDLVRWLPN 1928
Cdd:PRK03640  306 LGSA--GKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF---------KTGDIGYLDEE 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1929 GNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEG---GMLLQAYykTVDGIGIEKNKLAIHLSNVLPEY 2005
Cdd:PRK03640  374 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDdkwGQVPVAF--VVKSGEVTEEELRHFCEEKLAKY 451

                         490       500
                  ....*....|....*....|
gi 446581728 2006 MVPKYYSHVLEIPITANGKI 2025
Cdd:PRK03640  452 KVPKRFYFVEELPRNASGKL 471
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 1535-2026 1.81e-27

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 119.11  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1535 IQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGiKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPID 1614
Cdd:PRK07638    3 ITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1615 VKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNKPD---DLAYVIYTSGSTGKPKGT 1691
Cdd:PRK07638   82 IKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENvqnAPFYMGFTSGSTGKPKAF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1692 LLTHKGVLNLVEWRNEVFQISPNDKV----TQFYSHSFDSSVseifSTLLNGAELYLLsdeQRYSTVEYAQAIQetQATI 1767
Cdd:PRK07638  162 LRAQQSWLHSFDCNVHDFHMKREDSVliagTLVHSLFLYGAI----STLYVGQTVHLM---RKFIPNQVLDKLE--TENI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1768 SDLPTVffNELSTSLTKLDsEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATvsamyyFIPVLEGENN 1847
Cdd:PRK07638  233 SVMYTV--PTMLESLYKEN-RVIENKMKIISSGAKWEAEAKEKIKNIFPY-AKLYEFYGASELS------FVTALVDEES 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1848 LLGSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYwkqkektkqaFISNPFSEDNSKRLYRTGDLVRWL- 1926
Cdd:PRK07638  303 ERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY----------IIGGVLARELNADGWMTVRDVGYEd 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1927 PNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEG---GMLLQAYyktVDGiGIEKNKLAIHLSNVLP 2003
Cdd:PRK07638  373 EEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDsywGEKPVAI---IKG-SATKQQLKSFCLQRLS 448

                         490       500
                  ....*....|....*....|...
gi 446581728 2004 EYMVPKYYSHVLEIPITANGKID 2026
Cdd:PRK07638  449 SFKIPKEWHFVDEIPYTNSGKIA 471
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 469-963 4.10e-27

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 118.63  E-value: 4.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAI----SMGD-QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSG 543
Cdd:PRK08008    7 QHLRQMWDDLADVYGHKTALifesSGGVvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  544 GVYVPIDPKFPEKRIEYILKDSESQMIITKKEYRGLVERFA------IHTIYLEDFHyANSIENIAS------------- 604
Cdd:PRK08008   87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQqedatpLRHICLTRVA-LPADDGVSSftqlkaqqpatlc 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  605 ---THTIEDAAYIIYTSGSTGLPKGVVVPHkgvVNLSYSVINT---FHLGKEDVFLqfatiifdaSIMEIF--------- 669
Cdd:PRK08008  166 yapPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFAGYYSawqCALRDDDVYL---------TVMPAFhidcqctaa 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  670 -PILLCGGRMHLIseiEKRSAEEFINVSQKYGITnvvlptaffkLIADMPkeMLLKlnsvkrlfvggeTLPAESVRKW-- 746
Cdd:PRK08008  234 mAAFSAGATFVLL---EKYSARAFWGQVCKYRAT----------ITECIP--MMIR------------TLMVQPPSANdr 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  747 ---------------QSKLGL----KIPVLNAYGPTETTVcatmyEVNGEIQKEISNIP-IGKPIANSEVFVISPFNTLC 806
Cdd:PRK08008  287 qhclrevmfylnlsdQEKDAFeerfGVRLLTSYGMTETIV-----GIIGDRPGDKRRWPsIGRPGFCYEAEIRDDHNRPL 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  807 PSGVVGELFIGG---DGVANGYLNQKEKTEgafisldKSYNRDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIEL 883
Cdd:PRK08008  362 PAGEIGEICIKGvpgKTIFKEYYLDPKATA-------KVLEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSC 433

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  884 DEIEGTLFKHPEVRDAVVF----TYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDR 959
Cdd:PRK08008  434 VELENIIATHPKIQDIVVVgikdSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIK 513


                  ....
gi 446581728  960 KKLE 963
Cdd:PRK08008  514 KNLK 517
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
469-962 6.79e-27

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 118.44  E-value: 6.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  469 KTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYL-RENDLKKGQRVSITMEREIDTIVWILGILKSGGVYV 547
Cdd:PRK08751   25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  548 PIDPKFPEKRIEYILKDSESQMIITKKEYRGLVER----------------------------FAIHTI--YLEDFHYAN 597
Cdd:PRK08751  105 NVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQviadtpvkqvittglgdmlgfpkaalvnFVVKYVkkLVPEYRING 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  598 SIE-----NIASTHTI-------EDAAYIIYTSGSTGLPKGVVVPHKGVV-NLS-----YSVINTFHLGKEdvflqfaTI 659
Cdd:PRK08751  185 AIRfrealALGRKHSMptlqiepDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMQqahqwLAGTGKLEEGCE-------VV 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  660 IFDASIMEIFPI-------LLCGGRMHLISEieKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLF 732
Cdd:PRK08751  258 ITALPLYHIFALtanglvfMKIGGCNHLISN--PRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTL 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  733 VGGETLPAESVRKWQSKLGLkiPVLNAYGPTETTVCA-----TMYEVNGEIqkeisnipiGKPIANSEVFVISPFNTLCP 807
Cdd:PRK08751  336 GGGMAVQRSVAERWKQVTGL--TLVEAYGLTETSPAAcinplTLKEYNGSI---------GLPIPSTDACIKDDAGTVLA 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  808 SGVVGELFIGGDGVANGYLNQKEKTEgafisldKSYNRDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIE 887
Cdd:PRK08751  405 IGEIGELCIKGPQVMKGYWKRPEETA-------KVMDADGWLH-TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIE 476

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581728  888 GTLFKHP---EVRDAVVFTYQNDKIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK08751  477 DVIAMMPgvlEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 479-965 7.55e-27

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 117.96  E-value: 7.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRI 558
Cdd:PRK07786   27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  559 EYILKDSESQMIITKKEYRGLVE--RFAIHTIYL--------ED--FHYANSIENIASTHTIED-----AAYIIYTSGST 621
Cdd:PRK07786  107 AFLVSDCGAHVVVTEAALAPVATavRDIVPLLSTvvvaggssDDsvLGYEDLLAEAGPAHAPVDipndsPALIMYTSGTT 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  622 GLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFD-ASIMEIFPILLCGGRMhLISEIEKRSAEEFINVSQKYG 700
Cdd:PRK07786  187 GRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPT-VIYPLGAFDPGQLLDVLEAEK 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  701 ITNVVL-PTAFFKLIADM-PKEMLLKLnsvkRLFVGGETLPAESVRKWQSKLGLKIPVLNAYGPTETTVCATMYEVNGEI 778
Cdd:PRK07786  266 VTGIFLvPAQWQAVCAEQqARPRDLAL----RVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAI 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  779 QKEISnipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynrDKKMYCTGDLVRL 858
Cdd:PRK07786  342 RKLGS---VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---------AGGWFHSGDLVRQ 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  859 LANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK-----IVCFYLSKDNTELKQEALKTFLSES 933
Cdd:PRK07786  410 DEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwgevpVAVAAVRNDDAALTLEDLAEFLTDR 489

                         490       500       510
                  ....*....|....*....|....*....|..
gi 446581728  934 LPDFMMPNYIFHLESFPVSPSGKLDRKKLELQ 965
Cdd:PRK07786  490 LARYKHPKALEIVDALPRNPAGKVLKTELRER 521
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 483-962 9.44e-27

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 117.01  E-value: 9.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSItMEREIDTIV-WILGILKSGGVYVPIDPKFPEKRIEYI 561
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAV-LAPNTPAMYeLHFGVPMAGAVLNALNTRLDAEEIAFI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  562 LKDSESQMIITKKE--YRGLVER----FAIhtIYLEDfhyansiENiasthtieDAAYIIYTSGSTGLPKGVVVPHKGVV 635
Cdd:cd12118    97 LRHSEAKVLFVDREfeYEDLLAEgdpdFEW--IPPAD-------EW--------DPIALNYTSGTTGRPKGVVYHHRGAY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  636 NLSYSVINTFHLGKEDVFLQfatiifdasimeIFPILLCGGRMHLISE---------IEKRSAEEFINVSQKYGITNVVL 706
Cdd:cd12118   160 LNALANILEWEMKQHPVYLW------------TLPMFHCNGWCFPWTVaavggtnvcLRKVDAKAIYDLIEKHKVTHFCG 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  707 PTAFFKLIADMPKEMLLKLNSVKRLFVGGeTLPAESVRKWQSKLGLKipVLNAYGPTET----TVCATMYEVNGEIQKEI 782
Cdd:cd12118   228 APTVLNMLANAPPSDARPLPHRVHVMTAG-APPPAAVLAKMEELGFD--VTHVYGLTETygpaTVCAWKPEWDELPTEER 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  783 SNIPI--GKP-IANSEVFVISPfNTLCP---SGV-VGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKkMYCTGDL 855
Cdd:cd12118   305 ARLKArqGVRyVGLEEVDVLDP-ETMKPvprDGKtIGEIVFRGNIVMKGYLKNPEATAEAF--------RGG-WFHSGDL 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  856 VRLLANGNLEFIGR-KDnqVKIR-GYRIELDEIEGTLFKHPEVRDAVVFTYQNDK---IVCFYLS-KDNTELKQEALKTF 929
Cdd:cd12118   375 AVIHPDGYIEIKDRsKD--IIISgGENISSVEVEGVLYKHPAVLEAAVVARPDEKwgeVPCAFVElKEGAKVTEEEIIAF 452

                         490       500       510
                  ....*....|....*....|....*....|...
gi 446581728  930 LSESLPDFMMPNYIFHLEsFPVSPSGKLDRKKL 962
Cdd:cd12118   453 CREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 39-436 9.52e-27

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 115.48  E-value: 9.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   39 PIIIKLKGNLQIEVLKKALTTIVQSHPALRTIF--KKRDEKIKQLIQKNVefDIPIKDLTafknTEQKSiLKNFLESIVN 116
Cdd:cd19542    25 HFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLKSL--DPPIEEVE----TDEDS-LDALTRDLLD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  117 EKFsLEEGPLFKFHIIK--FSEDTFILHLmfHHIIYDGWSLGVFIRQLSNTYgellQGKSNVEFeSPYKNLVKHeesfID 194
Cdd:cd19542    98 DPT-LFGQPPHRLTLLEtsSGEVYLVLRI--SHALYDGVSLPIILRDLAAAY----NGQLLPPA-PPFSDYISY----LQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  195 SAIYKEGSSYWKDYLQGeLTPTEFPIDFNKMNEKRYTDKNISKNINsdlfyqIQCFAKKNNISIYRVMLSTYCTLLHQMT 274
Cdd:cd19542   166 SQSQEESLQYWRKYLQG-ASPCAFPSLSPKRPAERSLSSTRRSLAK------LEAFCASLGVTLASLFQAAWALVLARYT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  275 NAEEIIVGIPINTR--PYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAITYKHNSYSHIVKdlnlntnTN 352
Cdd:cd19542   239 GSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQR-------AL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  353 HNMVYSTAFNTMkipeLKIPDIESTVLTDCKRVNPFNMTWRIMRYE---------GETENKIEVDYNSALYKPESISDLV 423
Cdd:cd19542   312 GLWPSGTLFNTL----VSYQNFEASPESELSGSSVFELSAAEDPTEypvavevepSGDSLKVSLAYSTSVLSEEQAEELL 387

                         410
                  ....*....|...
gi 446581728  424 ERYIYLLQKLMKN 436
Cdd:cd19542   388 EQFDDILEALLAN 400
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 484-901 9.76e-27

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 118.07  E-value: 9.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  484 NQIAI----SMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIE 559
Cdd:PRK04319   59 DKVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  560 YILKDSESQMIITKKEyrgLVERF------AIHTIYLED---------FHYANSIENIASTHTI-----EDAAYIIYTSG 619
Cdd:PRK04319  139 DRLEDSEAKVLITTPA---LLERKpaddlpSLKHVLLVGedveegpgtLDFNALMEQASDEFDIewtdrEDGAILHYTSG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  620 STGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFAtiifD-----ASIMEIFPILLCGGRMhLISEiEKRSAEEFIN 694
Cdd:PRK04319  216 STGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVYWCTA----DpgwvtGTSYGIFAPWLNGATN-VIDG-GRFSPERWYR 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  695 VSQKYGITnvV---LPTAFfkliadmpkEMLLK----------LNSVKRLFVGGETLPAESVRKWQSKLGLkiPVLNAYG 761
Cdd:PRK04319  290 ILEDYKVT--VwytAPTAI---------RMLMGagddlvkkydLSSLRHILSVGEPLNPEVVRWGMKVFGL--PIHDNWW 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  762 PTETtvcatmyevnGEIQkeISNIP--------IGKPIANSEVFVISPFNTLCPSGVVGELFI--GGDGVANGYLNQKEK 831
Cdd:PRK04319  357 MTET----------GGIM--IANYPamdikpgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEK 424

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  832 TEGAFISldksynrdkKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVV 901
Cdd:PRK04319  425 YESYFAG---------DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 456-962 2.67e-26

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 116.24  E-value: 2.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  456 KEMNSNALTYPNlkTLDQLIdLQALKS-PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIV 534
Cdd:PRK06188    1 QATMADLLHSGA--TYGHLL-VSALKRyPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  535 WILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII---TKKEYRG--LVERFA--IHTIYLEDFHYANSIENIAST-- 605
Cdd:PRK06188   78 AIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIvdpAPFVERAlaLLARVPslKHVLTLGPVPDGVDLLAAAAKfg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  606 -------HTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLqFATIIFDASIMEIFPILLCGGRM 678
Cdd:PRK06188  158 paplvaaALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFL-MCTPLSHAGGAFFLPTLLRGGTV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  679 HLiseIEKRSAEEFINVSQKYGITNVVL-PTAFFKLIaDMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlkiPVL 757
Cdd:PRK06188  237 IV---LAKFDPAEVLRAIEEQRITATFLvPTMIYALL-DHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFG---PIF 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  758 -NAYGPTETTVCATMY---EVNGEIQKEISNipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTE 833
Cdd:PRK06188  310 aQYYGQTEAPMVITYLrkrDHDPDDPKRLTS--CGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETA 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  834 GAFisldksynRDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----I 909
Cdd:PRK06188  388 EAF--------RDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwgeaV 458

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446581728  910 VCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK06188  459 TAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1105-1332 3.13e-26

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 114.12  E-value: 3.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1105 HIYIE---PSLNKDILQDTIRFLVERHEMLRTVFIErNGepRQVILNSIAIDLI--HDeIEHMSKKEQQEYIRTTINQTD 1179
Cdd:cd19535    27 HAYLEfdgEDLDPDRLERAWNKLIARHPMLRAVFLD-DG--TQQILPEVPWYGItvHD-LRGLSEEEAEAALEELRERLS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1180 HTPFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYsafakrRNPE--LPTISNRYVDYAEWEQv 1257
Cdd:cd19535   103 HRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALY------EDPGepLPPLELSFRDYLLAEQ- 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581728 1258 QLNLGRWDTEKSYWMAELAAPLPILNLPLdfsRNRQSTNKGTVF---EMKLDNEMKESLKQVCEQENISMYMLFLAAY 1332
Cdd:cd19535   176 ALRETAYERARAYWQERLPTLPPAPQLPL---AKDPEEIKEPRFtrrEHRLSAEQWQRLKERARQHGVTPSMVLLTAY 250
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
471-965 3.36e-26

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 115.75  E-value: 3.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  471 LDQLIDLQALKSPNQIAISMGDQ--SITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVP 548
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  549 IDPKFPEK-----------RIEYILKDSESQMIITKKEYRGLVERFAIHTIYLE---DFHYANSIENIASTHTIE----D 610
Cdd:PRK05852   98 LDPALPIAeqrvrsqaagaRVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGgtlSVHLDAATEPTPATSTPEglrpD 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  611 AAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAE 690
Cdd:PRK05852  178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAH 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  691 EFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLP--AESVRKWQSKLGlkIPVLNAYGPTETTVC 768
Cdd:PRK05852  258 TFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPltAETAQALQTEFA--APVVCAFGMTEATHQ 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  769 ATMYEVNGEIQKE---ISNIPIGKPIAnSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISldkSYNR 845
Cdd:PRK05852  336 VTTTQIEGIGQTEnpvVSTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD---GWLR 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  846 dkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF-----TYqNDKIVCFYLSKDNTE 920
Cdd:PRK05852  412 ------TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFgvpdqLY-GEAVAAVIVPRESAP 484

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 446581728  921 LKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQ 965
Cdd:PRK05852  485 PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 483-958 4.80e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 115.37  E-value: 4.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:PRK07798   17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITKKEYRGLVERF------AIHTIYLEDfhyANSIENIASTHTIEDAA-----------------YIIYTSG 619
Cdd:PRK07798   97 DDSDAVALVYEREFAPRVAEVlprlpkLRTLVVVED---GSGNDLLPGAVDYEDALaagsperdfgerspddlYLLYTGG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  620 STGLPKGVVVPHK--------GVVNLSYSVINTFHLGKEDVFLQFATIIFD-------ASIMEIFPILLCGGRMhLISEI 684
Cdd:PRK07798  174 TTGMPKGVMWRQEdifrvllgGRDFATGEPIEDEEELAKRAAAGPGMRRFPapplmhgAGQWAAFAALFSGQTV-VLLPD 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  685 EKRSAEEFINVSQKYGITNVVlptaffkLIAD-MPKEMLLKLNSVKR-----LFV---GGETLPAESVRKWQSKLGlKIP 755
Cdd:PRK07798  253 VRFDADEVWRTIEREKVNVIT-------IVGDaMARPLLDALEARGPydlssLFAiasGGALFSPSVKEALLELLP-NVV 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  756 VLNAYGPTETTVCATMYEVNGEIQKEISNIPIGKpiansEVFVISP-FNTLCP-SGVVGELFIGGDgVANGYLNQKEKTE 833
Cdd:PRK07798  325 LTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP-----RTVVLDEdGNPVEPgSGEIGWIARRGH-IPLGYYKDPEKTA 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  834 GAFISLDksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----I 909
Cdd:PRK07798  399 ETFPTID-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERwgqeV 473

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 446581728  910 VCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:PRK07798  474 VAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 1542-2025 5.95e-26

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 115.24  E-value: 5.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1542 QVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDR 1621
Cdd:PRK06155   30 QAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1622 INYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRttINDDVKILN---------------------KPDDLAYVIY 1680
Cdd:PRK06155  110 LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWL--LDAPASVSVpagwstaplppldapapaaavQPGDTAAILY 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1681 TSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLlsdEQRYSTVEYAQAI 1760
Cdd:PRK06155  188 TSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL---EPRFSASGFWPAV 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1761 QETQATISDLPTVFFNELsTSLTKLDSEKIRSLRFIIMGGEAAStnAIRSWQNTFKnqVQLVNEYGPTEaTVSAMYYFIP 1840
Cdd:PRK06155  265 RRHGATVTYLLGAMVSIL-LSQPARESDRAHRVRVALGPGVPAA--LHAAFRERFG--VDLLDGYGSTE-TNFVIAVTHG 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1841 vlEGENNLLGSVPIGIPIsntkvHILNSYMQYCPVGCMGELYI---ESLGLAQGYWKQKEKTKQAFisnpfsednsKRL- 1916
Cdd:PRK06155  339 --SQRPGSMGRLAPGFEA-----RVVDEHDQELPDGEPGELLLradEPFAFATGYFGMPEKTVEAW----------RNLw 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1917 YRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV--TQTE-GGMLLQAYYKTVDGIGIEKNK 1993
Cdd:PRK06155  402 FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfpVPSElGEDEVMAAVVLRDGTALEPVA 481

                         490       500       510
                  ....*....|....*....|....*....|..
gi 446581728 1994 LAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK06155  482 LVRHCEPRLAYFAVPRYVEFVAALPKTENGKV 513
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 1558-2025 6.75e-26

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 113.21  E-value: 6.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEAcriits 1637
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1638 nkfkshlnvsdykvsiiediyrttinddvkilnKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK- 1716
Cdd:cd05912    75 ---------------------------------KLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNw 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1717 ---VTQFYShsfdSSVSEIFSTLLNGAELYLLsdeQRYSTVEYAQAIQETQATISDLPTVFFNELstsLTKLDSEKIRSL 1793
Cdd:cd05912   122 lcaLPLFHI----SGLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRL---LEILGEGYPNNL 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1794 RFIIMGGEAASTNAIRSWQNtfKNqVQLVNEYGPTEaTVSAMYYFIPvlEGENNLLGSVpiGIPISNTKVHILNSYMqyc 1873
Cdd:cd05912   192 RCILLGGGPAPKPLLEQCKE--KG-IPVYQSYGMTE-TCSQIVTLSP--EDALNKIGSA--GKPLFPVELKIEDDGQ--- 260

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1874 PVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlyRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEI 1953
Cdd:cd05912   261 PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF---------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEI 331

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1954 EDAMLQLEGISQAVV---TQTEGGMLLQAYYktVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05912   332 EEVLLSHPAIKEAGVvgiPDDKWGQVPVAFV--VSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKL 404
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 493-966 7.43e-26

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 115.08  E-value: 7.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIIT 572
Cdd:PLN02330   54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  573 KKEYRGLVERFAIHTIYLEDFHYANSI---------ENIASTHTIE-----DAAYIIYTSGSTGLPKGVVVPHKGVV-NL 637
Cdd:PLN02330  134 NDTNYGKVKGLGLPVIVLGEEKIEGAVnwkelleaaDRAGDTSDNEeilqtDLCALPFSSGTTGISKGVMLTHRNLVaNL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  638 SYSVintFHLGKEDVFlQFATIifdaSIMEIFPI-----LLCG-----GRMHLISEIEKRSaeeFIN--VSQKYGITNVV 705
Cdd:PLN02330  214 CSSL---FSVGPEMIG-QVVTL----GLIPFFHIygitgICCAtlrnkGKVVVMSRFELRT---FLNalITQEVSFAPIV 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  706 lPTAFFKLIAD-MPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTvCATMYEVNGE----IQK 780
Cdd:PLN02330  283 -PPIILNLVKNpIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFP-GVQVQEAYGLTEHS-CITLTHGDPEkghgIAK 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  781 EISnipIGKPIANSEVFVISPFNTLC-PSGVVGELFIGGDGVANGYLNQKEKTegafislDKSYNRDKKMYcTGDLVRLL 859
Cdd:PLN02330  360 KNS---VGFILPNLEVKFIDPDTGRSlPKNTPGELCVRSQCVMQGYYNNKEET-------DRTIDEDGWLH-TGDIGYID 428

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  860 ANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK-----IVCFYLSKDNTElKQEALKTFLSESL 934
Cdd:PLN02330  429 DDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEageipAACVVINPKAKE-SEEDILNFVAANV 507

                         490       500       510
                  ....*....|....*....|....*....|..
gi 446581728  935 PDFMMPNYIFHLESFPVSPSGKLDRKKLELQI 966
Cdd:PLN02330  508 AHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKM 539
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1532-2025 9.01e-26

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 114.97  E-value: 9.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1532 FQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLL-EKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAY 1610
Cdd:PRK08751   24 FRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1611 IPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLN--VSDYKVS---------IIEDIYRTTINDDVKILNK-------- 1671
Cdd:PRK08751  104 VNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQqvIADTPVKqvittglgdMLGFPKAALVNFVVKYVKKlvpeyrin 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 -----------------------PDDLAYVIYTSGSTGKPKGTLLTHKgvlNLV-------EWRNEVFQISPNDKVT--- 1718
Cdd:PRK08751  184 gairfrealalgrkhsmptlqiePDDIAFLQYTGGTTGVAKGAMLTHR---NLVanmqqahQWLAGTGKLEEGCEVVita 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1719 -QFYsHSFDSSVSEIFSTLLNGAElYLLSDEQRYSTveYAQAIQETQAT-ISDLPTVFFNELSTSltKLDSEKIRSLRFI 1796
Cdd:PRK08751  261 lPLY-HIFALTANGLVFMKIGGCN-HLISNPRDMPG--FVKELKKTRFTaFTGVNTLFNGLLNTP--GFDQIDFSSLKMT 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1797 IMGGEAASTNAIRSWQNTfkNQVQLVNEYGPTEATVSAMyyFIPVLEGENNllGSvpIGIPISNTKVHILNSYMQYCPVG 1876
Cdd:PRK08751  335 LGGGMAVQRSVAERWKQV--TGLTLVEAYGLTETSPAAC--INPLTLKEYN--GS--IGLPIPSTDACIKDDAGTVLAIG 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1877 CMGELYIESLGLAQGYWKQKEKTKQAFisnpfsedNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDA 1956
Cdd:PRK08751  407 EIGELCIKGPQVMKGYWKRPEETAKVM--------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDV 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728 1957 MLQLEGISQ--AV-VTQTEGGMLLQAYYKTVDGiGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK08751  479 IAMMPGVLEvaAVgVPDEKSGEIVKVVIVKKDP-ALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKI 549
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 472-960 1.55e-25

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 114.51  E-value: 1.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  472 DQLIDLQALKSPNQIAIS-MGD----QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVY 546
Cdd:cd05968    64 EQLLDKWLADTRTRPALRwEGEdgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  547 VPIDPKFPEKRIEYILKDSESQMIITKKEY--RG-----------------LVERFAIHTIYLEDFHYAN---------- 597
Cdd:cd05968   144 VPIFSGFGKEAAATRLQDAEAKALITADGFtrRGrevnlkeeadkacaqcpTVEKVVVVRHLGNDFTPAKgrdlsydeek 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  598 --SIENIASTHTiEDAAYIIYTSGSTGLPKGVVVPHKGV-VNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLC 674
Cdd:cd05968   224 etAGDGAERTES-EDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  675 GGRMHLISEI-EKRSAEEFINVSQKYGITNVVL-PTAFFKLIA--DMPKEMLlKLNSVKRLFVGGETLPAESVRkW--QS 748
Cdd:cd05968   303 GATMVLYDGApDHPKADRLWRMVEDHEITHLGLsPTLIRALKPrgDAPVNAH-DLSSLRVLGSTGEPWNPEPWN-WlfET 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  749 KLGLKIPVLNAYGPTEttvcatmyeVNGEIqkeISNIPIgKPIANSEvfvispFNTLCP--------------SGVVGEL 814
Cdd:cd05968   381 VGKGRNPIINYSGGTE---------ISGGI---LGNVLI-KPIKPSS------FNGPVPgmkadvldesgkpaRPEVGEL 441

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  815 FIGGD--GVANGYLNQKEKTegafisLDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFK 892
Cdd:cd05968   442 VLLAPwpGMTRGFWRDEDRY------LETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNA 515

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728  893 HPEVRDAVVFTYQND----KIVCFYLSKDN---TELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRK 960
Cdd:cd05968   516 HPAVLESAAIGVPHPvkgeAIVCFVVLKPGvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRR 590
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
472-962 1.65e-25

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 114.00  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  472 DQLIDL---QALKSPNQIA-ISMGdQSITYYELQQRSNQIVNYLrENDLK--KGQRVSITMEREIDTIVWILGILKSGGV 545
Cdd:PRK08974   23 QSLVDMfeqAVARYADQPAfINMG-EVMTFRKLEERSRAFAAYL-QNGLGlkKGDRVALMMPNLLQYPIALFGILRAGMI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  546 YVPIDPKFPEKRIEYILKDSESQMIItkkeyrgLVERFAiHTiyLEDFHYANSIENIAST-------------------- 605
Cdd:PRK08974  101 VVNVNPLYTPRELEHQLNDSGAKAIV-------IVSNFA-HT--LEKVVFKTPVKHVILTrmgdqlstakgtlvnfvvky 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  606 -----------HTI---------------------EDAAYIIYTSGSTGLPKGVVVPHKGVV-NL-----SYSVIntFHL 647
Cdd:PRK08974  171 ikrlvpkyhlpDAIsfrsalhkgrrmqyvkpelvpEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLeqakaAYGPL--LHP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  648 GKEDVFLQFATI-IFDASIMEIFPILLcGGRMHLISEieKRSAEEFINVSQKY---GITNVvlPTAFFKLIADmpkEMLL 723
Cdd:PRK08974  249 GKELVVTALPLYhIFALTVNCLLFIEL-GGQNLLITN--PRDIPGFVKELKKYpftAITGV--NTLFNALLNN---EEFQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  724 KLN-SVKRLFVGGETLPAESV-RKWQSKLGLKIpvLNAYGPTETT--VCATMYEVNGEiqkeisNIPIGKPIANSEVFVI 799
Cdd:PRK08974  321 ELDfSSLKLSVGGGMAVQQAVaERWVKLTGQYL--LEGYGLTECSplVSVNPYDLDYY------SGSIGLPVPSTEIKLV 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  800 SPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMyCTGDLVRLLANGNLEFIGRKDNQVKIRGY 879
Cdd:PRK08974  393 DDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI--------KDGWL-ATGDIAVMDEEGFLRIVDRKKDMILVSGF 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  880 RIELDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKDNTeLKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSG 955
Cdd:PRK08974  464 NVYPNEIEDVVMLHPKVLEVAAVGVPSEvsgeAVKIFVVKKDPS-LTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVG 542


                  ....*..
gi 446581728  956 KLDRKKL 962
Cdd:PRK08974  543 KILRREL 549
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 1534-2025 2.10e-25

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 113.36  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1534 NIQEQF---YMQVDR----QPERIAIA---TATES--LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSML 1601
Cdd:cd05970    11 NVPENFnfaYDVVDAmakeYPDKLALVwcdDAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1602 GILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITS---------NKFKSHLNVSDYKVSIIEDI------YRTTINDDV 1666
Cdd:cd05970    91 ALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIaednipeeiEKAAPECPSKPKLVWVGDPVpegwidFRKLIKNAS 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1667 KILNKP--------DDLAYVIYTSGSTGKPK----------GTLLTHKgvlnlvEWRNevfqISPNDKVTQFYSHSFDSS 1728
Cdd:cd05970   171 PDFERPtansypcgEDILLVYFSSGTTGMPKmvehdftyplGHIVTAK------YWQN----VREGGLHLTVADTGWGKA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1729 V-SEIFSTLLNGAELYLLsDEQRYSTVEYAQAIQETQAT-ISDLPTVFFNELSTSLTKLDsekIRSLRFIIMGGEAASTN 1806
Cdd:cd05970   241 VwGKIYGQWIAGAAVFVY-DYDKFDPKALLEKLSKYGVTtFCAPPTIYRFLIREDLSRYD---LSSLRYCTTAGEALNPE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1807 AIRSWQNtfKNQVQLVNEYGPTEATVSAMYYfiPVLEGENnllGSvpIGIPISNTKVHILNSYMQYCPVGCMGELYIES- 1885
Cdd:cd05970   317 VFNTFKE--KTGIKLMEGFGQTETTLTIATF--PWMEPKP---GS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTs 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1886 ----LGLAQGYWKQKEKTKQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLE 1961
Cdd:cd05970   388 kgkpVGLFGGYYKDAEKTAEVWHDG---------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHP 458

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446581728 1962 GISQAVVT---------QTEGGMLLQAYYKTVDGIgieKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05970   459 AVLECAVTgvpdpirgqVVKATIVLAKGYEPSEEL---KKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 486-962 2.28e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 113.07  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  486 IAISMG--DQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREID--TIVWilGILKSGGVYVPIDPKFPEKRIEYI 561
Cdd:PRK08276    1 PAVIMApsGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEffEVYW--AARRSGLYYTPINWHLTAAEIAYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  562 LKDSESQMIITKKEYRGLVERFAIHT--------IYLEDFHYANSIENIASTHT---IED---AAYIIYTSGSTGLPKGV 627
Cdd:PRK08276   79 VDDSGAKVLIVSAALADTAAELAAELpagvplllVVAGPVPGFRSYEEALAAQPdtpIADetaGADMLYSSGTTGRPKGI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  628 VVPHKGV------VNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLiseIEKRSAEEFINVSQKYGI 701
Cdd:PRK08276  159 KRPLPGLdpdeapGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVV---MEKFDAEEALALIERYRV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  702 TNVVL-PTAFFKLIAdMPKEMLLK--LNSVKRLFVGGETLPAESVRK---WqskLGlkiPVLNA-YGPTE---TTVCatm 771
Cdd:PRK08276  236 THSQLvPTMFVRMLK-LPEEVRARydVSSLRVAIHAAAPCPVEVKRAmidW---WG---PIIHEyYASSEgggVTVI--- 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  772 yevNGE--IQKEISnipIGKPIAnSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEgafisldKSYNrDKKM 849
Cdd:PRK08276  306 ---TSEdwLAHPGS---VGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTA-------AARN-PHGW 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  850 YCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKDNTELKQE- 924
Cdd:PRK08276  371 VTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEemgeRVKAVVQPADGADAGDAl 450

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 446581728  925 --ALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK08276  451 aaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
2163-2445 5.83e-25

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 107.76  E-value: 5.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLPsTTIYCLVRENEdqvigaklkermefyfGKEILQKLkERVELIEGDLslmnlgLDSK 2242
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARG-HEVVGLDRSPP----------------GAANLAAL-PGVEFVRGDL------RDPE 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2243 QLDHLKKNVESIIHCGGEVRH-YGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKEfeffesdfDR 2320
Cdd:COG0451    57 ALAAALAGVDAVVHLAAPAGVgEEDPDETLEVNVEGTLNLLEAARAAGVkRFVYASSSSVYGDGEGPIDE--------DT 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 GQNLDNLYLESKFQGEKMVREAMEK-GVRATIYRVGNLVgnsktGKFQYNINENAFYRLLKGICLsSIAPDVNTYVDLTP 2399
Cdd:COG0451   129 PLRPVSPYGASKLAAELLARAYARRyGLPVTILRPGNVY-----GPGDRGVLPRLIRRALAGEPV-PVFGDGDQRRDFIH 202

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 446581728 2400 VDYGSLAITELSYKANTVNKTMHICNPNQLKWDQFINSL-QAFGYDI 2445
Cdd:COG0451   203 VDDVARAIVLALEAPAAPGGVYNVGGGEPVTLRELAEAIaEALGRPP 249
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 1557-2024 6.17e-25

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 110.91  E-value: 6.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1557 ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAayipidvkyPEDRINYIVRdSEACRiit 1636
Cdd:cd05940     2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAALINYNLR-GESLA--- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1637 snkfksH-LNVSDYKVSIIediyrttinddvkilnkpdDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPND 1715
Cdd:cd05940    69 ------HcLNVSSAKHLVV-------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSD 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1716 KvtqFYS-----HSFDSSVSeIFSTLLNGAELYLlsdEQRYSTVEYAQAIQETQATIsdlpTVFFNELSTSLTKL---DS 1787
Cdd:cd05940   124 V---LYTclplyHSTALIVG-WSACLASGATLVI---RKKFSASNFWDDIRKYQATI----FQYIGELCRYLLNQppkPT 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1788 EKIRSLRfiimggeAASTNAIRS--WQNtFKN--QVQLVNE-YGPTEATVSAMYYF-IPVLEGENNLLGSVPIGIPI--- 1858
Cdd:cd05940   193 ERKHKVR-------MIFGNGLRPdiWEE-FKErfGVPRIAEfYAATEGNSGFINFFgKPGAIGRNPSLLRKVAPLALvky 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1859 ---SNTKVHILNSYMQYCPVGCMGEL--YIESLGLAQGYWKQKEKTKQaFISNPFSEDNskRLYRTGDLVRWLPNGNIEF 1933
Cdd:cd05940   265 dleSGEPIRDAEGRCIKVPRGEPGLLisRINPLEPFDGYTDPAATEKK-ILRDVFKKGD--AWFNTGDLMRLDGEGFWYF 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1934 MGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV-----TQTEG--GMllqAYYKTVDGIGIEKNKLAIHLSNVLPEYM 2006
Cdd:cd05940   342 VDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqvPGTDGraGM---AAIVLQPNEEFDLSALAAHLEKNLPGYA 418

                         490
                  ....*....|....*...
gi 446581728 2007 VPKYYSHVLEIPITANGK 2024
Cdd:cd05940   419 RPLFLRLQPEMEITGTFK 436
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 19-320 7.50e-25

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 110.24  E-value: 7.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   19 GQEALWIAHQMeieigMN-----NEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIF--KKRDEKIKQ--LIQKNVEFD 89
Cdd:cd19532     7 GQSRFWFLQQY-----LEdpttfNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQgvLASSPLRLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   90 IpikdltafKNTEQKSILKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYgel 169
Cdd:cd19532    82 H--------VQISDEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY--- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  170 lQGKSNVEFESPYKNLVKHEESFIDSAIYKEGSSYWKDylqgELTPTEFPID---FNK----MNEKRYTDKNISKNINSD 242
Cdd:cd19532   151 -NGQPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKS----EFSTLPEPLPllpFAKvksrPPLTRYDTHTAERRLDAA 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581728  243 LFYQIQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRITIEKGETFKGIL 320
Cdd:cd19532   226 LAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVL 303
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 1540-1968 8.61e-25

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 111.91  E-value: 8.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1540 YMQVDRQPE-----RIAI----ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGA-- 1608
Cdd:PRK04319   46 YEAIDRHADggrkdKVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAiv 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1609 -----AYIPIDVKypeDRINyivrDSEACRIITSNKFKS-----------HLNVSDYKVSIIEDIYR-----TTINDDVK 1667
Cdd:PRK04319  126 gplfeAFMEEAVR---DRLE----DSEAKVLITTPALLErkpaddlpslkHVLLVGEDVEEGPGTLDfnalmEQASDEFD 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1668 ILN-KPDDLAYVIYTSGSTGKPKGTLLTHKGVLN---LVEWrneVFQISPNDK---------VTqfyshsfdSSVSEIFS 1734
Cdd:PRK04319  199 IEWtDREDGAILHYTSGSTGKPKGVLHVHNAMLQhyqTGKY---VLDLHEDDVywctadpgwVT--------GTSYGIFA 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1735 TLLNGAElyLLSDEQRYSTVEYAQAIQETQATI-SDLPTVFfnelsTSLTKLDSEKIR-----SLRFIIMGGEAASTNAI 1808
Cdd:PRK04319  268 PWLNGAT--NVIDGGRFSPERWYRILEDYKVTVwYTAPTAI-----RMLMGAGDDLVKkydlsSLRHILSVGEPLNPEVV 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1809 RSWQNTFKNQVQlvNEYGPTE--ATVSAMYYFIPVlegennLLGSvpIGIPISNTKVHILNSYMQYCPVGCMGELYIESl 1886
Cdd:PRK04319  341 RWGMKVFGLPIH--DNWWMTEtgGIMIANYPAMDI------KPGS--MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKK- 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1887 G---LAQGYWKQKEKTKQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGI 1963
Cdd:PRK04319  410 GwpsMMRGIWNNPEKYESYFAGD---------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV 480


                  ....*
gi 446581728 1964 SQAVV 1968
Cdd:PRK04319  481 AEAGV 485
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 1545-2025 9.36e-25

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 111.18  E-value: 9.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK08316   23 RYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAY 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSNKFKSHL-------NVSDYKVSIIE----------DIYRTTINDDVKILNKP---DDLAYVIYTSGS 1684
Cdd:PRK08316  103 ILDHSGARAFLVDPALAPTAeaalallPVDTLILSLVLggreapggwlDFADWAEAGSVAEPDVEladDDLAQILYTSGT 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1685 TGKPKGTLLTHKGVLNlvEWRNEVF--QISPNDKVTQ----FYSHSFDSSVSEIF-----STLLNGAELYLLSDeqrysT 1753
Cdd:PRK08316  183 ESLPKGAMLTHRALIA--EYVSCIVagDMSADDIPLHalplYHCAQLDVFLGPYLyvgatNVILDAPDPELILR-----T 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1754 VEYAQAIQETQAtisdlPTVFFNELSTSLtkLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKnQVQLVNEYGPTEATVS 1833
Cdd:PRK08316  256 IEAERITSFFAP-----PTVWISLLRHPD--FDTRDLSSLRKGYYGASIMPVEVLKELRERLP-GLRFYNCYGQTEIAPL 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1834 AMyyfipVLEGENNL--LGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsed 1911
Cdd:PRK08316  328 AT-----VLGPEEHLrrPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF--- 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1912 nskrlyRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGMLLQAYYKTV---DGIG 1988
Cdd:PRK08316  398 ------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVvpkAGAT 471

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 446581728 1989 IEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK08316  472 VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 607-971 1.10e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 111.63  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  607 TIEDAAYIIYTSGSTGLPKGVVVPHKGVV-NLS----------------YSVINTFHLGKEDVFLQFATIIfdASIMEIF 669
Cdd:PRK05605  217 TPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAqgkawvpglgdgpervLAALPMFHAYGLTLCLTLAVSI--GGELVLL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  670 PILlcggRMHLISEIEKRSAEEFINVsqkygitnvvLPTAFFKlIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSK 749
Cdd:PRK05605  295 PAP----DIDLILDAMKKHPPTWLPG----------VPPLYEK-IAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKL 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  750 LGLKIpvLNAYGPTETTVCATMYEVNGEIQkeisniP--IGKPIANSEVFVISPFN---TLcPSGVVGELFIGGDGVANG 824
Cdd:PRK05605  360 TGGLL--VEGYGLTETSPIIVGNPMSDDRR------PgyVGVPFPDTEVRIVDPEDpdeTM-PDGEEGELLVRGPQVFKG 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  825 YLNQKEKTEGAFisLDksynrdkKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTY 904
Cdd:PRK05605  431 YWNRPEETAKSF--LD-------GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGL 501

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728  905 QND----KIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQIPSLLE 971
Cdd:PRK05605  502 PREdgseEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLG 572
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 1543-2025 1.40e-24

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 110.29  E-value: 1.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIATATES--LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPED 1620
Cdd:cd05923    11 ASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1621 RINYIVRDSEACRIITSN----------KFKSHLNVSDYKVSIIEDIYRTTINDDVKilnKPDDLAYVIYTSGSTGKPKG 1690
Cdd:cd05923    91 ELAELIERGEMTAAVIAVdaqvmdaifqSGVRVLALSDLVGLGEPESAGPLIEDPPR---EPEQPAFVFYTSGTTGLPKG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1691 TLLTHKG----VL-------NLVEWRNEVFQISPNDKVTQFYShsfdssvseIFSTLLNGAELYLLSDEqrYSTVEYAQA 1759
Cdd:cd05923   168 AVIPQRAaesrVLfmstqagLRHGRHNVVLGLMPLYHVIGFFA---------VLVAALALDGTYVVVEE--FDPADALKL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1760 IQETQATISDLPTVFFNELSTSLTkLDSEKIRSLRFIIMGGeAASTNAIRSWQNTFKnQVQLVNEYGPTEATVSamyyfi 1839
Cdd:cd05923   237 IEQERVTSLFATPTHLDALAAAAE-FAGLKLSSLRHVTFAG-ATMPDAVLERVNQHL-PGEKVNIYGTTEAMNS------ 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1840 pvLEGENNLLGSVpiGIPISNTKVH---ILNSYMQYCPVGCMGELYIESLGLA--QGYWKQKEKTkqafisnpfSEDNSK 1914
Cdd:cd05923   308 --LYMRDARTGTE--MRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEAT---------AKKLQD 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1915 RLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEK 1991
Cdd:cd05923   375 GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgvaDERWGQSVTACVVPREGTLSAD 454

                         490       500       510
                  ....*....|....*....|....*....|....
gi 446581728 1992 NKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05923   455 ELDQFCRASELADFKRPRRYFFLDELPKNAMNKV 488
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1672-2025 1.52e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 107.75  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 PDDLAYVIYTSGSTGKPKGTLLTHKGVLN---LVEWRNEVfqiSPNDKV---TQFYsHSFDSSVSeIFSTLLNGAELYLL 1745
Cdd:cd05917     1 PDDVINIQFTSGTTGSPKGATLTHHNIVNngyFIGERLGL---TEQDRLcipVPLF-HCFGSVLG-VLACLTHGATMVFP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1746 SDEqrYSTVEYAQAIQETQAT-ISDLPTVFFNELstSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFkNQVQLVNE 1824
Cdd:cd05917    76 SPS--FDPLAVLEAIEKEKCTaLHGVPTMFIAEL--EHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVM-NMKDVTIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1825 YGPTEAT-VSAMYYFIPVLEGENNLLGSVpigipISNTKVHILNSY-MQYCPVGCMGELYIESLGLAQGYWKQKEKTKQA 1902
Cdd:cd05917   151 YGMTETSpVSTQTRTDDSIEKRVNTVGRI-----MPHTEAKIVDPEgGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1903 fISNpfsednsKRLYRTGDLVRWLPNGNIEFMGR-KDkqVKIRG-HRIELGEIEDAMLQLEGISQAVVTqteG------G 1974
Cdd:cd05917   226 -IDG-------DGWLHTGDLAVMDEDGYCRIVGRiKD--MIIRGgENIYPREIEEFLHTHPKVSDVQVV---GvpderyG 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446581728 1975 MLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05917   293 EEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 475-974 1.76e-24

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 111.25  E-value: 1.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKS-PNQIAI------SMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVY- 546
Cdd:cd05967    56 LDRHVEAGrGDQIALiydspvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHs 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  547 ------------VPID---PKF---------PEKRIEYI-LKDSESQMIITKKEY-----RGLVERFAIHTiyLEDFHYA 596
Cdd:cd05967   136 vvfggfaakelaSRIDdakPKLivtascgiePGKVVPYKpLLDKALELSGHKPHHvlvlnRPQVPADLTKP--GRDLDWS 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  597 NSIEN--------IASTHTIedaaYIIYTSGSTGLPKGVVVPHKG-VVNLSYSVINTFHLGKEDVFlqfatiiFDASIME 667
Cdd:cd05967   214 ELLAKaepvdcvpVAATDPL----YILYTSGTTGKPKGVVRDNGGhAVALNWSMRNIYGIKPGDVW-------WAASDVG 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  668 --------IFPILLCGGRMHLISEIEKRS--AEEFINVSQKYGITNV-VLPTAFFKLIADMPKEMLLK---LNSVKRLFV 733
Cdd:cd05967   283 wvvghsyiVYGPLLHGATTVLYEGKPVGTpdPGAFWRVIEKYQVNALfTAPTAIRAIRKEDPDGKYIKkydLSSLRTLFL 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  734 GGETLPAESVrKWQSKLgLKIPVLNAYGPTETTVCATMYEVNgeiqkeISNIPI-----GKPIANSEVFVISPFNTLCPS 808
Cdd:cd05967   363 AGERLDPPTL-EWAENT-LGVPVIDHWWQTETGWPITANPVG------LEPLPIkagspGKPVPGYQVQVLDEDGEPVGP 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  809 GVVGELFIGGD---GVANGYLNQKEKTEGAFISLDKSYnrdkkmYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDE 885
Cdd:cd05967   435 NELGNIVIKLPlppGCLLTLWKNDERFKKLYLSKFPGY------YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGE 508

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  886 IEGTLFKHPEVRDAVVFTYQnDKI-----VCFYLSKDNTELKQEALKTFL----SESLPDFMMPNYIFHLESFPVSPSGK 956
Cdd:cd05967   509 MEESVLSHPAVAECAVVGVR-DELkgqvpLGLVVLKEGVKITAEELEKELvalvREQIGPVAAFRLVIFVKRLPKTRSGK 587

                         570       580
                  ....*....|....*....|....*
gi 446581728  957 LDRKKL-------ELQIPSLLENMQ 974
Cdd:cd05967   588 ILRRTLrkiadgeDYTIPSTIEDPS 612
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 494-963 1.98e-24

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 110.70  E-value: 1.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  494 SITYYELQQRSNQIVNYLREN-DLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIIT 572
Cdd:PLN02574   66 SISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  573 KKEYRGLVERFAIHTIYL-EDFHYANSIENIASTHTI---------------EDAAYIIYTSGSTGLPKGVVVPHKgvvN 636
Cdd:PLN02574  146 SPENVEKLSPLGVPVIGVpENYDFDSKRIEFPKFYELikedfdfvpkpvikqDDVAAIMYSSGTTGASKGVVLTHR---N 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  637 LSYSVintfhlgkeDVFLQFATIIFDAS--------IMEIFPI----LLCGGRMHLISEI---EKRSAEEFINVSQKYGI 701
Cdd:PLN02574  223 LIAMV---------ELFVRFEASQYEYPgsdnvylaALPMFHIyglsLFVVGLLSLGSTIvvmRRFDASDMVKVIDRFKV 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  702 TNV-VLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTVCATMyEVNGEIQK 780
Cdd:PLN02574  294 THFpVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLP-HVDFIQGYGMTESTAVGTR-GFNTEKLS 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  781 EISNIPIGKPIANSEVFVISPfNTLCPSGVVGELFIGGDGVANGYLNQKEKTegafislDKSYNRDKKMYcTGDLVRLLA 860
Cdd:PLN02574  372 KYSSVGLLAPNMQAKVVDWST-GCLLPPGNCGELWIQGPGVMKGYLNNPKAT-------QSTIDKDGWLR-TGDIAYFDE 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  861 NGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI----VCFYLSKDNTELKQEALKTFLSESLPD 936
Cdd:PLN02574  443 DGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECgeipVAFVVRRQGSTLSQEAVINYVAKQVAP 522

                         490       500
                  ....*....|....*....|....*..
gi 446581728  937 FMMPNYIFHLESFPVSPSGKLDRKKLE 963
Cdd:PLN02574  523 YKKVRKVVFVQSIPKSPAGKILRRELK 549
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 492-943 2.23e-24

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 108.98  E-value: 2.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  492 DQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVyvpidpkfpekrieyilkdseSQMII 571
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV---------------------AALIN 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  572 TKKEYRGLVerfaiHTIyledfhyansieNIAST-HTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKE 650
Cdd:cd05940    60 YNLRGESLA-----HCL------------NVSSAkHLVVDAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  651 DVF-----LQFATiifdASIMEIFPILLCGGRMHLiseIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKL 725
Cdd:cd05940   123 DVLytclpLYHST----ALIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERK 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  726 NSVKRLFvgGETLPAESVRKWQSKLGlkIP-VLNAYGPTETTVCATMYE-------VNGEIQKEISNIPI-------GKP 790
Cdd:cd05940   196 HKVRMIF--GNGLRPDIWEEFKERFG--VPrIAEFYAATEGNSGFINFFgkpgaigRNPSLLRKVAPLALvkydlesGEP 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  791 IANSEVFVISpfntlCPSGVVGELF--IGGDGVANGYLNQKEKTE----GAFISLDKSYNrdkkmycTGDLVRLLANGNL 864
Cdd:cd05940   272 IRDAEGRCIK-----VPRGEPGLLIsrINPLEPFDGYTDPAATEKkilrDVFKKGDAWFN-------TGDLMRLDGEGFW 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  865 EFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQ----NDKIVCFYLS-KDNTELKQEALKTFLSESLPDFMM 939
Cdd:cd05940   340 YFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgtDGRAGMAAIVlQPNEEFDLSALAAHLEKNLPGYAR 419


                  ....
gi 446581728  940 PNYI 943
Cdd:cd05940   420 PLFL 423
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 491-903 3.13e-24

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 110.02  E-value: 3.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  491 GDQSITYYELQQRSNQIVNYLREnDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEK---RIEYILKDSES 567
Cdd:cd05931    21 REETLTYAELDRRARAIAARLQA-VGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRhaeRLAAILADAGP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  568 QMIITKKEYRGLVERFAIHTIYLEDFHYAnSIENIASTH---------TIEDAAYIIYTSGSTGLPKGVVVPHKGVV-NL 637
Cdd:cd05931   100 RVVLTTAAALAAVRAFAASRPAAGTPRLL-VVDLLPDTSaadwpppspDPDDIAYLQYTSGSTGTPKGVVVTHRNLLaNV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  638 SySVINTFHLGKEDVFlqfatiifdAS----------IMEIFPILLCGGRMHLIseiekrSAEEFIN--------VSqKY 699
Cdd:cd05931   179 R-QIRRAYGLDPGDVV---------VSwlplyhdmglIGGLLTPLYSGGPSVLM------SPAAFLRrplrwlrlIS-RY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  700 GITNVVLPTAFFKLIAD--MPKEML-LKLNSVKRLFVGGETLPAESVRKWQ---SKLGLKiP--VLNAYGPTETTVCATM 771
Cdd:cd05931   242 RATISAAPNFAYDLCVRrvRDEDLEgLDLSSWRVALNGAEPVRPATLRRFAeafAPFGFR-PeaFRPSYGLAEATLFVSG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  772 YEVNG-----EIQKEISNIPI----------------GKPIANSEVFVISP-FNTLCPSGVVGELFIGGDGVANGYLNQK 829
Cdd:cd05931   321 GPPGTgpvvlRVDRDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPeTGRELPDGEVGEIWVRGPSVASGYWGRP 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581728  830 EKTEGAFISLDksyNRDKKMYC-TGDLVRlLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFK-HPEVR--DAVVFT 903
Cdd:cd05931   401 EATAETFGALA---ATDEGGWLrTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRpgCVAAFS 474
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 475-962 4.14e-24

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 109.91  E-value: 4.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKS------------PNQIAISMGDQSITYYELQQRSNQIVNYLREN-DLKKGQRVSITMEREIDTIVWILGILK 541
Cdd:PRK12492   18 IDLAAYKSvvevfersckkfADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  542 SGGVYVPIDPKFPEKRIEYILKDSESQMII---------------TKKEYrgLVER-----------FAIHTI------Y 589
Cdd:PRK12492   98 AGLIVVNTNPLYTAREMRHQFKDSGARALVylnmfgklvqevlpdTGIEY--LIEAkmgdllpaakgWLVNTVvdkvkkM 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  590 LEDFHYANSI-------ENIASTH-----TIEDAAYIIYTSGSTGLPKGVVVPHKGVV-NLSYSVINTFHLGKEDvflqf 656
Cdd:PRK12492  176 VPAYHLPQAVpfkqalrQGRGLSLkpvpvGLDDIAVLQYTGGTTGLAKGAMLTHGNLVaNMLQVRACLSQLGPDG----- 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  657 ATIIFDASIMEIFPILL---------CGGRM----HLISEIEKRSAEEFINVSQKYGITNVV-LPTAFFKLIaDMPKEML 722
Cdd:PRK12492  251 QPLMKEGQEVMIAPLPLyhiyaftanCMCMMvsgnHNVLITNPRDIPGFIKELGKWRFSALLgLNTLFVALM-DHPGFKD 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  723 LKLNSVKRLFVGGETLPAESVRKWQSKLGLKIpvLNAYGPTETT--VCATMYevnGEIQKEISnipIGKPIANSEVFVIS 800
Cdd:PRK12492  330 LDFSALKLTNSGGTALVKATAERWEQLTGCTI--VEGYGLTETSpvASTNPY---GELARLGT---VGIPVPGTALKVID 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  801 PFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAfisLDKsynrdKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYR 880
Cdd:PRK12492  402 DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEA---LDA-----EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFN 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  881 IELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTeLKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGK 956
Cdd:PRK12492  474 VYPNEIEDVVMAHPKVANCAAIGVPDERsgeaVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGK 552


                  ....*.
gi 446581728  957 LDRKKL 962
Cdd:PRK12492  553 ILRREL 558
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 464-962 7.93e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 108.68  E-value: 7.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  464 TYPNLKTLDQLIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSG 543
Cdd:PRK06164    5 AAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  544 GVYVPIDPKFPEKRIEYILKDSESQMIITKKEYRGLvERFAI-------------------------------HTIYLED 592
Cdd:PRK06164   85 ATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGI-DFAAIlaavppdalpplraiavvddaadatpapapgARVQLFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  593 FHYANSIENIASTHTIEDAAYIIYT-SGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATI--IFDASIMEIF 669
Cdd:PRK06164  164 LPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFcgVFGFSTLLGA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  670 piLLCGGRMHLISEIEKRSAEEFInvsQKYGITNVVLPTAFFKLIADMPKEMLlKLNSVKRLFVGGETLPAESVRKWQSK 749
Cdd:PRK06164  244 --LAGGAPLVCEPVFDAARTARAL---RRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLFGFASFAPALGELAALARA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  750 LGlkIPVLNAYGPTETTVCATMYEVNGEIQKEIsnIPIGKPI-ANSEVFVISPFN-TLCPSGVVGELFIGGDGVANGYLN 827
Cdd:PRK06164  318 RG--VPLTGLYGSSEVQALVALQPATDPVSVRI--EGGGRPAsPEARVRARDPQDgALLPDGESGEIEIRAPSLMRGYLD 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  828 QKEKTEGAFIslDKSYNRdkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND 907
Cdd:PRK06164  394 NPDATARALT--DDGYFR------TGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD 465

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728  908 ---KIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSG---KLDRKKL 962
Cdd:PRK06164  466 gktVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 1545-1922 8.31e-24

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 108.48  E-value: 8.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIA------TATESLTYRQLNMSSNQVAQHLLEKGiKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVkyP 1618
Cdd:cd05931     5 ARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP--P 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1619 E-----DRINYIVRDSEACRIITSNKFKSHLNVSDYKVS-------IIEDIYRTTINDDV-KILNKPDDLAYVIYTSGST 1685
Cdd:cd05931    82 TpgrhaERLAAILADAGPRVVLTTAAALAAVRAFAASRPaagtprlLVVDLLPDTSAADWpPPSPDPDDIAYLQYTSGST 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1686 GKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQ---FYsHSFdSSVSEIFSTLLNGAELYLLSDE---QRysTVEYAQA 1759
Cdd:cd05931   162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSwlpLY-HDM-GLIGGLLTPLYSGGPSVLMSPAaflRR--PLRWLRL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1760 IQETQATISDLPTvFFNELSTSltKLDSEKIR-----SLRFIIMGGEAASTNAIRSWQNTF-----KNQVqLVNEYGPTE 1829
Cdd:cd05931   238 ISRYRATISAAPN-FAYDLCVR--RVRDEDLEgldlsSWRVALNGAEPVRPATLRRFAEAFapfgfRPEA-FRPSYGLAE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1830 AT----------------VSAMYYFIPVLEGENNLLGSVPI---GIPISNTKVHILNSY-MQYCPVGCMGELYIESLGLA 1889
Cdd:cd05931   314 ATlfvsggppgtgpvvlrVDRDALAGRAVAVAADDPAARELvscGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVA 393

                         410       420       430
                  ....*....|....*....|....*....|...
gi 446581728 1890 QGYWKQKEKTKQAFisNPFSEDNSKRLYRTGDL 1922
Cdd:cd05931   394 SGYWGRPEATAETF--GALAATDEGGWLRTGDL 424
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 613-959 8.93e-24

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 104.79  E-value: 8.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  613 YIIYTSGSTGLPKGVVVPHKGVVNlSYSVINT-FHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISeieKRSAEE 691
Cdd:cd17633     4 YIGFTSGTTGLPKAYYRSERSWIE-SFVCNEDlFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFNPKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  692 FINVSQKYGITNVVL-PTAFFKLIADMPKEmllklNSVKRLFVGGETLPAESVRKWQsKLGLKIPVLNAYGPTETTVCAt 770
Cdd:cd17633    80 WIRKINQYNATVIYLvPTMLQALARTLEPE-----SKIKSIFSSGQKLFESTKKKLK-NIFPKANLIEFYGTSELSFIT- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  771 mYEVNGEIQKEISnipIGKPIANSEVFVISPFNtlcpsGVVGELFIGGDGVANGYLNQKEKTEGAFISldksynrdkkmy 850
Cdd:cd17633   153 -YNFNQESRPPNS---VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGWMS------------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  851 cTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK---IVCFYLSKDNTELKQeaLK 927
Cdd:cd17633   212 -VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARfgeIAVALYSGDKLTYKQ--LK 288

                         330       340       350
                  ....*....|....*....|....*....|..
gi 446581728  928 TFLSESLPDFMMPNYIFHLESFPVSPSGKLDR 959
Cdd:cd17633   289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 1545-2025 1.09e-23

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 107.66  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK06145   14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSNKFKSHLNVSDYKVSIIEdiyrtTINDDVKIL------------NKPDDLAYVIYTSGSTGKPKGTL 1692
Cdd:PRK06145   94 ILGDAGAKLLLVDEEFDAIVALETPKIVIDA-----AAQADSRRLaqggleippqaaVAPTDLVRLMYTSGTTDRPKGVM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1693 LTHKGvlnlVEWRN----EVFQISPNDK---VTQFYsHSFDSSVSEIfSTLLNGAELYLLSDEQRYSTVEyaqAIQETQA 1765
Cdd:PRK06145  169 HSYGN----LHWKSidhvIALGLTASERllvVGPLY-HVGAFDLPGI-AVLWVGGTLRIHREFDPEAVLA---AIERHRL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1766 TISDLPTVFFNELSTSLTKlDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEaTVSAMYYFIPVLEGE 1845
Cdd:PRK06145  240 TCAWMAPVMLSRVLTVPDR-DRFDLDSLAWCIGGGEKTPESRIRDFTRVFTR-ARYIDAYGLTE-TCSGDTLMEAGREIE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1846 NnlLGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlyRTGDLVRW 1925
Cdd:PRK06145  317 K--IGST--GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF---------RSGDVGYL 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1926 LPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVL 2002
Cdd:PRK06145  384 DEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgvhDDRWGERITAVVVLNPGATLTLEALDRHCRQRL 463

                         490       500
                  ....*....|....*....|...
gi 446581728 2003 PEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK06145  464 ASFKVPRQLKVRDELPRNPSGKV 486
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 1545-2026 2.40e-23

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 107.43  E-value: 2.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK06178   45 ERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSNKFK------------SHLNVSDY---------------------KVSIIEDIYRTTINDDVKILNK 1671
Cdd:PRK06178  125 ELNDAGAEVLLALDQLApvveqvraetslRHVIVTSLadvlpaeptlplpdslraprlAAAGAIDLLPALRACTAPVPLP 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 P---DDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVT-----QFYSHSFDSSVseIFStLLNGAELY 1743
Cdd:PRK06178  205 PpalDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFlsflpEFWIAGENFGL--LFP-LFSGATLV 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1744 LLSdeqRYSTVEYAQAIQETQATISDLPTVFFNELsTSLTKLDSEKIRSLRFIimggEAAS-----TNAIRS-WQNtFKN 1817
Cdd:PRK06178  282 LLA---RWDAVAFMAAVERYRVTRTVMLVDNAVEL-MDHPRFAEYDLSSLRQV----RVVSfvkklNPDYRQrWRA-LTG 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1818 QVQLVNEYGPTEATVSAMyyFIPVLEGENNLLGSVPI--GIPISNTKVHILN-SYMQYCPVGCMGELYIESLGLAQGYWK 1894
Cdd:PRK06178  353 SVLAEAAWGMTETHTCDT--FTAGFQDDDFDLLSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWN 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1895 QKEKTKQAFisnpfsEDNskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGI-SQAVVTQT-- 1971
Cdd:PRK06178  431 KPEATAEAL------RDG---WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVlGSAVVGRPdp 501

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1972 EGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYShVLEIPITANGKID 2026
Cdd:PRK06178  502 DKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVR 555
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 1546-2025 3.72e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 106.40  E-value: 3.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1546 QPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYI 1625
Cdd:PRK07786   30 QPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1626 VRDSEACRIIT--------------SNKFKSHLNV---SDYKVSIIEDIYRTTiNDDVKILNKPDDL-AYVIYTSGSTGK 1687
Cdd:PRK07786  110 VSDCGAHVVVTeaalapvatavrdiVPLLSTVVVAggsSDDSVLGYEDLLAEA-GPAHAPVDIPNDSpALIMYTSGTTGR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1688 PKGTLLTHkgvLNLV--------EWRNEVfqispNDKVTQFYSHSFD-SSVSEIFSTLLNGAE--LYLLSdeqRYSTVEY 1756
Cdd:PRK07786  189 PKGAVLTH---ANLTgqamtclrTNGADI-----NSDVGFVGVPLFHiAGIGSMLPGLLLGAPtvIYPLG---AFDPGQL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1757 AQAIQETQATisdlpTVFFNELSTSLTkLDSEKIR----SLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEatv 1832
Cdd:PRK07786  258 LDVLEAEKVT-----GIFLVPAQWQAV-CAEQQARprdlALRVLSWGAAPASDTLLRQMAATFPE-AQILAAFGQTE--- 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1833 saMYYFIPVLEGENNL--LGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFse 1910
Cdd:PRK07786  328 --MSPVTCMLLGEDAIrkLGSV--GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-- 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1911 dnskrlyRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQ------TEGGMLLQAYYKTV 1984
Cdd:PRK07786  402 -------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGradekwGEVPVAVAAVRNDD 474

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 446581728 1985 DGIGIEknKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK07786  475 AALTLE--DLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 1543-2025 1.27e-22

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 105.35  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQ----PERIAI------ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIP 1612
Cdd:cd17634    59 LDRHlrenGDRTAIiyegddTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1613 IDVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIY-RTTINDDVKILNK-------------------- 1671
Cdd:cd17634   139 IFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRtgsdidwqegrdlwwrdlia 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 ------------PDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWR-NEVFQISPNDKVTQF------YSHSFdssvsEI 1732
Cdd:cd17634   219 kaspehqpeamnAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDYGPGDIYWCTadvgwvTGHSY-----LL 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1733 FSTLLNGAELYLLSDEQRYSTVE-YAQAIQETQATISDL-PTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIR- 1809
Cdd:cd17634   294 YGPLACGATTLLYEGVPNWPTPArMWQVVDKHGVNILYTaPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEw 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1810 SWQNTFKNQVQLVNEYGPTEaTVSAMyyfIPVLEGENNLLGSVPIgIPISNTKVHILNSYMQYCPVGCMGELYIESL--G 1887
Cdd:cd17634   374 YWKKIGKEKCPVVDTWWQTE-TGGFM---ITPLPGAIELKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpG 448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1888 LAQGYWKQKEKTKQAFISnpfsedNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAV 1967
Cdd:cd17634   449 QTRTLFGDHERFEQTYFS------TFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAA 522

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1968 VTQTEGGMLLQAYYKTV---DGIgIEKNKLAIHLSNVLPEYM----VPKYYSHVLEIPITANGKI 2025
Cdd:cd17634   523 VVGIPHAIKGQAPYAYVvlnHGV-EPSPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGKI 586
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 1545-1924 1.31e-22

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 105.04  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEK-GIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRIN 1623
Cdd:PRK08314   22 RYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1624 YIVRDSEACRIITS----NKFK--------SHLNVSDYK--------------------VSIIEDIYRTTINDDVKILNK 1671
Cdd:PRK08314  102 HYVTDSGARVAIVGselaPKVApavgnlrlRHVIVAQYSdylpaepeiavpawlraeppLQALAPGGVVAWKEALAAGLA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 P-------DDLAYVIYTSGSTGKPKGTLLTHKGVL-NLV---EWRNE-----VFQISPNDKVTQFyshsfdssVSEIFST 1735
Cdd:PRK08314  182 PpphtagpDDLAVLPYTSGTTGVPKGCMHTHRTVMaNAVgsvLWSNStpesvVLAVLPLFHVTGM--------VHSMNAP 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1736 LLNGAELYLLSdeqRYSTVEYAQAIQETQATI-SDLPTVFFNELSTSltKLDSEKIRSLRFiIMGGEAASTNAI--RSWQ 1812
Cdd:PRK08314  254 IYAGATVVLMP---RWDREAAARLIERYRVTHwTNIPTMVVDFLASP--GLAERDLSSLRY-IGGGGAAMPEAVaeRLKE 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1813 NTfknQVQLVNEYGPTEaTVSAMyYFIPVLEGENNLLgsvpiGIPISNTKVHILN-SYMQYCPVGCMGELYIESLGLAQG 1891
Cdd:PRK08314  328 LT---GLDYVEGYGLTE-TMAQT-HSNPPDRPKLQCL-----GIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKG 397

                         410       420       430
                  ....*....|....*....|....*....|...
gi 446581728 1892 YWKQKEKTKQAFIsnpfsEDNSKRLYRTGDLVR 1924
Cdd:PRK08314  398 YWNRPEATAEAFI-----EIDGKRFFRTGDLGR 425
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 493-962 1.44e-22

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 104.85  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLR-ENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII 571
Cdd:PRK05677   48 KTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  572 TKKEYRGLVERFAIHT-----IYLE--DFH--YANSIENIASTHT---------------------------------IE 609
Cdd:PRK05677  128 CLANMAHLAEKVLPKTgvkhvIVTEvaDMLppLKRLLINAVVKHVkkmvpayhlpqavkfndalakgagqpvteanpqAD 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVVN-------LSYSVINTfhlGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLIS 682
Cdd:PRK05677  208 DVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqcraLMGSNLNE---GCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILIS 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  683 EieKRSAEEFINVSQKYGITNVV-LPTAFFKLIADmpkEMLLKLN--SVKRLFVGGETLPAESVRKWQSKLGlkIPVLNA 759
Cdd:PRK05677  285 N--PRDLPAMVKELGKWKFSGFVgLNTLFVALCNN---EAFRKLDfsALKLTLSGGMALQLATAERWKEVTG--CAICEG 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  760 YGPTETTVCATmyeVNgeiqkEISNI---PIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTegaf 836
Cdd:PRK05677  358 YGMTETSPVVS---VN-----PSQAIqvgTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEAT---- 425

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  837 islDKSYNRDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCF 912
Cdd:PRK05677  426 ---DEILDSDGWLK-TGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKsgeaIKVF 501

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 446581728  913 YLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK05677  502 VVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
 2162-2402 1.68e-22

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 100.84  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLL-QLPST-TIYCLVRENEDQVIGAKLKE---RMEFYFGKEILQKLKERVELIEGDLSLMN 2236
Cdd:cd05236     1 KSVLITGATGFLGKVLLEKLLrSCPDIgKIYLLIRGKSGQSAEERLREllkDKLFDRGRNLNPLFESKIVPIEGDLSEPN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2237 LGLDSKQLDHLKKNVESIIHCGGEVRhYGER-EHFQKVNVQSTKYLLELAKN-TNV-RFHYISTLSVVGQaeRDPKEFEF 2313
Cdd:cd05236    81 LGLSDEDLQTLIEEVNIIIHCAATVT-FDERlDEALSINVLGTLRLLELAKRcKKLkAFVHVSTAYVNGD--RQLIEEKV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2314 FESDFDRGQNLD----------------------NLYLESKFQGEKMVREamEKG------VRATIyrvgnlVGNSKTGK 2365
Cdd:cd05236   158 YPPPADPEKLIDilelmddleleratpkllgghpNTYTFTKALAERLVLK--ERGnlplviVRPSI------VGATLKEP 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 446581728 2366 FQ-YNINENAFYRLL----KGIcLSSIAPDVNTYVDLTPVDY 2402
Cdd:cd05236   230 FPgWIDNFNGPDGLFlaygKGI-LRTMNADPNAVADIIPVDV 270
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 1540-2033 2.84e-22

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 103.90  E-value: 2.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1540 YMQVDRQPERiaiatatesLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDV---- 1615
Cdd:cd05906    30 YIDADGSEEF---------QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVppty 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1616 KYPEDRINYIVRDS---EACRIITSNKFKSHL-------NVSDYKVSIIEDIYRTTINDDVKILnKPDDLAYVIYTSGST 1685
Cdd:cd05906   101 DEPNARLRKLRHIWqllGSPVVLTDAELVAEFagletlsGLPGIRVLSIEELLDTAADHDLPQS-RPDDLALLMLTSGST 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1686 GKPKGTLLTHKGVLNLVEWRNEVFQISPNDkVTQFYSHsFDSSVSEIFSTLlngAELYLLSDEQRYSTVEYAQA------ 1759
Cdd:cd05906   180 GFPKAVPLTHRNILARSAGKIQHNGLTPQD-VFLNWVP-LDHVGGLVELHL---RAVYLGCQQVHVPTEEILADplrwld 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1760 -IQETQATISDLPTVFFNELSTSLTKLDSEK--IRSLRFIIMGGEAASTNAIRSWQNTFK----NQVQLVNEYGPTEaTV 1832
Cdd:cd05906   255 lIDRYRVTITWAPNFAFALLNDLLEEIEDGTwdLSSLRYLVNAGEAVVAKTIRRLLRLLEpyglPPDAIRPAFGMTE-TC 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1833 SAM-YYFIPVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAfisnpFSED 1911
Cdd:cd05906   334 SGViYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEA-----FTED 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1912 NskrLYRTGDLVrWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGI---SQAVVTQTEGGM------------- 1975
Cdd:cd05906   409 G---WFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAeteelaiffvpey 484

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728 1976 -LLQAYYKTVDGIgiekNKLAIHLSNVLPEYMVPkyyshvL---EIPITANGKIDFEKLPKI 2033
Cdd:cd05906   485 dLQDALSETLRAI----RSVVSREVGVSPAYLIP------LpkeEIPKTSLGKIQRSKLKAA 536
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 1549-2030 4.32e-22

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 102.17  E-value: 4.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1549 RIAIATATESLTYRQLNMSSNQVAQHLLEKGIKR-GDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVR 1627
Cdd:cd05958     1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1628 DseaCRIitsnkfkshlnvsdyKVSIIEDiyRTTINDDVKILNkpddlayviYTSGSTGKPKGTLLTHKGVLNLVE-WRN 1706
Cdd:cd05958    81 K---ARI---------------TVALCAH--ALTASDDICILA---------FTSGTTGAPKATMHFHRDPLASADrYAV 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1707 EVFQISPNDKvtqfyshsFDSSVSEIFSTLLNGAELYLLSDEQrySTVEYAQAI-QETQATISDL-PTVFFN---ELSTS 1781
Cdd:cd05958   132 NVLRLREDDR--------FVGSPPLAFTFGLGGVLLFPFGVGA--SGVLLEEATpDLLLSAIARYkPTVLFTaptAYRAM 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1782 LTKLDSEK--IRSLRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTEatvsAMYYFIPVLEGENNlLGSVpiGIPIS 1859
Cdd:cd05958   202 LAHPDAAGpdLSSLRKCVSAGEALPAALHRAWKEATG--IPIIDGIGSTE----MFHIFISARPGDAR-PGAT--GKPVP 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1860 NTKVHILNSYMQYCPVGCMGELYIESlglAQGYWKQKEKTKQAFISNPFSEdnskrlyrTGDLVRWLPNGNIEFMGRKDK 1939
Cdd:cd05958   273 GYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQGGWNI--------TGDTYSRDPDGYFRHQGRSDD 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1940 QVKIRGHRIELGEIEDAMLQLEGISQAVVTQTE---GGMLLQAYYKTVDGIGIEK---NKLAIHLSNVLPEYMVPKYYSH 2013
Cdd:cd05958   342 MIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPdesRGVVVKAFVVLRPGVIPGPvlaRELQDHAKAHIAPYKYPRAIEF 421

                         490
                  ....*....|....*..
gi 446581728 2014 VLEIPITANGKIDFEKL 2030
Cdd:cd05958   422 VTELPRTATGKLQRFAL 438
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 1542-2008 6.46e-22

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 103.03  E-value: 6.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1542 QVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGA--AYipidvkype 1619
Cdd:PRK08279   46 AAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvAL--------- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1620 drINYIVRD---------SEACRIITSNKF-------KSHLNVSdyKVSIIEDIYRTTINDDVKILNK------------ 1671
Cdd:PRK08279  117 --LNTQQRGavlahslnlVDAKHLIVGEELveafeeaRADLARP--PRLWVAGGDTLDDPEGYEDLAAaaagapttnpas 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 -----PDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKvtqFYS-----HS--FDSSVSeifSTLLNG 1739
Cdd:PRK08279  193 rsgvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDV---LYCclplyHNtgGTVAWS---SVLAAG 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1740 AELYLlsdEQRYSTVEYAQAIQETQATIsdlpTVFFNELSTSLTKL---DSEKIRSLRFIImGgeaastNAIR-----SW 1811
Cdd:PRK08279  267 ATLAL---RRKFSASRFWDDVRRYRATA----FQYIGELCRYLLNQppkPTDRDHRLRLMI-G------NGLRpdiwdEF 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1812 QNTFKnqVQLVNE-YGPTEATVSamyyFIPVlEGENNLLGSVPI---------------GIPISNTkvhilNSYMQYCPV 1875
Cdd:PRK08279  333 QQRFG--IPRILEfYAASEGNVG----FINV-FNFDGTVGRVPLwlahpyaivkydvdtGEPVRDA-----DGRCIKVKP 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1876 GCMGELY--IESLGLAQGYwKQKEKTKQAFISNPFSEDNskRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEI 1953
Cdd:PRK08279  401 GEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFKKGD--AWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEV 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728 1954 EDAMLQLEGISQAVV-----TQTEG--GMllqAYYKTVDGIGIEKNKLAIHLSNVLPEYMVP 2008
Cdd:PRK08279  478 ENALSGFPGVEEAVVygvevPGTDGraGM---AAIVLADGAEFDLAALAAHLYERLPAYAVP 536
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 1545-2025 7.38e-22

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 102.80  E-value: 7.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK06710   36 RYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEY 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRI---------ITSNKFKSHLN------VSDY---------------------KVSIIEDIY-----RTTIN 1663
Cdd:PRK06710  116 QLHDSGAKVIlcldlvfprVTNVQSATKIEhvivtrIADFlpfpknllypfvqkkqsnlvvKVSESETIHlwnsvEKEVN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1664 DDVKILNKPD-DLAYVIYTSGSTGKPKGTLLTHKGVL-----------NLVEWRNEVFQISPndkvtqfYSHSFDSSVSE 1731
Cdd:PRK06710  196 TGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVsntlmgvqwlyNCKEGEEVVLGVLP-------FFHVYGMTAVM 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1732 IFStLLNGAELYLLSdeqRYSTVEYAQAIQETQATI-SDLPTVFFNELSTSLTKldSEKIRSLRFIIMGGEAASTNAirs 1810
Cdd:PRK06710  269 NLS-IMQGYKMVLIP---KFDMKMVFEAIKKHKVTLfPGAPTIYIALLNSPLLK--EYDISSIRACISGSAPLPVEV--- 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1811 wQNTFKNQV--QLVNEYGPTEATVSAMYYFIpvleGENNLLGSvpIGIPISNTKVHILN-SYMQYCPVGCMGELYIESLG 1887
Cdd:PRK06710  340 -QEKFETVTggKLVEGYGLTESSPVTHSNFL----WEKRVPGS--IGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQ 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1888 LAQGYWKQKEKTKQAFisnpfsEDNskrlyrtgdlvrWLPNGNIEFM---------GRKDKQVKIRGHRIELGEIEDAML 1958
Cdd:PRK06710  413 IMKGYWNKPEETAAVL------QDG------------WLHTGDVGYMdedgffyvkDRKKDMIVASGFNVYPREVEEVLY 474

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1959 QLEGISQAVVTQTEG---GMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK06710  475 EHEKVQEVVTIGVPDpyrGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKI 544
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 1674-2025 1.03e-21

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 99.26  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1674 DLAYVIYTSGSTGKPKGTLLTHKG-VLNLVEWRNEVFQISpNDKVTQFYSH-SFDSSVSEIFSTLLNGAELYLLSDEQRY 1751
Cdd:cd17635     2 DPLAVIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWV-VGDVTYLPLPaTHIGGLWWILTCLIHGGLCVTGGENTTY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1752 STVeyAQAIQETQATISDLPTVFFNELsTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQnTFKNqVQLVNEYGPTEAT 1831
Cdd:cd17635    81 KSL--FKILTTNAVTTTCLVPTLLSKL-VSELKSANATVPSLRLIGYGGSRAIAADVRFIE-ATGL-TNTAQVYGLSETG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1832 VSAmyyFIPVLEGENNlLGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsed 1911
Cdd:cd17635   156 TAL---CLPTDDDSIE-INAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1912 nskrlyRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKT---VD 1985
Cdd:cd17635   227 ------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACyeiSDEEFGELVGLAVVAsaeLD 300

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 446581728 1986 GIGIEKNKLAIHLSnvLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd17635   301 ENAIRALKHTIRRE--LEPYARPSTIVIVTDIPRTQSGKV 338
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 1543-1969 1.24e-21

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 101.54  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIATAT--ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPED 1620
Cdd:cd05904    15 ASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1621 RINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIED-------IYRTTINDD------VKIlnKPDDLAYVIYTSGSTGK 1687
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSaefdslsFSDLLFEADeaeppvVVI--KQDDVAALLYSSGTTGR 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1688 PKGTLLTHKGVLNLVEWRNEVF-QISPNDKVTQF---YSHSFdsSVSEIFSTLL-NGAELYLLSdeqRYSTVEYAQAIQE 1762
Cdd:cd05904   173 SKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCvlpMFHIY--GLSSFALGLLrLGATVVVMP---RFDLEELLAAIER 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1763 TQATIsdLPTVffNELSTSLTK---LDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEAT-VSAMyyf 1838
Cdd:cd05904   248 YKVTH--LPVV--PPIVLALVKspiVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN-VDLGQGYGMTESTgVVAM--- 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1839 IPVLEGENNLLGSVpiGIPISNTKVHILN-SYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpfsedNSKRLY 1917
Cdd:cd05904   320 CFAPEKDRAKYGSV--GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI--------DKEGWL 389

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446581728 1918 RTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT 1969
Cdd:cd05904   390 HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 474-973 1.28e-21

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 101.80  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  474 LIDLQALKSPNQIAISmGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKF 553
Cdd:PLN02860   13 LTRLATLRGNAVVTIS-GNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRW 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  554 PEKRIEYILKDSESQMIITKKEYRGLVERFAIHTIY-------LED-----FHYANSIENIAS--THTI----------- 608
Cdd:PLN02860   92 SFEEAKSAMLLVRPVMLVTDETCSSWYEELQNDRLPslmwqvfLESpsssvFIFLNSFLTTEMlkQRALgtteldyawap 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRS 688
Cdd:PLN02860  172 DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKA 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  689 AEEFInvsQKYGITN-VVLPTAFFKLIADMPKEMLLKLN-SVKRLFVGGETLPAESVrKWQSKLGLKIPVLNAYGPTETt 766
Cdd:PLN02860  252 ALQAI---KQHNVTSmITVPAMMADLISLTRKSMTWKVFpSVRKILNGGGSLSSRLL-PDAKKLFPNAKLFSAYGMTEA- 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  767 vCATM------------YEVNGEIQKEISNIP--------IGKPIANSEVFVISPfntlcPSGVVGELFIGGDGVANGYL 826
Cdd:PLN02860  327 -CSSLtfmtlhdptlesPKQTLQTVNQTKSSSvhqpqgvcVGKPAPHVELKIGLD-----ESSRVGRILTRGPHVMLGYW 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  827 NQKEKTEGAFIS---LDksynrdkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFT 903
Cdd:PLN02860  401 GQNSETASVLSNdgwLD-----------TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVG 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  904 YQNDK-----IVCFYL-------------SKDNTELKQEALKTFLSE-SLPDFMMPN-YIFHLESFPVSPSGKLDRKKLE 963
Cdd:PLN02860  470 VPDSRltemvVACVRLrdgwiwsdnekenAKKNLTLSSETLRHHCREkNLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVR 549

                         570
                  ....*....|
gi 446581728  964 LQIPSLLENM 973
Cdd:PLN02860  550 REVLSHLQSL 559
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1559-2025 1.56e-21

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 100.29  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSN 1638
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1639 KFKSHLNvsdykvsiiediyrttinddvkilnkpDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK-- 1716
Cdd:cd05973    81 ANRHKLD---------------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSfw 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1717 -------VTQFYSHSFDSSVSEIFSTLLNGAelylLSDEQRYSTVEyaqaiqetQATISDL---PTVFFNELSTSLTKLD 1786
Cdd:cd05973   134 naadpgwAYGLYYAITGPLALGHPTILLEGG----FSVESTWRVIE--------RLGVTNLagsPTAYRLLMAAGAEVPA 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1787 SEKIRsLRFIIMGGEAASTNAIRSWQNTFKNQVQlvNEYGPTE-ATVSAMYYFI--PVLEGEnnllgsvpIGIPISNTKV 1863
Cdd:cd05973   202 RPKGR-LRRVSSAGEPLTPEVIRWFDAALGVPIH--DHYGQTElGMVLANHHALehPVHAGS--------AGRAMPGWRV 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1864 HILNSYMQYCPVGCMGELYIES----LGLAQGYWKQKEKTKqafisnpfsednSKRLYRTGDLVRWLPNGNIEFMGRKDK 1939
Cdd:cd05973   271 AVLDDDGDELGPGEPGRLAIDIanspLMWFRGYQLPDTPAI------------DGGYYLTGDTVEFDPDGSFSFIGRADD 338

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1940 QVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYY---KTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSH 2013
Cdd:cd05973   339 VITMSGYRIGPFDVESALIEHPAVAEAAVIgvpDPERTEVVKAFVvlrGGHEGTPALADELQLHVKKRLSAHAYPRTIHF 418

                         490
                  ....*....|..
gi 446581728 2014 VLEIPITANGKI 2025
Cdd:cd05973   419 VDELPKTPSGKI 430
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 605-962 1.95e-21

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 102.69  E-value: 1.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  605 THTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLqfatiifdaSIMEIFPIL---------LCG 675
Cdd:PRK08633  778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVIL---------SSLPFFHSFgltvtlwlpLLE 848

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  676 GrMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKIp 755
Cdd:PRK08633  849 G-IKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRI- 926

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  756 vLNAYGPTETTVCATmyeVN------GEIQKEISNIP--IGKPIANSEVFVISPfNTL--CPSGVVGELFIGGDGVANGY 825
Cdd:PRK08633  927 -LEGYGATETSPVAS---VNlpdvlaADFKRQTGSKEgsVGMPLPGVAVRIVDP-ETFeeLPPGEDGLILIGGPQVMKGY 1001

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  826 LNQKEKTEGAFISLDksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIEL----DEIEGTLFKhpevrDAVV 901
Cdd:PRK08633 1002 LGDPEKTAEVIKDID-----GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLgaveEELAKALGG-----EEVV 1071

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  902 FTYQN-------DKIVCFYlskDNTELKQEALKTFLSES-LPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK08633 1072 FAVTAvpdekkgEKLVVLH---TCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK09274 PRK09274
peptide synthase; Provisional
 479-962 2.39e-21

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 101.13  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGD----------QSITYYELQQRSNQIVNYLRENDLKKGQRVsITMER-EIDTIVWILGILKSGGVYV 547
Cdd:PRK09274   16 AQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRA-VLMVTpSLEFFALTFALFKAGAVPV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  548 PIDPKFPEKRIEYILKDSESQMIIT--------------KKEYRGLV---ERFAIHTIYLEDF--HYANSIENIASTHTI 608
Cdd:PRK09274   95 LVDPGMGIKNLKQCLAEAQPDAFIGipkahlarrlfgwgKPSVRRLVtvgGRLLWGGTTLATLlrDGAAAPFPMADLAPD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAyIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLqfATiifdasimeiFPI-----LLCGGRMhLISE 683
Cdd:PRK09274  175 DMAA-ILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL--PT----------FPLfalfgPALGMTS-VIPD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  684 IE-KRSA----EEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKIPVLN 758
Cdd:PRK09274  241 MDpTRPAtvdpAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDAEILT 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  759 AYGPTE----TTVcaTMYEVNGEIQKEISN---IPIGKPIANSEVFVIS----PFNTL-----CPSGVVGELFIGGDGVA 822
Cdd:PRK09274  321 PYGATEalpiSSI--ESREILFATRAATDNgagICVGRPVDGVEVRIIAisdaPIPEWddalrLATGEIGEIVVAGPMVT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  823 NGYLNQKEKTEGAFISLDKSYNRdkkmYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEV-RDAVV 901
Cdd:PRK09274  399 RSYYNRPEATRLAKIPDGQGDVW----HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkRSALV 474

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581728  902 FTYQNDKIV---CFYLSKD--------NTELKQEALKTFLSESLPDFMmpnyiFHlESFPVSP--SGKLDRKKL 962
Cdd:PRK09274  475 GVGVPGAQRpvlCVELEPGvacsksalYQELRALAAAHPHTAGIERFL-----IH-PSFPVDIrhNAKIFREKL 542
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 488-962 2.49e-21

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 100.87  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  488 ISMGdQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSES 567
Cdd:PRK07059   43 ICMG-KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  568 QMIItkkeyrgLVERFAiHTIyledfhyANSIENIASTHTI--------------------------------------- 608
Cdd:PRK07059  122 EAIV-------VLENFA-TTV-------QQVLAKTAVKHVVvasmgdllgfkghivnfvvrrvkkmvpawslpghvrfnd 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 -----------------EDAAYIIYTSGSTGLPKGVVVPHKGVVNlsysviNTFHLgkeDVFLQFA----------TIIF 661
Cdd:PRK07059  187 alaegarqtfkpvklgpDDVAFLQYTGGTTGVSKGATLLHRNIVA------NVLQM---EAWLQPAfekkprpdqlNFVC 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  662 DASIMEIFPILLC-------GGRMHLISEieKRSAEEFINVSQKYGITNV-VLPTAFFKLI--ADMPKemlLKLNSVKRL 731
Cdd:PRK07059  258 ALPLYHIFALTVCgllgmrtGGRNILIPN--PRDIPGFIKELKKYQVHIFpAVNTLYNALLnnPDFDK---LDFSKLIVA 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  732 FVGGETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCATmyeVNGEIQKEISNIpIGKPIANSEVFVISPFNTLCPSGVV 811
Cdd:PRK07059  333 NGGGMAVQRPVAERWLEMTG--CPITEGYGLSETSPVAT---CNPVDATEFSGT-IGLPLPSTEVSIRDDDGNDLPLGEP 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  812 GELFIGGDGVANGYLNQKEKTEGAfISLDkSYNRdkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLF 891
Cdd:PRK07059  407 GEICIRGPQVMAGYWNRPDETAKV-MTAD-GFFR------TGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581728  892 KHPEVRDAVVFTYQNDK---IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK07059  479 SHPGVLEVAAVGVPDEHsgeAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 1533-2025 2.82e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 100.62  E-value: 2.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1533 QNIQEQFYMQVDRQPERIAIATATESL--TYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAY 1610
Cdd:PRK12583   18 QTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1611 IPIDVKYPEDRINYIVRDSEACRIITSNKFKShlnvSDYkVSIIEDIYRTTINDDVKILN-------------------- 1670
Cdd:PRK12583   98 VNINPAYRASELEYALGQSGVRWVICADAFKT----SDY-HAMLQELLPGLAEGQPGALAcerlpelrgvvslapapppg 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1671 --------------------------KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKV---TQFY 1721
Cdd:PRK12583  173 flawhelqargetvsrealaerqaslDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLcvpVPLY 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1722 sHSFdSSVSEIFSTLLNGAELYLLSDEqrYSTVEYAQAIQETQAT-ISDLPTVFFNELSTSltKLDSEKIRSLRFIIMGG 1800
Cdd:PRK12583  253 -HCF-GMVLANLGCMTVGACLVYPNEA--FDPLATLQAVEEERCTaLYGVPTMFIAELDHP--QRGNFDLSSLRTGIMAG 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1801 EAASTNAIRSWQNTFkNQVQLVNEYGPTEAT-VSAMYYFIPVLEGENNLLGSVpigIPISNTKVhiLNSYMQYCPVGCMG 1879
Cdd:PRK12583  327 APCPIEVMRRVMDEM-HMAEVQIAYGMTETSpVSLQTTAADDLERRVETVGRT---QPHLEVKV--VDPDGATVPRGEIG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1880 ELYIESLGLAQGYWKQKEKTKQAFisnpfseDNSKRLYrTGDLVRWLPNGNIEFMGRKdKQVKIR-GHRIELGEIEDAML 1958
Cdd:PRK12583  401 ELCTRGYSVMKGYWNNPEATAESI-------DEDGWMH-TGDLATMDEQGYVRIVGRS-KDMIIRgGENIYPREIEEFLF 471

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1959 QLEGISQ-AV--VTQTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK12583  472 THPAVADvQVfgVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 493-962 3.68e-21

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 99.46  E-value: 3.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIIT 572
Cdd:cd05910     1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  573 kkeyrglverfaihtIYLEDfhyansieniasthtiEDAAyIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDV 652
Cdd:cd05910    81 ---------------IPKAD----------------EPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  653 ----FLQFAtiIFDASImeifpillcgGRMHLISEIEKR-----SAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLL 723
Cdd:cd05910   129 dlatFPLFA--LFGPAL----------GLTSVIPDMDPTrparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGI 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  724 KLNSVKRLFVGGETLPAESVRKWQSKLGLKIPVLNAYGPTETTVCATM--YEVNGEIQKEISN---IPIGKPIANSEVFV 798
Cdd:cd05910   197 TLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEALPVSSIgsRELLATTTAATSGgagTCVGRPIPGVRVRI 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  799 I--------SPFNTLC-PSGVVGELFIGGDGVANGYLNQKEKTegafiSLDKSYNRDKKM-YCTGDLVRLLANGNLEFIG 868
Cdd:cd05910   277 IeiddepiaEWDDTLElPRGEIGEITVTGPTVTPTYVNRPVAT-----ALAKIDDNSEGFwHRMGDLGYLDDEGRLWFCG 351

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  869 RKDNQVKIRGYRIELDEIEGTLFKHPEVRDAV------------VFTYQNDKIVCFYLSKDNTELKQEALKTFLSESLPD 936
Cdd:cd05910   352 RKAHRVITTGGTLYTEPVERVFNTHPGVRRSAlvgvgkpgcqlpVLCVEPLPGTITPRARLEQELRALAKDYPHTQRIGR 431

                         490       500
                  ....*....|....*....|....*...
gi 446581728  937 FMmpnyiFHlESFPVSP--SGKLDRKKL 962
Cdd:cd05910   432 FL-----IH-PSFPVDIrhNAKIFREKL 453
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 1559-1954 4.44e-21

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 99.60  E-value: 4.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGaayIPIDVKYP---EDRINYIVRDSEACRII 1635
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1636 TSnkfkshlnvsdykvsiiediyrttinddvkilNKPDDLAYVIYTSGSTGKPKGTLLTHK----GVLNLVEWRNEVfqI 1711
Cdd:cd17639    83 TD--------------------------------GKPDDLACIMYTSGSTGNPKGVMLTHGnlvaGIAGLGDRVPEL--L 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1712 SPNDKVTQFY--SHSFDSSVSEIFstLLNGAEL-Y-----LLSDEQRYS---TVEY-------AQAIQET--QATISDLP 1771
Cdd:cd17639   129 GPDDRYLAYLplAHIFELAAENVC--LYRGGTIgYgsprtLTDKSKRGCkgdLTEFkptlmvgVPAIWDTirKGVLAKLN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1772 -------TVFFNELSTSLTKLDS------------EKIRS-----LRFIIMGGEAASTNAIRsWQNTFKNQVqlVNEYGP 1827
Cdd:cd17639   207 pmgglkrTLFWTAYQSKLKALKEgpgtplldelvfKKVRAalggrLRYMLSGGAPLSADTQE-FLNIVLCPV--IQGYGL 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1828 TEaTVSAMyyfiPVLEGENNLLGSVpiGIPISNTKVHILN------SYMQYCPvgcMGELYIESLGLAQGYWKQKEKTKQ 1901
Cdd:cd17639   284 TE-TCAGG----TVQDPGDLETGRV--GPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKTKE 353

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446581728 1902 AFisnpfsedNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIR-GHRIELGEIE 1954
Cdd:cd17639   354 AF--------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLE 399
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 1532-2025 4.74e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 100.22  E-value: 4.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1532 FQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLL-EKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAY 1610
Cdd:PRK05677   23 YPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1611 IPIDVKYPEDRINYIVRDSEACRIIT-------SNKFKSHLNVSDYKVSIIEDIY----RTTINDDVKILNK-------- 1671
Cdd:PRK05677  103 VNTNPLYTAREMEHQFNDSGAKALVClanmahlAEKVLPKTGVKHVIVTEVADMLpplkRLLINAVVKHVKKmvpayhlp 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 -----------------------PDDLAYVIYTSGSTGKPKGTLLTHKG-VLNLVEWR-------NEVFQ--ISPNdKVT 1718
Cdd:PRK05677  183 qavkfndalakgagqpvteanpqADDVAVLQYTGGTTGVAKGAMLTHRNlVANMLQCRalmgsnlNEGCEilIAPL-PLY 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1719 QFYSHSFDSSVseifsTLLNGAELYLLSDEQrystveyaqaiqETQATISDLPTVFFNE---LSTSLTKL-DSEKIRSLR 1794
Cdd:PRK05677  262 HIYAFTFHCMA-----MMLIGNHNILISNPR------------DLPAMVKELGKWKFSGfvgLNTLFVALcNNEAFRKLD 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1795 F-----IIMGGEAASTNAIRSWQNTfkNQVQLVNEYGPTEATvsamyyfiPVLEG---ENNLLGSvpIGIPISNTKVHIL 1866
Cdd:PRK05677  325 FsalklTLSGGMALQLATAERWKEV--TGCAICEGYGMTETS--------PVVSVnpsQAIQVGT--IGIPVPSTLCKVI 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1867 NSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKDKQVKIRGH 1946
Cdd:PRK05677  393 DDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW--------LKTGDIALIQEDGYMRIVDRKKDMILVSGF 464

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1947 RIELGEIEDAMLQLEGISQAV---VTQTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANG 2023
Cdd:PRK05677  465 NVYPNELEDVLAALPGVLQCAaigVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVG 544


                  ..
gi 446581728 2024 KI 2025
Cdd:PRK05677  545 KI 546
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 1557-2025 5.39e-21

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 99.04  E-value: 5.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1557 ESLTYRQLNMSSNQVAQHLL-EKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAyipidvkypEDRINYIVRDseacrii 1635
Cdd:cd05937     4 KTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLSG------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1636 tsNKFKSHLNVSDYKVSIIEdiyrttinddvkilnkPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPND 1715
Cdd:cd05937    68 --DPLIHCLKLSGSRFVIVD----------------PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGD 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1716 KvtqFYS-----HSFDSSVSEIfSTLLNGAELYLlsdEQRYSTVEYAQAIQETQATIsdlpTVFFNE-----LSTSLTKL 1785
Cdd:cd05937   130 R---TYTcmplyHGTAAFLGAC-NCLMSGGTLAL---SRKFSASQFWKDVRDSGATI----IQYVGElcrylLSTPPSPY 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1786 DsekiRSLRFIIMGGeaastNAIRS--WQNtFKNQ--VQLVNE-YGPTEATVSAMYY----FIPVLEGENNLL------- 1849
Cdd:cd05937   199 D----RDHKVRVAWG-----NGLRPdiWER-FRERfnVPEIGEfYAATEGVFALTNHnvgdFGAGAIGHHGLIrrwkfen 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1850 GSVPIGI------PISNTKvhilNSYMQYCPVGCMGE----LYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSkrLYRT 1919
Cdd:cd05937   269 QVVLVKMdpetddPIRDPK----TGFCVRAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFRKGDI--YFRT 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1920 GDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTqtegGMLLQAYYKTVDGIGIE--------- 1990
Cdd:cd05937   343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVY----GVKVPGHDGRAGCAAITleessavpt 418

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 446581728 1991 ---KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05937   419 eftKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQ 456
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1113-1486 5.77e-21

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 98.54  E-value: 5.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1113 NKDILQDTIRFLVERHEMLRTVFIERN-GEPRQVILNSIAIDLIHDEIEHMSKKEQQEYIRTTINQTDHTPFDLEKGPLF 1191
Cdd:cd19547    37 DEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1192 RIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNPELPTIsNRYVDYAEWeqVQLNLGRWDTEKSYW 1271
Cdd:cd19547   117 RLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQLSPC-RPYRDYVRW--IRARTAQSEESERFW 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1272 MAELA--APLPILNLPLDfsrnRQSTNKGTVFEMKldNEMKESLKQVCEQENISMYMLFLAAYIQLLHYLTDQKDIIVGT 1349
Cdd:cd19547   194 REYLRdlTPSPFSTAPAD----REGEFDTVVHEFP--EQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGL 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1350 PVVGR--NHQEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKVI-----EQINPDRSFGNNPI 1422
Cdd:cd19547   268 TIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLAQIKswasgERLSGGRVFDNLVA 347

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1423 FStmfSYQKDILQQhDAYKLQLLP-NKQDISKFDISLAVEEgLDYVGISFEYDINLFKEESINRF 1486
Cdd:cd19547   348 FE---NYPEDNLPG-DDLSIQIIDlHAQEKTEYPIGLIVLP-LQKLAFHFNYDTTHFTRAQVDRF 407
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 479-901 5.80e-21

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 98.79  E-value: 5.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRI 558
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  559 EYILKDSESQMIITKKEYRglverfaiHTIYLEDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVvpH------- 631
Cdd:PRK09029   93 EELLPSLTLDFALVLEGEN--------TFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAV--Htaqahla 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  632 --KGVVNLsysvintFHLGKEDVFLqFATIIFDASIMEIF-PILLCGGRMHLiseiekRSAEEFINVSQkyGITNVVL-P 707
Cdd:PRK09029  163 saEGVLSL-------MPFTAQDSWL-LSLPLFHVSGQGIVwRWLYAGATLVV------RDKQPLEQALA--GCTHASLvP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  708 TAFFKLIADMPKEMLLklnsvKRLFVGGETLPAESVRKWQSK-----LGlkipvlnaYGPTE--TTVCAtmyevngeiqK 780
Cdd:PRK09029  227 TQLWRLLDNRSEPLSL-----KAVLLGGAAIPVELTEQAEQQgircwCG--------YGLTEmaSTVCA----------K 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  781 EISNIP-IGKPIANSEVFVispfntlcpsgVVGELFIGGDGVANGYLNQKEKT-----EGAFISldksynRDKkmyctGD 854
Cdd:PRK09029  284 RADGLAgVGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLVplvndEGWFAT------RDR-----GE 341

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 446581728  855 lvrlLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVV 901
Cdd:PRK09029  342 ----WQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFV 384
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 608-964 6.70e-21

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 97.17  E-value: 6.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  608 IEDAAYIIYTSGSTGLPKgvVVPHKgVVNLSYS--VINTFHLGKEDVFLQFATIIF--DASIMEIFPILLCGGRMHLISE 683
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPK--LAQHT-HSNEVYNawMLALNSLFDPDDVLLCGLPLFhvNGSVVTLLTPLASGAHVVLAGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  684 IEKRSA---EEFINVSQKYGITNVV-LPTAffkLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLkiPVLNA 759
Cdd:cd05944    78 AGYRNPglfDNFWKLVERYRITSLStVPTV---YAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGL--PVVEG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  760 YGPTETTVCATMYEVNGEiqKEISNIPIGKPIANSEVFVISPFNTL---CPSGVVGELFIGGDGVANGYLNQkEKTEGAF 836
Cdd:cd05944   153 YGLTEATCLVAVNPPDGP--KRPGSVGLRLPYARVRIKVLDGVGRLlrdCAPDEVGEICVAGPGVFGGYLYT-EGNKNAF 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  837 IsldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVkIRG-YRIELDEIEGTLFKHPEVRDAVVFTyQND----KIVC 911
Cdd:cd05944   230 V--------ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAFAGAVG-QPDahagELPV 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728  912 FYLS-KDNTELKQEALKTFLSESLPD-FMMPNYIFHLESFPVSPSGKLDRKKLEL 964
Cdd:cd05944   300 AYVQlKPGAVVEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRA 354
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 495-962 9.57e-21

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 98.75  E-value: 9.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  495 ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKK 574
Cdd:cd17642    45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSK 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  575 EYRGLVERFA-----IHTIYL----EDFHYANSIENIASTHTI----------------EDAAYIIYTSGSTGLPKGVVV 629
Cdd:cd17642   125 KGLQKVLNVQkklkiIKTIIIldskEDYKGYQCLYTFITQNLPpgfneydfkppsfdrdEQVALIMNSSGSTGLPKGVQL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  630 PHKGVVnlsysviNTFHLGKEDVFLQfaTIIFDASIMEIFPI------------LLCGGRMHLISEIEKrsaEEFINVSQ 697
Cdd:cd17642   205 THKNIV-------ARFSHARDPIFGN--QIIPDTAILTVIPFhhgfgmfttlgyLICGFRVVLMYKFEE---ELFLRSLQ 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  698 KYGITNVVL-PTaffkLIADMPKEMLLK---LNSVKRLFVGGETLPAESVRKWQSKLGLKIpVLNAYGPTETTVCATmye 773
Cdd:cd17642   273 DYKVQSALLvPT----LFAFFAKSTLVDkydLSNLHEIASGGAPLSKEVGEAVAKRFKLPG-IRQGYGLTETTSAIL--- 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  774 vngeIQKEISNIP--IGKPIANSEVFVISPFN--TLCPSGvVGELFIGGDGVANGYLNQKEKTEGAFisldksyNRDKKM 849
Cdd:cd17642   345 ----ITPEGDDKPgaVGKVVPFFYAKVVDLDTgkTLGPNE-RGELCVKGPMIMKGYVNNPEATKALI-------DKDGWL 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  850 YcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK-------IVCFYLSKDNTElk 922
Cdd:cd17642   413 H-SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDagelpaaVVVLEAGKTMTE-- 489

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 446581728  923 QEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd17642   490 KEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1080-1498 9.70e-21

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 97.71  E-value: 9.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1080 LSSAQKriWFLNKYNAINRVYDTPLHIYIEPSLNKDILQDTIRFLVERHEMLRTVFIERNGEPRQVILNSIAiDLIHDEI 1159
Cdd:cd19534     4 LTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVE-ELFRLEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1160 EHMSKKEQQEYIRTTINQTDHTpFDLEKGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYSAFAKRRNP 1239
Cdd:cd19534    81 VDLSSLAQAAAIEALAAEAQSS-LDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1240 ELPTiSNRYVDYAEWEQVQLNLGRWDTEKSYWMAELAAPLPilNLPLDFSRNRQSTnkgTVFEMKLDNEMKESL-KQVCE 1318
Cdd:cd19534   160 PLPS-KTSFQTWAELLAEYAQSPALLEELAYWRELPAADYW--GLPKDPEQTYGDA---RTVSFTLDEEETEALlQEANA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1319 QENISMYMLFLAAYIQLLHYLTDQKdiivgTPVV-----GRnHQEFEKIQ-----GFFVNTLAIRTQLNDVKNLTQLLQV 1388
Cdd:cd19534   234 AYRTEINDLLLAALALAFQDWTGRA-----PPAIfleghGR-EEIDPGLDlsrtvGWFTSMYPVVLDLEASEDLGDTLKR 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1389 VREKC---------------LNSFQNQSYPFDKVIEqinpdrsfgnnpifsTMFSY--QKDILQQHDAYKLQLLPN-KQD 1450
Cdd:cd19534   308 VKEQLrripnkgigygilryLTPEGTKRLAFHPQPE---------------ISFNYlgQFDQGERDDALFVSAVGGgGSD 372

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728 1451 ISK-------FDISLAVEEG-LDyvgISFEYDINLFKEESINRFTQNLLNILDAFI 1498
Cdd:cd19534   373 IGPdtprfalLDINAVVEGGqLV---ITVSYSRNMYHEETIQQLADSYKEALEALI 425
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 496-962 1.21e-20

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 98.69  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  496 TYYELQQRSNQIVNYLREN-DLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKK 574
Cdd:cd05928    43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  575 EYRGLVERFA-----IHTIYL-------------EDFHYANSIENIASTHTiEDAAYIIYTSGSTGLPKGVVVPHkGVVN 636
Cdd:cd05928   123 ELAPEVDSVAsecpsLKTKLLvseksrdgwlnfkELLNEASTEHHCVETGS-QEPMAIYFTSGTTGSPKMAEHSH-SSLG 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  637 LSYSVINTFHLG--KEDVFLQFA-TIIFDASIMEIFPILLCGGRMhLISEIEKRSAEEFINVSQKYGITNVV-LPTAFFK 712
Cdd:cd05928   201 LGLKVNGRYWLDltASDIMWNTSdTGWIKSAWSSLFEPWIQGACV-FVHHLPRFDPLVILKTLSSYPITTFCgAPTVYRM 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  713 LIADMPKEmlLKLNSVKRLFVGGETLPAESVRKWQSKLGLKIpvLNAYGPTETTV-CATMYEVngeiqkEISNIPIGKPI 791
Cdd:cd05928   280 LVQQDLSS--YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI--YEGYGQTETGLiCANFKGM------KIKPGSMGKAS 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  792 ANSEVFVISPFNTLCPSGVVGELFIGGD-----GVANGYLNQKEKTegafislDKSYNRDkkMYCTGDLVRLLANGNLEF 866
Cdd:cd05928   350 PPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKT-------AATIRGD--FYLTGDRGIMDEDGYFWF 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  867 IGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFT----YQNDKIVCF------YLSKDNTELKQEaLKTFLSESLPD 936
Cdd:cd05928   421 MGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSspdpIRGEVVKAFvvlapqFLSHDPEQLTKE-LQQHVKSVTAP 499

                         490       500
                  ....*....|....*....|....*.
gi 446581728  937 FMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05928   500 YKYPRKVEFVQELPKTVTGKIQRNEL 525
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 610-959 1.41e-20

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 95.41  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLqfatiifdaSIMEIFPI--------LLCGGRMHLI 681
Cdd:cd17637     1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYL---------NMLPLFHIaglnlalaTFHAGGANVV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  682 seIEKRSAEEFINVSQKYGITnvvlptaffkLIADMPKeML-----------LKLNSVKrlFVGGETLPaESVRKWQSKL 750
Cdd:cd17637    72 --MEKFDPAEALELIEEEKVT----------LMGSFPP-ILsnlldaaeksgVDLSSLR--HVLGLDAP-ETIQRFEETT 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  751 GLKIPVLnaYGPTETTVCATMYEVNgeiqkeisNIP--IGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQ 828
Cdd:cd17637   136 GATFWSL--YGQTETSGLVTLSPYR--------ERPgsAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNL 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  829 KEKTEGAFisldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQ--VKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN 906
Cdd:cd17637   206 PELTAYTF---------RNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPD 276

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  907 D------KIVCfyLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDR 959
Cdd:cd17637   277 PkwgegiKAVC--VLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 1543-2025 1.75e-20

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 98.53  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIATATE----SLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAA-------YI 1611
Cdd:PRK05605   38 YDNAVARFGDRPALDffgaTTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvvehnplYT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1612 PIDVKYP-ED--------------RINYIVRDSEACRIITSNKFKSHLNVSDYKVSI---------------------IE 1655
Cdd:PRK05605  118 AHELEHPfEDhgarvaivwdkvapTVERLRRTTPLETIVSVNMIAAMPLLQRLALRLpipalrkaraaltgpapgtvpWE 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1656 DIYRTTINDDVKILNKP----DDLAYVIYTSGSTGKPKGTLLTHKGVL-NLVEWRNEVFQISPNDKVtqFYS-----HSF 1725
Cdd:PRK05605  198 TLVDAAIGGDGSDVSHPrptpDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQGKAWVPGLGDGPER--VLAalpmfHAY 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1726 DSSVSEIFSTLLnGAELYLLSdeqRYSTVEYAQAIQETQATIsdLPTVffNELSTSLTKLDSEK---IRSLRFIIMGGEA 1802
Cdd:PRK05605  276 GLTLCLTLAVSI-GGELVLLP---APDIDLILDAMKKHPPTW--LPGV--PPLYEKIAEAAEERgvdLSGVRNAFSGAMA 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1803 ASTNAIRSWQNTFKNQvqLVNEYGPTEATvsamyyfiPVLEGenNLLGSVP----IGIPISNTKVHILN--SYMQYCPVG 1876
Cdd:PRK05605  348 LPVSTVELWEKLTGGL--LVEGYGLTETS--------PIIVG--NPMSDDRrpgyVGVPFPDTEVRIVDpeDPDETMPDG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1877 CMGELYIESLGLAQGYWKQKEKTKQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKdKQVKIR-GHRIELGEIED 1955
Cdd:PRK05605  416 EEGELLVRGPQVFKGYWNRPEETAKSFLDG---------WFRTGDVVVMEEDGFIRIVDRI-KELIITgGFNVYPAEVEE 485

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446581728 1956 AMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK05605  486 VLREHPGVEDAAVVglpREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 479-962 1.84e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 98.08  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSItMEReiDTIVWILGILKSGGVYVPI---DPKFPE 555
Cdd:PRK07788   59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LAR--NHRGFVLALYAAGKVGARIillNTGFSG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  556 KRIEYILKDSESQMIITKKEYRGLVE-------RFAIHTIYLEDFHYANS----IENIASTHTIE-------DAAYIIYT 617
Cdd:PRK07788  136 PQLAEVAAREGVKALVYDDEFTDLLSalppdlgRLRAWGGNPDDDEPSGStdetLDDLIAGSSTAplpkppkPGGIVILT 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  618 SGSTGLPKGVVVPH------------------KGVVNLSYSVintFH-LGkedvFLQF-------ATIIFdasiMEIFpi 671
Cdd:PRK07788  216 SGTTGTPKGAPRPEpsplaplagllsrvpfraGETTLLPAPM---FHaTG----WAHLtlamalgSTVVL----RRRF-- 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  672 llcggrmhliseiekrSAEEFINVSQKYGITN-VVLPTaFFKLIADMPKEMLLK--LNSVKRLFVGGETLPAESVRKWQS 748
Cdd:PRK07788  283 ----------------DPEATLEDIAKHKATAlVVVPV-MLSRILDLGPEVLAKydTSSLKIIFVSGSALSPELATRALE 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  749 KLGlkiPVL-NAYGPTETTVC--ATMyevngeiqKEISNIP--IGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVAN 823
Cdd:PRK07788  346 AFG---PVLyNLYGSTEVAFAtiATP--------EDLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFE 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  824 GYlnqkekTEGafisldksynRDKK----MYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDA 899
Cdd:PRK07788  415 GY------TDG----------RDKQiidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA 478

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728  900 VVFTYQND----KIVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK07788  479 AVIGVDDEefgqRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 1541-2025 4.29e-20

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 96.41  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1541 MQVDRQPERIAIA--TATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYP 1618
Cdd:PRK09088    3 FHARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1619 EDRINYIVRDSEAcRIItsnkfkshlnVSDYKVS----IIEDIYRTTINDDVKILN-----KPDDLAYVIYTSGSTGKPK 1689
Cdd:PRK09088   83 ASELDALLQDAEP-RLL----------LGDDAVAagrtDVEDLAAFIASADALEPAdtpsiPPERVSLILFTSGTSGQPK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1690 GTLLTHK---------GVLNLVEWRNEVFQISPndkvtQFYSHSFDSSVSEIF---STLL--NGAE----LYLLSDeQRY 1751
Cdd:PRK09088  152 GVMLSERnlqqtahnfGVLGRVDAHSSFLCDAP-----MFHIIGLITSVRPVLavgGSILvsNGFEpkrtLGRLGD-PAL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1752 STVEYAQAIQETQAtISDLPTvffnelstsltkLDSEKIRSLRFIIMGGEAASTNAIRSWqntFKNQVQLVNEYGPTEA- 1830
Cdd:PRK09088  226 GITHYFCVPQMAQA-FRAQPG------------FDAAALRHLTALFTGGAPHAAEDILGW---LDDGIPMVDGFGMSEAg 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1831 TVSAMYYFIPVLEGEnnlLGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFse 1910
Cdd:PRK09088  290 TVFGMSVDCDVIRAK---AGAA--GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-- 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1911 dnskrlYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGI 1987
Cdd:PRK09088  363 ------FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVgmaDAQWGEVGYLAIVPADGA 436

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 446581728 1988 GIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK09088  437 PLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
PRK13382 PRK13382
bile acid CoA ligase;
494-962 5.59e-20

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 96.37  E-value: 5.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  494 SITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITK 573
Cdd:PRK13382   68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  574 KEYRGLVER------FAIHTIYLEDFHYANSIENIASTH-------TIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYS 640
Cdd:PRK13382  148 EEFSATVDRaladcpQATRIVAWTDEDHDLTVEVLIAAHagqrpepTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  641 VINTFHLGKEDVFL---------QFATIIFDASimeifpiLLCggRMHLISEIEKRSAEEFINVSQKYGItnVVLPTaFF 711
Cdd:PRK13382  228 ILDRTPWRAEEPTVivapmfhawGFSQLVLAAS-------LAC--TIVTRRRFDPEATLDLIDRHRATGL--AVVPV-MF 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  712 KLIADMPKEMLLKLN--SVKRLFVGGETLPAESVRKWQSKLGlkiPVL-NAYGPTETTVCATmyEVNGEIQKEISNIpiG 788
Cdd:PRK13382  296 DRIMDLPAEVRNRYSgrSLRFAAASGSRMRPDVVIAFMDQFG---DVIyNNYNATEAGMIAT--ATPADLRAAPDTA--G 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  789 KPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYlnqkekTEGAfislDKSYNrdKKMYCTGDLVRLLANGNLEFIG 868
Cdd:PRK13382  369 RPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------TSGS----TKDFH--DGFMASGDVGYLDENGRLFVVG 436

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  869 RKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIF 944
Cdd:PRK13382  437 RDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQygqrLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIV 516

                         490
                  ....*....|....*...
gi 446581728  945 HLESFPVSPSGKLDRKKL 962
Cdd:PRK13382  517 VLDELPRGATGKILRREL 534
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 1543-2026 6.09e-20

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 96.21  E-value: 6.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRI 1622
Cdd:PRK06188   22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1623 NYIVRDSEA-CRIITSNKFKSH----------------LNVSDYKVSIIE--DIY--RTTINDDVkilnkPDDLAYVIYT 1681
Cdd:PRK06188  102 AYVLEDAGIsTLIVDPAPFVERalallarvpslkhvltLGPVPDGVDLLAaaAKFgpAPLVAAAL-----PPDIAGLAYT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1682 SGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK--VTQFYSHsfdSSVSEIFSTLLNGAELYLLsdeQRYSTVEYAQA 1759
Cdd:PRK06188  177 GGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRflMCTPLSH---AGGAFFLPTLLRGGTVIVL---AKFDPAEVLRA 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1760 IQETQATISDL-PTVFFnelstslTKLDSEKIR-----SLRFIIMGGEAAS----TNAIRSWQNTFknqVQLvneYGPTE 1829
Cdd:PRK06188  251 IEEQRITATFLvPTMIY-------ALLDHPDLRtrdlsSLETVYYGASPMSpvrlAEAIERFGPIF---AQY---YGQTE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1830 ATvsamyYFIPVLEGENN------LLGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAF 1903
Cdd:PRK06188  318 AP-----MVITYLRKRDHdpddpkRLTSC--GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1904 ISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQ----------------AV 1967
Cdd:PRK06188  391 RDG---------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQvavigvpdekwgeavtAV 461

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446581728 1968 VTQTEGGML----LQAYYKTVDGigieknklAIHlsnvlpeymVPKYYSHVLEIPITANGKID 2026
Cdd:PRK06188  462 VVLRPGAAVdaaeLQAHVKERKG--------SVH---------APKQVDFVDSLPLTALGKPD 507
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 41-335 7.25e-20

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 94.67  E-value: 7.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   41 IIKLKGNLQIEVLKKALTTIVQSHPALRT-IFKKRDEKIKQLIQKNVEFDIpikdltafkntEQKSILKNFLESIVNEKF 119
Cdd:cd19545    27 VFELPPDIDLARLQAAWEQVVQANPILRTrIVQSDSGGLLQVVVKESPISW-----------TESTSLDEYLEEDRAAPM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  120 SLEeGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYgellQGKSNVEFeSPYKNLVKHeesfIDSAIYK 199
Cdd:cd19545    96 GLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY----QGEPVPQP-PPFSRFVKY----LRQLDDE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  200 EGSSYWKDYLQGELtptefPIDFNKMNEKRYT---DKNISKNINSDlfyqiqcfakknNISIYRVMLSTYC-----TLLH 271
Cdd:cd19545   166 AAAEFWRSYLAGLD-----PAVFPPLPSSRYQprpDATLEHSISLP------------SSASSGVTLATVLraawaLVLS 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  272 QMTNAEEIIVGIPINTR--PYTEERNTFGYFVNTLPIRITIEKGETFKGILNKVNKSIHLAITYKH 335
Cdd:cd19545   229 RYTGSDDVVFGVTLSGRnaPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEH 294
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1556-2033 7.35e-20

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 97.73  E-value: 7.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1556 TESLTYRQLNMSSnQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGaaYIPIdvkypedRINY---IVRDSEAC 1632
Cdd:PRK06814  656 NGPLTYRKLLTGA-FVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAG--RVPA-------MINFsagIANILSAC 725

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1633 R------IITSNKF--KSHLNVS----DYKVSII--EDIyRTTINDDVKIL--------------NKPDDLAYVIYTSGS 1684
Cdd:PRK06814  726 KaaqvktVLTSRAFieKARLGPLiealEFGIRIIylEDV-RAQIGLADKIKgllagrfplvyfcnRDPDDPAVILFTSGS 804

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1685 TGKPKGTLLTHKgvlNLVEWRNEV---FQISPNDKVtqFYS----HSFDSSVSEIFsTLLNGAELYLLSDEQRYSTVeyA 1757
Cdd:PRK06814  805 EGTPKGVVLSHR---NLLANRAQVaarIDFSPEDKV--FNAlpvfHSFGLTGGLVL-PLLSGVKVFLYPSPLHYRII--P 876

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1758 QAIQETQATISDLPTVFFNELSTSLTKLDsekIRSLRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGPTEATvsamyy 1837
Cdd:PRK06814  877 ELIYDTNATILFGTDTFLNGYARYAHPYD---FRSLRYVFAGAEKVKEETRQTWMEKFG--IRILEGYGVTETA------ 945

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1838 fiPVLEGEN---NLLGSVPIGIPISNTKVHilnsymqycPV-----GcmGELYIESLGLAQGYWKqkektkqafISNPFS 1909
Cdd:PRK06814  946 --PVIALNTpmhNKAGTVGRLLPGIEYRLE---------PVpgideG--GRLFVRGPNVMLGYLR---------AENPGV 1003

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1910 -EDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQL-EGISQAVVT---QTEGGMLLQAyykTV 1984
Cdd:PRK06814 1004 lEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAVSipdARKGERIILL---TT 1080

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 446581728 1985 DGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKI 2033
Cdd:PRK06814 1081 ASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 504-962 9.88e-20

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 95.14  E-value: 9.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  504 SNQIVNYLRENDL---KKGQRVSITMereIDTIVWILGILKSGGVYVPIDPKFPEkrieyiLKDSESQMIITKKEYRGLV 580
Cdd:cd05929    24 SIALNRNARAAAAegvWIADGVYIYL---INSILTVFAAAAAWKCGACPAYKSSR------APRAEACAIIEIKAAALVC 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  581 ERFAIHTIYLEDFHYANSIENIASTHTIEDAAY--IIYTSGSTGLPKGVVVPHKGVVnlsysvINTFHL---------GK 649
Cdd:cd05929    95 GLFTGGGALDGLEDYEAAEGGSPETPIEDEAAGwkMLYSGGTTGRPKGIKRGLPGGP------PDNDTLmaaalgfgpGA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  650 EDVFLQFATIIFDASIMEIFPILLCGGrmHLISeIEKRSAEEFINVSQKYGITNVVL-PTAFFKLIAdMPKEMLLK--LN 726
Cdd:cd05929   169 DSVYLSPAPLYHAAPFRWSMTALFMGG--TLVL-MEKFDPEEFLRLIERYRVTFAQFvPTMFVRLLK-LPEAVRNAydLS 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  727 SVKRLFVGGETLPAESVRKWQSKLGLKIPVLnaYGPTEttvCATMYEVNGEiqkEISNIP--IGKPIAnSEVFVISPFNT 804
Cdd:cd05929   245 SLKRVIHAAAPCPPWVKEQWIDWGGPIIWEY--YGGTE---GQGLTIINGE---EWLTHPgsVGRAVL-GKVHILDEDGN 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  805 LCPSGVVGEL-FIGGDGVAngYLNQKEKTEgafisldKSYNRDKkMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIEL 883
Cdd:cd05929   316 EVPPGEIGEVyFANGPGFE--YTNDPEKTA-------AARNEGG-WSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYP 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  884 DEIEGTLFKHPEVRDAVVFTYQNDK-------IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGK 956
Cdd:cd05929   386 QEIENALIAHPKVLDAAVVGVPDEElgqrvhaVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGK 465


                  ....*.
gi 446581728  957 LDRKKL 962
Cdd:cd05929   466 LYRRLL 471
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1672-2026 1.00e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 93.70  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 PDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKV----TQFysHSFdSSVSEIFSTLLNGAELYLLSD 1747
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLlcglPLF--HVN-GSVVTLLTPLASGAHVVLAGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1748 E-QRYSTV--EYAQAIQETQAT-ISDLPTVffneLSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNtfKNQVQLVN 1823
Cdd:cd05944    78 AgYRNPGLfdNFWKLVERYRITsLSTVPTV----YAALLQVPVNADISSLRFAMSGAAPLPVELRARFED--ATGLPVVE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1824 EYGPTEAT-VSAMYYfiPvlEGENNLlGSVPIGIPISNTKVHILN---SYMQYCPVGCMGELYIESLGLAQGYwKQKEKT 1899
Cdd:cd05944   152 GYGLTEATcLVAVNP--P--DGPKRP-GSVGLRLPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGY-LYTEGN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1900 KQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKdKQVKIRG-HRIELGEIEDAMLQLEGIS-QAVVTQTE--GGM 1975
Cdd:cd05944   226 KNAFVADGW--------LNTGDLGRLDADGYLFITGRA-KDLIIRGgHNIDPALIEEALLRHPAVAfAGAVGQPDahAGE 296

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446581728 1976 LLQAYYKTVDGIGIEKNKLAIHLSNVLPEY-MVPKYYSHVLEIPITANGKID 2026
Cdd:cd05944   297 LPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVF 348
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 475-962 1.82e-19

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 95.32  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKSPNQIAI----SMGDQS--ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVP 548
Cdd:cd05966    59 LDRHLKERGDKVAIiwegDEPDQSrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  549 IDPKFPEKRIEYILKDSESQMIITKKE-YRG------------------------LVERFAIHTIYLE--DFHYANSIEN 601
Cdd:cd05966   139 VFAGFSAESLADRINDAQCKLVITADGgYRGgkviplkeivdealekcpsvekvlVVKRTGGEVPMTEgrDLWWHDLMAK 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  602 IASTHTI-----EDAAYIIYTSGSTGLPKGVVVPHKG-VVNLSYSVINTFHLGKEDVFLQFATI--IFDASIMEIFPilL 673
Cdd:cd05966   219 QSPECEPewmdsEDPLFILYTSGSTGKPKGVVHTTGGyLLYAATTFKYVFDYHPDDIYWCTADIgwITGHSYIVYGP--L 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  674 CGGRMHLISEiekrSAEEFINVS------QKYGITnvVL---PTA---FFKLIADMPKEMLLK----LNSVkrlfvgGET 737
Cdd:cd05966   297 ANGATTVMFE----GTPTYPDPGrywdivEKHKVT--IFytaPTAiraLMKFGDEWVKKHDLSslrvLGSV------GEP 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  738 LPAESVRKWQSKLGL-KIPVLNAYGPTETtvcatmyevnGEIQkeISNIPIG---KPIANS------EVFVISPFNTLCP 807
Cdd:cd05966   365 INPEAWMWYYEVIGKeRCPIVDTWWQTET----------GGIM--ITPLPGAtplKPGSATrpffgiEPAILDEEGNEVE 432

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  808 SGVVGELFIGGD--GVANGYLNQKEKTEgafisldKSY-NRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELD 884
Cdd:cd05966   433 GEVEGYLVIKRPwpGMARTIYGDHERYE-------DTYfSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTA 505

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  885 EIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKD----NTELKQEaLKTFLSESLPDFMMPNYIFHLESFPVSPSGK 956
Cdd:cd05966   506 EVESALVAHPAVAEAAVVGRPHDikgeAIYAFVTLKDgeepSDELRKE-LRKHVRKEIGPIATPDKIQFVPGLPKTRSGK 584


                  ....*.
gi 446581728  957 LDRKKL 962
Cdd:cd05966   585 IMRRIL 590
PRK07529 PRK07529
AMP-binding domain protein; Validated
 1544-2025 2.69e-19

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 95.02  E-value: 2.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1544 DRQPERIAI-----ATAT---ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYiPIDV 1615
Cdd:PRK07529   36 ARHPDAPALsflldADPLdrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1616 KYPEDRINYIVRDSEACRIITSNKF--------------------------------------------KSHLNVSDYKV 1651
Cdd:PRK07529  115 LLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqkvaevlaalpelrtvvevdlarylpgpkrlavplirrKAHARILDFDA 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1652 SIIEDIYRTTINDDVKilnKPDDLAYVIYTSGSTGKPKGTLLTHKG-VLNlvEWR-NEVFQISPNDkvTQFYS----HSF 1725
Cdd:PRK07529  195 ELARQPGDRLFSGRPI---GPDDVAAYFHTGGTTGMPKLAQHTHGNeVAN--AWLgALLLGLGPGD--TVFCGlplfHVN 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1726 dSSVSEIFSTLLNGAELYLLS-----DEQRYStvEYAQAIQETQAT-ISDLPTVFfneLSTSLTKLDSEKIRSLRFIIMG 1799
Cdd:PRK07529  268 -ALLVTGLAPLARGAHVVLATpqgyrGPGVIA--NFWKIVERYRINfLSGVPTVY---AALLQVPVDGHDISSLRYALCG 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1800 GEAASTNAIRSWQNtfKNQVQLVNEYGPTEAT-VSAMYYfipvLEGENNLlGSVPIGIPISNTKVHILN---SYMQYCPV 1875
Cdd:PRK07529  342 AAPLPVEVFRRFEA--ATGVRIVEGYGLTEATcVSSVNP----PDGERRI-GSVGLRLPYQRVRVVILDdagRYLRDCAV 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1876 GCMGELYIESLGLAQGYwKQKEKTKQAFISnpfsednsKRLYRTGDLVRWLPNGNIEFMGRKdKQVKIR-GHRIELGEIE 1954
Cdd:PRK07529  415 DEVGVLCIAGPNVFSGY-LEAAHNKGLWLE--------DGWLNTGDLGRIDADGYFWLTGRA-KDLIIRgGHNIDPAAIE 484

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1955 DAMLQLEGISQA-VVTQTEG--GMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYM-VPKYYSHVLEIPITANGKI 2025
Cdd:PRK07529  485 EALLRHPAVALAaAVGRPDAhaGELPVAYVQLKPGASATEAELLAFARDHIAERAaVPKHVRILDALPKTAVGKI 559
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1532-2025 3.82e-19

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 93.97  E-value: 3.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1532 FQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLL-EKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAY 1610
Cdd:PRK08974   22 YQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1611 IPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIY-----------RTTINDDVKILNK-------- 1671
Cdd:PRK08974  102 VNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILtrmgdqlstakGTLVNFVVKYIKRlvpkyhlp 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 -----------------------PDDLAYVIYTSGSTGKPKGTLLTHKGVL-NL--VEWRNEVFQISPNDKVTQ---FYs 1722
Cdd:PRK08974  182 daisfrsalhkgrrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLeqAKAAYGPLLHPGKELVVTalpLY- 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1723 HSFDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETqaTISDLPTVFfNEL--STSLTKLDsekIRSLRFIIMGG 1800
Cdd:PRK08974  261 HIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFT--AITGVNTLF-NALlnNEEFQELD---FSSLKLSVGGG 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1801 EAASTNAIRSWQNTFKNQvqLVNEYGPTEAT--VSAMYYfipVLEGENnllGSvpIGIPISNTKVHILNSYMQYCPVGCM 1878
Cdd:PRK08974  335 MAVQQAVAERWVKLTGQY--LLEGYGLTECSplVSVNPY---DLDYYS---GS--IGLPVPSTEIKLVDDDGNEVPPGEP 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1879 GELYIESLGLAQGYWKQKEKT----KQAFISnpfsednskrlyrTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIE 1954
Cdd:PRK08974  405 GELWVKGPQVMLGYWQRPEATdeviKDGWLA-------------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE 471

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581728 1955 DAMLQLEGISQAV---VTQTEGGMLLQAYYKTVDGiGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK08974  472 DVVMLHPKVLEVAavgVPSEVSGEAVKIFVVKKDP-SLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 483-962 5.30e-19

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 93.93  E-value: 5.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYIL 562
Cdd:PLN03102   28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  563 KDSESQMIITKKEYRGLVER----------------FAIHTI------YLEDFHYANSIENIAST----------HTIED 610
Cdd:PLN03102  108 RHAKPKILFVDRSFEPLAREvlhllssedsnlnlpvIFIHEIdfpkrpSSEELDYECLIQRGEPTpslvarmfriQDEHD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  611 AAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQfatiifdasimeIFPILLCGGRMHLISE------- 683
Cdd:PLN03102  188 PISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLW------------TLPMFHCNGWTFTWGTaarggts 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  684 --IEKRSAEEFINVSQKYGITNV-VLPTAFFKLIADMPKEMLLKLNSVKRLfVGGETLPAESVRKWQsKLGLKipVLNAY 760
Cdd:PLN03102  256 vcMRHVTAPEIYKNIEMHNVTHMcCVPTVFNILLKGNSLDLSPRSGPVHVL-TGGSPPPAALVKKVQ-RLGFQ--VMHAY 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  761 GPTETT----VCATMYEVNG-------EIQKE--ISNIPIGK-PIANSEVFVISPFNtlcpSGVVGELFIGGDGVANGYL 826
Cdd:PLN03102  332 GLTEATgpvlFCEWQDEWNRlpenqqmELKARqgVSILGLADvDVKNKETQESVPRD----GKTMGEIVIKGSSIMKGYL 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  827 NQKEKTEGAFisldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF---- 902
Cdd:PLN03102  408 KNPKATSEAF---------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVamph 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  903 -TYQNDKIVCFYLSKDNTELKQEALK---------TFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PLN03102  479 pTWGETPCAFVVLEKGETTKEDRVDKlvtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 1543-2026 5.44e-19

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 93.16  E-value: 5.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAayIPIdVKYPEDR- 1621
Cdd:cd05920    25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPV-LALPSHRr 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1622 --INYIVRDSEACRIITSNKFKSHLNVSDYKvsiiediyrttinddvKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVL 1699
Cdd:cd05920   102 seLSAFCAHAEAVAYIVPDRHAGFDHRALAR----------------ELAESIPEVALFLLSGGTTGTPKLIPRTHNDYA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1700 NLVEWRNEVFQISPNDKvtqfY------SHSFDSSVSEIFSTLLNGAELYLLSDEqrySTVEYAQAIQETQATISDL-PT 1772
Cdd:cd05920   166 YNVRASAEVCGLDQDTV----YlavlpaAHNFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIEREGVTVTALvPA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1773 VffneLSTSLTKLDSEK--IRSLRFIIMGGEAASTNAIRSWQNTFKNQVQLVneYGPTEATVSamyyFIPVLEGENNLLG 1850
Cdd:cd05920   239 L----VSLWLDAAASRRadLSSLRLLQVGGARLSPALARRVPPVLGCTLQQV--FGMAEGLLN----YTRLDDPDEVIIH 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1851 SVpiGIPIS-NTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNG 1929
Cdd:cd05920   309 TQ--GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF--------YRTGDLVRRTPDG 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1930 NIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGMLLQAYYKTV--DGIGIEKNKLAIHLSNV-LPEYM 2006
Cdd:cd05920   379 YLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVvlRDPPPSAAQLRRFLRERgLAAYK 458

                         490       500
                  ....*....|....*....|
gi 446581728 2007 VPKYYSHVLEIPITANGKID 2026
Cdd:cd05920   459 LPDRIEFVDSLPLTAVGKID 478
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 475-902 6.37e-19

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 93.40  E-value: 6.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  475 IDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFP 554
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  555 EKRIEYILKDSESQMIITKKEYRGLVER-----------------FAIHTIYLEDFHYANS---IENIASTH--TIEDAA 612
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEELVEAFEEaradlarpprlwvaggdTLDDPEGYEDLAAAAAgapTTNPASRSgvTAKDTA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  613 YIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVF-----LQFATiifdASIMEIFPILLCGGRMHLiseIEKR 687
Cdd:PRK08279  203 FYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLycclpLYHNT----GGTVAWSSVLAAGATLAL---RRKF 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  688 SAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVkRLFVG-GetLPAESVRKWQSKLGlkIP-VLNAYGPTET 765
Cdd:PRK08279  276 SASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRL-RLMIGnG--LRPDIWDEFQQRFG--IPrILEFYAASEG 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  766 TVcaTMYEVNGeIQKEISNIPI---------------GKPIANSEVFVIspfntLCPSGVVGELF--IGGDGVANGYlNQ 828
Cdd:PRK08279  351 NV--GFINVFN-FDGTVGRVPLwlahpyaivkydvdtGEPVRDADGRCI-----KVKPGEVGLLIgrITDRGPFDGY-TD 421

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  829 KEKTE-----GAFISLDKSYNrdkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF 902
Cdd:PRK08279  422 PEASEkkilrDVFKKGDAWFN-------TGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVY 493
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 479-956 8.75e-19

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 92.63  E-value: 8.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGD-QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKR 557
Cdd:PRK07514   12 AFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  558 IEYILKDSESQMIITKKEYRGLVER--FAIHTIYLE--DFHYANSIENIASTHT---------IEDAAYIIYTSGSTGLP 624
Cdd:PRK07514   92 LDYFIGDAEPALVVCDPANFAWLSKiaAAAGAPHVEtlDADGTGSLLEAAAAAPddfetvprgADDLAAILYTSGTTGRS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  625 KGVVVPHKGVVNLSYSVINTFHLGKEDVFLQfATIIFDAS--IMEIFPILLCGGRMHLISeieKRSAEEFInvsQKYGIT 702
Cdd:PRK07514  172 KGAMLSHGNLLSNALTLVDYWRFTPDDVLIH-ALPIFHTHglFVATNVALLAGASMIFLP---KFDPDAVL---ALMPRA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  703 NVVL--PTAFFKLIAD--MPKEMLLKLnsvkRLFVGGET-LPAESVRKWQSKLGLKIpvLNAYGPTETtvcaTMYEVN-- 775
Cdd:PRK07514  245 TVMMgvPTFYTRLLQEprLTREAAAHM----RLFISGSApLLAETHREFQERTGHAI--LERYGMTET----NMNTSNpy 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  776 -GEiqkeisNIP--IGKPIANSEVFVISPFN-TLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMYC 851
Cdd:PRK07514  315 dGE------RRAgtVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF--------RADGFFI 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  852 TGDLVRLLANGNLEFIGRKDNQVKIRGYRI-------ELDEIEGTL------FKHP---EVRDAVVftyqndkiVCfyls 915
Cdd:PRK07514  381 TGDLGKIDERGYVHIVGRGKDLIISGGYNVypkevegEIDELPGVVesavigVPHPdfgEGVTAVV--------VP---- 448

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 446581728  916 KDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGK 956
Cdd:PRK07514  449 KPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGK 489
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 495-962 9.11e-19

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 92.66  E-value: 9.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  495 ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITkk 574
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  575 eyrglverfaihtiyledfhyansieniasTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVnlsySVINTF------HLG 648
Cdd:cd17639    84 ------------------------------DGKPDDLACIMYTSGSTGNPKGVMLTHGNLV----AGIAGLgdrvpeLLG 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  649 KEDVFLQFATIifdASIMEIFPILLC---GGRM------HLISEIEKRS---AEEF--------------------INVS 696
Cdd:cd17639   130 PDDRYLAYLPL---AHIFELAAENVClyrGGTIgygsprTLTDKSKRGCkgdLTEFkptlmvgvpaiwdtirkgvlAKLN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  697 QKYGITNVVLPTAF---FKLIADMPKEMLL-KL--NSVKRL--------FVGGETLPAESvRKWQSKLGLkiPVLNAYGP 762
Cdd:cd17639   207 PMGGLKRTLFWTAYqskLKALKEGPGTPLLdELvfKKVRAAlggrlrymLSGGAPLSADT-QEFLNIVLC--PVIQGYGL 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  763 TETTVCATMYEVnGEIQKEIsnipIGKPIANSEVFVIS------PFNTLCPSGvvgELFIGGDGVANGYLNQKEKTEGAF 836
Cdd:cd17639   284 TETCAGGTVQDP-GDLETGR----VGPPLPCCEIKLVDweeggySTDKPPPRG---EILIRGPNVFKGYYKNPEKTKEAF 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  837 isldksynRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIR-GYRIELDEIEGTLFKHPEVRDAVVFTYQN-DKIVCF-- 912
Cdd:cd17639   356 --------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDkSYPVAIvv 427

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  913 ----YLSK----------------DNTELKQEALKTFL----SESLPDFMMPNYIfHLESFP-------VSPSGKLDRKK 961
Cdd:cd17639   428 pnekHLTKlaekhgvinseweelcEDKKLQKAVLKSLAetarAAGLEKFEIPQGV-VLLDEEwtpenglVTAAQKLKRKE 506


                  .
gi 446581728  962 L 962
Cdd:cd17639   507 I 507
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 487-962 1.91e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 91.20  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  487 AISMGDQSITYYELQQRSNQIVNYLRendlkKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSE 566
Cdd:PRK07787   18 AVRIGGRVLSRSDLAGAATAVAERVA-----GARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  567 SQMII--TKKEYRGLvERFAIHTIYLEDFHYANSIEniasthtiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINT 644
Cdd:PRK07787   93 AQAWLgpAPDDPAGL-PHVPVRLHARSWHRYPEPDP--------DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  645 FHLGKEDVFLQfATIIFDAS--IMEIFPILLCGGRM-HLISEIEKRSAEEF-INVSQKYGItnvvlPTAFFKLIADmpkE 720
Cdd:PRK07787  164 WQWTADDVLVH-GLPLFHVHglVLGVLGPLRIGNRFvHTGRPTPEAYAQALsEGGTLYFGV-----PTVWSRIAAD---P 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  721 MLLKLNSVKRLFVGGET-LPAESVRKWQSKLGLkiPVLNAYGPTET--TVCAtmyEVNGEIQkeisniP--IGKPIANSE 795
Cdd:PRK07787  235 EAARALRGARLLVSGSAaLPVPVFDRLAALTGH--RPVERYGMTETliTLST---RADGERR------PgwVGLPLAGVE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  796 VFVISPFNTLCPSGV--VGELFIGGDGVANGYLNQKEKTEGAFisldksynRDKKMYCTGDLVRLLANGNLEFIGRKD-N 872
Cdd:PRK07787  304 TRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAF--------TADGWFRTGDVAVVDPDGMHRIVGREStD 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  873 QVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKDntELKQEALKTFLSESLPDFMMPNYIFHLES 948
Cdd:PRK07787  376 LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdlgqRIVAYVVGAD--DVAADELIDFVAQQLSVHKRPREVRFVDA 453

                         490
                  ....*....|....
gi 446581728  949 FPVSPSGKLDRKKL 962
Cdd:PRK07787  454 LPRNAMGKVLKKQL 467
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 1560-2026 2.10e-18

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 91.54  E-value: 2.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1560 TYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNK 1639
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1640 F-------KSHLNVSDYKVSIIEDI------------YRTTINDDVKILNKPD---DLAYVI-YTSGSTGKPKGTLLTHK 1696
Cdd:cd12119   107 FlplleaiAPRLPTVEHVVVMTDDAampepagvgvlaYEELLAAESPEYDWPDfdeNTAAAIcYTSGTTGNPKGVVYSHR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1697 -------GVLNlvewrNEVFQISPNDK----VTQFYSHSFDSSvseiFSTLLNGAELYLlsdEQRYSTVEY-AQAIQETQ 1764
Cdd:cd12119   187 slvlhamAALL-----TDGLGLSESDVvlpvVPMFHVNAWGLP----YAAAMVGAKLVL---PGPYLDPASlAELIEREG 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1765 ATISD-LPTVFFNELStSLTKLDSEkIRSLRFIIMGGEAASTNAIRSWQntfKNQVQLVNEYGPTE----ATVSAMYYFI 1839
Cdd:cd12119   255 VTFAAgVPTVWQGLLD-HLEANGRD-LSSLRRVVIGGSAVPRSLIEAFE---ERGVRVIHAWGMTEtsplGTVARPPSEH 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1840 PVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCPV--GCMGELYIESLGLAQGYWKQKEKTKQafisnpFSEDNskrLY 1917
Cdd:cd12119   330 SNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEA------LTEDG---WL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1918 RTGDLVRWLPNGNIEFMGR-KDkQVKIRGHRIELGEIEDAMLQLEGISQA----------------VVTQTEGgmllqay 1980
Cdd:cd12119   401 RTGDVATIDEDGYLTITDRsKD-VIKSGGEWISSVELENAIMAHPAVAEAavigvphpkwgerplaVVVLKEG------- 472

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 446581728 1981 yKTVDgigieKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:cd12119   473 -ATVT-----AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKID 512
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 980-1057 2.23e-18

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 81.44  E-value: 2.23e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  980 PISETEKRLAKTWAEILNLGKYRIGRDDDFFK-LGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIASLSAYIDKLMA 1057
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 609-958 2.38e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 89.36  E-value: 2.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPH-------KGVVNL---SYSVINTFHLGKED----VFLQFATIIFDASIMEIFPILLC 674
Cdd:cd05924     3 ADDLYILYTGGTTGMPKGVMWRQedifrmlMGGADFgtgEFTPSEDAHKAAAAaagtVMFPAPPLMHGTGSWTAFGGLLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  675 GGRMHLISEieKRSAEEFINVSQKYGITNVVL-PTAFFK-LIADMPKEMLLKLNSVKRLFVGGETLpAESVRKWQSKLGL 752
Cdd:cd05924    83 GQTVVLPDD--RFDPEEVWRTIEKHKVTSMTIvGDAMARpLIDALRDAGPYDLSSLFAISSGGALL-SPEVKQGLLELVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  753 KIPVLNAYGPTETTvcATMYEVNGEiqkeisNIPIGKP--IANSEVFVISPFNTLCPSGVVGELFIGGDG-VANGYLNQK 829
Cdd:cd05924   160 NITLVDAFGSSETG--FTGSGHSAG------SGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  830 EKTEGAFISLDksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK- 908
Cdd:cd05924   232 AKTAETFPEVD-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERw 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446581728  909 ---IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:cd05924   307 gqeVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 474-962 2.50e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 91.21  E-value: 2.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  474 LIDLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITME--REIDTIVWILGILksGGVYVPIDP 551
Cdd:PRK13383   40 LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRngRGFVTAVFAVGLL--GADVVPIST 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  552 KFPEKRIEYILKDSESQMIITKKEYrglVERFAI--HTIYLEDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVvv 629
Cdd:PRK13383  118 EFRSDALAAALRAHHISTVVADNEF---AERIAGadDAVAVIDPATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGV-- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  630 PHK----GVVNLSYSVINTFHLgKEDVFLQFATIIFDA--SIMEIFPILLCGG---RMHLisEIEKRSAEEFINVSQKYG 700
Cdd:PRK13383  193 PRApqlrSAVGVWVTILDRTRL-RTGSRISVAMPMFHGlgLGMLMLTIALGGTvltHRHF--DAEAALAQASLHRADAFT 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  701 ITNVVLPTaffklIADMPKEMLLK--LNSVKRLFVGGETLPAESVRKWQSKLGlkiPVL-NAYGPTETTVCATmyevngE 777
Cdd:PRK13383  270 AVPVVLAR-----ILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYG---DILyNGYGSTEVGIGAL------A 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  778 IQKEISNIP--IGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKtegAFISldksynrdkKMYCTGDL 855
Cdd:PRK13383  336 TPADLRDAPetVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGK---AVVD---------GMTSTGDM 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  856 VRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKDNTELKQEALKTFLS 931
Cdd:PRK13383  404 GYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErfghRLAAFVVLHPGSGVDAAQLRDYLK 483

                         490       500       510
                  ....*....|....*....|....*....|.
gi 446581728  932 ESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK13383  484 DRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
PLN02246 PLN02246
4-coumarate--CoA ligase
 496-962 2.59e-18

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 91.20  E-value: 2.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  496 TYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKE 575
Cdd:PLN02246   52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  576 YRGLVERFAIH---TIYLED------FHYA---NSIENIASTHTI--EDAAYIIYTSGSTGLPKGVVVPHKGVVNlsySV 641
Cdd:PLN02246  132 YVDKLKGLAEDdgvTVVTIDdppegcLHFSeltQADENELPEVEIspDDVVALPYSSGTTGLPKGVMLTHKGLVT---SV 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  642 IN-------TFHLGKEDVFLQFATIIfdaSIMEIFPILLCGGR----MHLISEIEKRSAEEFInvsQKYGIT--NVVLPT 708
Cdd:PLN02246  209 AQqvdgenpNLYFHSDDVILCVLPMF---HIYSLNSVLLCGLRvgaaILIMPKFEIGALLELI---QRHKVTiaPFVPPI 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  709 AFfkLIADMPKEMLLKLNSVKRLFVGGETLPAEsvrkWQSKLGLKIPvlNA-----YGPTETTVCATMYEVNGEIQKEIS 783
Cdd:PLN02246  283 VL--AIAKSPVVEKYDLSSIRMVLSGAAPLGKE----LEDAFRAKLP--NAvlgqgYGMTEAGPVLAMCLAFAKEPFPVK 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  784 NIPIGKPIANSEVFVISPfNTLC--PSGVVGELFIGGDGVANGYLNQKEKTEGafiSLDKsynrDKKMYcTGDLVRLLAN 861
Cdd:PLN02246  355 SGSCGTVVRNAELKIVDP-ETGAslPRNQPGEICIRGPQIMKGYLNDPEATAN---TIDK----DGWLH-TGDIGYIDDD 425

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  862 GNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI----VCFYLSKDNTELKQEALKTFLSESLPDF 937
Cdd:PLN02246  426 DELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAgevpVAFVVRSNGSEITEDEIKQFVAKQVVFY 505

                         490       500
                  ....*....|....*....|....*
gi 446581728  938 MMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PLN02246  506 KRIHKVFFVDSIPKAPSGKILRKDL 530
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 1555-2025 2.64e-18

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 91.78  E-value: 2.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1555 ATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRI 1634
Cdd:cd05968    88 TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1635 ITSNKF---------KSHLNVSDYKVSIIEDI--YRTTINDDVKIL-------------------NKPDDLAYVIYTSGS 1684
Cdd:cd05968   168 ITADGFtrrgrevnlKEEADKACAQCPTVEKVvvVRHLGNDFTPAKgrdlsydeeketagdgaerTESEDPLMIIYTSGT 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1685 TGKPKGTLLTH-----KGVLNLVewrnEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLL-------SDEQRYS 1752
Cdd:cd05968   248 TGKPKGTVHVHagfplKAAQDMY----FQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYdgapdhpKADRLWR 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1753 TVEyaqAIQETQATISdlPTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNairSWQNTF----KNQVQLVNEYGPT 1828
Cdd:cd05968   324 MVE---DHEITHLGLS--PTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPE---PWNWLFetvgKGRNPIINYSGGT 395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1829 EATvsamyyfipvlegeNNLLGSVPI--------GIPISNTKVHILNSYMQycPV-GCMGELYIES--LGLAQGYWKQKE 1897
Cdd:cd05968   396 EIS--------------GGILGNVLIkpikpssfNGPVPGMKADVLDESGK--PArPEVGELVLLApwPGMTRGFWRDED 459

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1898 KTKQAFISNpfsEDNskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAV---VTQTEGG 1974
Cdd:cd05968   460 RYLETYWSR---FDN---VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAaigVPHPVKG 533

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446581728 1975 MLLQAYYKTVDGI---GIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05968   534 EAIVCFVVLKPGVtptEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKV 587
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 493-901 4.25e-18

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 90.22  E-value: 4.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIIT 572
Cdd:cd05932     5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  573 KK------EYRGLVERFAIHTIYLED---FHY--------ANSIENiASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVV 635
Cdd:cd05932    85 GKlddwkaMAPGVPEGLISISLPPPSaanCQYqwddliaqHPPLEE-RPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  636 NLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEiekrSAEEFINVSQKYGitnvvlPTAFF---- 711
Cdd:cd05932   164 WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE----SLDTFVEDVQRAR------PTLFFsvpr 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  712 -------KLIADMPKEML--------------------LKLNSVKRLFVGGETLPaESVRKWQSKLGLkiPVLNAYGPTE 764
Cdd:cd05932   234 lwtkfqqGVQDKIPQQKLnlllkipvvnslvkrkvlkgLGLDQCRLAGCGSAPVP-PALLEWYRSLGL--NILEAYGMTE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  765 TTVCATMyevngeiqkeisNIP-------IGKPIANSEVfVISPfntlcpsgvVGELFIGGDGVANGYLNQKEKTEGAFi 837
Cdd:cd05932   311 NFAYSHL------------NYPgrdkigtVGNAGPGVEV-RISE---------DGEILVRSPALMMGYYKDPEATAEAF- 367

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728  838 sldksyNRDKKMYcTGDLVRLLANGNLEFIGR-KDNQVKIRGYRIELDEIEGTLFKHPEVRDAVV 901
Cdd:cd05932   368 ------TADGFLR-TGDKGELDADGNLTITGRvKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCV 425
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 609-959 4.50e-18

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 88.09  E-value: 4.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVV----NLSYSVINtfhLGKEDVFLQFATIIFDASIMEIFPILLCGGRmhLISEI 684
Cdd:cd17635     1 EDPLAVIFTSGTTGEPKAVLLANKTFFavpdILQKEGLN---WVVGDVTYLPLPATHIGGLWWILTCLIHGGL--CVTGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  685 EKRSAEEFINVSQKYGITNVVL-PTAFFKLIaDMPKEMLLKLNSVKRLFVGGETLPAESVRKWQskLGLKIPVLNAYGPT 763
Cdd:cd17635    76 ENTTYKSLFKILTTNAVTTTCLvPTLLSKLV-SELKSANATVPSLRLIGYGGSRAIAADVRFIE--ATGLTNTAQVYGLS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  764 ETT-VCATMYevnGEIQKEISNipIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFIsldks 842
Cdd:cd17635   153 ETGtALCLPT---DDDSIEINA--VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI----- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  843 ynrDKKMYcTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF-----TYQNDKIVCFYLSKD 917
Cdd:cd17635   223 ---DGWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYeisdeEFGELVGLAVVASAE 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 446581728  918 NTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDR 959
Cdd:cd17635   299 LDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 1556-2026 5.88e-18

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 90.13  E-value: 5.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1556 TESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRII 1635
Cdd:PRK08008   35 VRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1636 TSNKF----KSHLNVSDYKVSIIEdIYRTTINDDVKILN------------------KPDDLAYVIYTSGSTGKPKGTLL 1693
Cdd:PRK08008  115 TSAQFypmyRQIQQEDATPLRHIC-LTRVALPADDGVSSftqlkaqqpatlcyapplSTDDTAEILFTSGTTSRPKGVVI 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1694 THkgvLNLV------EWRNevfQISPNDK-VTQFYSHSFDSSVSEIFSTLLNGAELYLLsdeQRYSTVEYAQAIQETQAT 1766
Cdd:PRK08008  194 TH---YNLRfagyysAWQC---ALRDDDVyLTVMPAFHIDCQCTAAMAAFSAGATFVLL---EKYSARAFWGQVCKYRAT 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1767 ISD-LPTVFFNELSTSLTKLDSE-KIRSLRFIImggeAASTNAIRSWQNTFKnqVQLVNEYGPTEATVSamyyfipvleg 1844
Cdd:PRK08008  265 ITEcIPMMIRTLMVQPPSANDRQhCLREVMFYL----NLSDQEKDAFEERFG--VRLLTSYGMTETIVG----------- 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1845 ennLLGSVP--------IGIPISNTKVHILNSYMQYCPVGCMGELYIESL---GLAQGYWKQKEKTKQAFISNPFsedns 1913
Cdd:PRK08008  328 ---IIGDRPgdkrrwpsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGW----- 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1914 krLYrTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGMLLQAYYKTV---DGIGIE 1990
Cdd:PRK08008  400 --LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVvlnEGETLS 476

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 446581728 1991 KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:PRK08008  477 EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKII 512
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 1545-2025 6.33e-18

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 90.10  E-value: 6.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVaifLDRSMNSI---VSMLGILKAGAAYIPIDVKYPEDR 1621
Cdd:PRK07470   19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRI---LVHSRNCNqmfESMFAAFRLGAVWVPTNFRQTPDE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1622 INYIVRDSEACRIITSNKFKSHLNVS-------DYKVSI--------IEDIYRTTINDDVKILN-KPDDLAYVIYTSGST 1685
Cdd:PRK07470   96 VAYLAEASGARAMICHADFPEHAAAVraaspdlTHVVAIggaragldYEALVARHLGARVANAAvDHDDPCWFFFTSGTT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1686 GKPKGTLLTHkGVLNLVeWRNEVFQISPNdkVTQfyshsfdSSVSEIFSTLLNGAELYLLSDEQRYST----------VE 1755
Cdd:PRK07470  176 GRPKAAVLTH-GQMAFV-ITNHLADLMPG--TTE-------QDASLVVAPLSHGAGIHQLCQVARGAAtvllpserfdPA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1756 YAQAIQEtQATISDLPTVffnelsTSLTKL-------DSEKIRSLRFIIMGGeAASTNAIRSWQNTFKNQVqLVNEYGPT 1828
Cdd:PRK07470  245 EVWALVE-RHRVTNLFTV------PTILKMlvehpavDRYDHSSLRYVIYAG-APMYRADQKRALAKLGKV-LVQYFGLG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1829 EATVSamyyfIPVL--------EGENNLLGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTK 1900
Cdd:PRK07470  316 EVTGN-----ITVLppalhdaeDGPDARIGTC--GFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANA 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1901 QAFISNPFsednskrlyRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV------TQTEGG 1974
Cdd:PRK07470  389 KAFRDGWF---------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVlgvpdpVWGEVG 459

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446581728 1975 MllqAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK07470  460 V---AVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 1517-1936 6.75e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 90.49  E-value: 6.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1517 SLYKKVNHTERPYPyfQNIQEQFYMQVDRQPERIAIATAT------ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFL 1590
Cdd:PRK12582   35 SIVIKSRHPLGPYP--RSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1591 DRSMNSIVSMLGILKAGAAYIPIDVKY---PED--RINYIVrDSEACRII---TSNKFKSHLNVSDYK-VSII------- 1654
Cdd:PRK12582  113 GNSIEHALMTLAAMQAGVPAAPVSPAYslmSHDhaKLKHLF-DLVKPRVVfaqSGAPFARALAALDLLdVTVVhvtgpge 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1655 -------EDIYRTTINDDVKI----LNkPDDLAYVIYTSGSTGKPKGTLLTHK---GVLNLVEwrnEVFQISPNDKVTQF 1720
Cdd:PRK12582  192 giasiafADLAATPPTAAVAAaiaaIT-PDTVAKYLFTSGSTGMPKAVINTQRmmcANIAMQE---QLRPREPDPPPPVS 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1721 -----YSHSFDSSVseIFSTLL-NGAELYLlsDEQRYSTVEYAQAIQETQaTISdlPTVFFN------ELSTSLTKlDSE 1788
Cdd:PRK12582  268 ldwmpWNHTMGGNA--NFNGLLwGGGTLYI--DDGKPLPGMFEETIRNLR-EIS--PTVYGNvpagyaMLAEAMEK-DDA 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1789 KIRS----LRFIIMGGEAASTN--------AIRswqnTFKNQVQLVNEYGPTE-ATVSAMYYFIPVLEGEnnllgsvpIG 1855
Cdd:PRK12582  340 LRRSffknLRLMAYGGATLSDDlyermqalAVR----TTGHRIPFYTGYGATEtAPTTTGTHWDTERVGL--------IG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1856 IPISNTKVHILnsymqycPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWL----PNGNI 1931
Cdd:PRK12582  408 LPLPGVELKLA-------PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF--------YRLGDAARFVdpddPEKGL 472


                  ....*
gi 446581728 1932 EFMGR 1936
Cdd:PRK12582  473 IFDGR 477
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1108-1496 7.05e-18

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 88.51  E-value: 7.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1108 IEPSLNKDILQDTIRFLVERHEMLRTVFIE-RNGEPRQVILNsiaidliHDEIEHMSKKEQQEYIRTTINQtdhtPFDLe 1186
Cdd:cd19545    30 LPPDIDLARLQAAWEQVVQANPILRTRIVQsDSGGLLQVVVK-------ESPISWTESTSLDEYLEEDRAA----PMGL- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1187 KGPLFRIRIFNLNKKKSYLYINLHHIITDEWSVRNLLDELMKVYsafaKRRNPELPTISNRYVDYaeweqvqlnLGRWDT 1266
Cdd:cd19545    98 GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY----QGEPVPQPPPFSRFVKY---------LRQLDD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1267 EKS--YWMAELA-------APLPilnlpldfSRNRQSTNKGTvfemkLDNEMKESlkqVCEQENISMYMLFLAAYIQLLH 1337
Cdd:cd19545   165 EAAaeFWRSYLAgldpavfPPLP--------SSRYQPRPDAT-----LEHSISLP---SSASSGVTLATVLRAAWALVLS 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1338 YLTDQKDIIVGTPVVGRNH--QEFEKIQGFFVNTLAIRTQLNDVKNLTQLLQVVREKCLNSFQNQSYPFDKvIEQINPDR 1415
Cdd:cd19545   229 RYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQN-IRRLGPDA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1416 SfgNNPIFSTMFSYQKDILQQHDAYK-LQLLPNKQDISKFD---ISLAVEEGLDYVGISFEYDINLFKEESINR----FT 1487
Cdd:cd19545   308 R--AACNFQTLLVVQPALPSSTSESLeLGIEEESEDLEDFSsygLTLECQLSGSGLRVRARYDSSVISEEQVERlldqFE 385


                  ....*....
gi 446581728 1488 QNLLNILDA 1496
Cdd:cd19545   386 HVLQQLASA 394
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 1543-2027 7.68e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 89.94  E-value: 7.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRI 1622
Cdd:PRK07798   13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDEL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1623 NYIVRDSEACRIITSNKF------------KSHLNVS--------------DYkvsiiEDIYRTTINDDVKILNKPDDLa 1676
Cdd:PRK07798   93 RYLLDDSDAVALVYEREFaprvaevlprlpKLRTLVVvedgsgndllpgavDY-----EDALAAGSPERDFGERSPDDL- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1677 YVIYTSGSTGKPKGtllthkgvlnlVEWRNE-VFQISPN--DKVTQFYSHSFDSSVSEI--------------------- 1732
Cdd:PRK07798  167 YLLYTGGTTGMPKG-----------VMWRQEdIFRVLLGgrDFATGEPIEDEEELAKRAaagpgmrrfpapplmhgagqw 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1733 --FSTLLNGAELYLLSDeQRYSTVEYAQAIQETQATIsdLPTV---FFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNA 1807
Cdd:PRK07798  236 aaFAALFSGQTVVLLPD-VRFDADEVWRTIEREKVNV--ITIVgdaMARPLLDALEARGPYDLSSLFAIASGGALFSPSV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1808 IRSWQNTFKNqVQLVNEYGPTE------------ATVSAMYYFIP-----VLEGENNLL--GSVPIGIpisntkvhilns 1868
Cdd:PRK07798  313 KEALLELLPN-VVLTDSIGSSEtgfggsgtvakgAVHTGGPRFTIgprtvVLDEDGNPVepGSGEIGW------------ 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1869 ymqycpvgcmgelyieslgLAQ------GYWKQKEKTKQAFIsnpfsEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVK 1942
Cdd:PRK07798  380 -------------------IARrghiplGYYKDPEKTAETFP-----TIDGVRYAIPGDRARVEADGTITLLGRGSVCIN 435

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1943 IRGHRIELGEIEDAMLQLEGISQAVVTqteG------GMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLE 2016
Cdd:PRK07798  436 TGGEKVFPEEVEEALKAHPDVADALVV---GvpderwGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDE 512

                         570
                  ....*....|.
gi 446581728 2017 IPITANGKIDF 2027
Cdd:PRK07798  513 VQRSPAGKADY 523
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 487-962 1.01e-17

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 89.37  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  487 AISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSE 566
Cdd:PRK12406    4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  567 SQMIITKKE-YRGLVERFAIHTIYLEdfhyANSIENIASTHTIEDA-----------------------------AYIIY 616
Cdd:PRK12406   84 ARVLIAHADlLHGLASALPAGVTVLS----VPTPPEIAAAYRISPAlltppagaidwegwlaqqepydgppvpqpQSMIY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  617 TSGSTGLPKGV----VVPHKG-----VVNLSYSVINT---------FHLGKEDVFLQFATIifdasimeifpillcGGRM 678
Cdd:PRK12406  160 TSGTTGHPKGVrraaPTPEQAaaaeqMRALIYGLKPGiralltgplYHSAPNAYGLRAGRL---------------GGVL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  679 HLISEIEkrsAEEFINVSQKYGITNV-VLPTAFFKLIaDMPKEMLLK--LNSVKRLFVGGETLPAESVRKWQSKLGlkiP 755
Cdd:PRK12406  225 VLQPRFD---PEELLQLIERHRITHMhMVPTMFIRLL-KLPEEVRAKydVSSLRHVIHAAAPCPADVKRAMIEWWG---P 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  756 VLNA-YGPTETTVcatmyeVNGEIQKEISNIP--IGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVAN-GYLNQKEK 831
Cdd:PRK12406  298 VIYEyYGSTESGA------VTFATSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEK 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  832 ----TEGAFISLdksynrdkkmyctGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND 907
Cdd:PRK12406  372 raeiDRGGFITS-------------GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDA 438

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  908 KI---VCFYLSKD-NTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK12406  439 EFgeaLMAVVEPQpGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 1559-1937 1.03e-17

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 89.58  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLLEKGIKR--GDKVAIFldrSMNS---IVSMLGILKAGAAYIPI-DVKYPEDrINYIVRDSEAC 1632
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGKPapASFVGIY---SINRpewIISELACYAYSLVTVPLyDTLGPEA-IEYILNHAEIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1633 RIITSNKFKShlnvsdYKVSIIEDIYRTTINDDVKilNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLV----EWRNEV 1708
Cdd:cd05927    82 IVFCDAGVKV------YSLEEFEKLGKKNKVPPPP--PKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEIL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1709 FQISPNDKVTQF--YSHSFDSSVseIFSTLLNGAELYLLSDEQRYsTVEYAQAIQET----------------QATISDL 1770
Cdd:cd05927   154 NKINPTDVYISYlpLAHIFERVV--EALFLYHGAKIGFYSGDIRL-LLDDIKALKPTvfpgvprvlnriydkiFNKVQAK 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1771 PTV---FFN---------------ELSTSLTKLDSEKIRSL-----RFIIMGGEAASTNAIRSWQNTFKnqVQLVNEYGP 1827
Cdd:cd05927   231 GPLkrkLFNfalnyklaelrsgvvRASPFWDKLVFNKIKQAlggnvRLMLTGSAPLSPEVLEFLRVALG--CPVLEGYGQ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1828 TE----ATVSamyyfipvLEGENNlLGSVpiGIPISNTKVHILN-SYMQYCPVGC--MGELYIESLGLAQGYWKQKEKTK 1900
Cdd:cd05927   309 TEctagATLT--------LPGDTS-VGHV--GGPLPCAEVKLVDvPEMNYDAKDPnpRGEVCIRGPNVFSGYYKDPEKTA 377

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 446581728 1901 QAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRK 1937
Cdd:cd05927   378 EALDEDGW--------LHTGDIGEWLPNGTLKIIDRK 406
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 519-962 1.36e-17

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 89.10  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  519 GQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKKEyrgLVERFA-IHT---------I 588
Cdd:PRK06334   67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQ---LMQHLAqTHGedaeypfslI 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  589 YLED--------------------FHYANSIENIASTHTiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLG 648
Cdd:PRK06334  144 YMEEvrkelsfwekcrigiymsipFEWLMRWFGVSDKDP-EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  649 KEDVFLQFATiIFDA---SIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQK--YGITNVvlptaFFKLIADMPKEMLL 723
Cdd:PRK06334  223 EDDVMMSFLP-PFHAygfNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVtfLGSTPV-----FFDYILKTAKKQES 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  724 KLNSVKRLFVGGETLpAESVRKWQSKLGLKIPVLNAYGPTEttvCATMYEVNGEIQKEISNIpIGKPIANSEVFVISPfN 803
Cdd:PRK06334  297 CLPSLRFVVIGGDAF-KDSLYQEALKTFPHIQLRQGYGTTE---CSPVITINTVNSPKHESC-VGMPIRGMDVLIVSE-E 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  804 TLCP--SGVVGELFIGGDGVANGYLNQKEKTegAFISLDksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRI 881
Cdd:PRK06334  371 TKVPvsSGETGLVLTRGTSLFSGYLGEDFGQ--GFVELG-----GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMV 443

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  882 ELDEIEGTLFKH---PEVRDA---VVFTYQNDKI-VCFY--LSKDNTELkQEALKTFLSESLpdfMMPNYIFHLESFPVS 952
Cdd:PRK06334  444 SLEALESILMEGfgqNAADHAgplVVCGLPGEKVrLCLFttFPTSISEV-NDILKNSKTSSI---LKISYHHQVESIPML 519

                         490
                  ....*....|
gi 446581728  953 PSGKLDRKKL 962
Cdd:PRK06334  520 GTGKPDYCSL 529
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 475-962 1.93e-17

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 88.84  E-value: 1.93e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   475 IDLQALKSPNQIAI-----SMGDQ-SITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVP 548
Cdd:TIGR02188   63 VDRHLEARPDKVAIiwegdEPGEVrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSV 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   549 IDPKF-PEKRIEYILkDSESQMIITKKE-YRG-------------------------LVERFAIHTIYL---EDFHYANS 598
Cdd:TIGR02188  143 VFGGFsAEALADRIN-DAGAKLVITADEgLRGgkviplkaivdealekcpvsvehvlVVRRTGNPVVPWvegRDVWWHDL 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   599 IENIASTHTI-----EDAAYIIYTSGSTGLPKGVVVPHKG-VVNLSYSVINTFHLGKEDVFLQFATI--IFDASIMEIFP 670
Cdd:TIGR02188  222 MAKASAYCEPepmdsEDPLFILYTSGSTGKPKGVLHTTGGyLLYAAMTMKYVFDIKDGDIFWCTADVgwITGHSYIVYGP 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   671 ilLCGGRMHLISEiekrSAEEFINVS------QKYGITNV-VLPTA---FFKLIADMPKEMllKLNSVKRLFVGGETLPA 740
Cdd:TIGR02188  302 --LANGATTVMFE----GVPTYPDPGrfweiiEKHKVTIFyTAPTAiraLMRLGDEWVKKH--DLSSLRLLGSVGEPINP 373

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   741 ESVRKWQSKLGL-KIPVLNAYGPTETtvcatmyevnGEIQkeISNIPIGKPI----ANSEVFVISPF------NTLCPSG 809
Cdd:TIGR02188  374 EAWMWYYKVVGKeRCPIVDTWWQTET----------GGIM--ITPLPGATPTkpgsATLPFFGIEPAvvdeegNPVEGPG 441

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   810 VVGELFIGGD--GVANGYLNQKEKtegaFIsldKSY-NRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEI 886
Cdd:TIGR02188  442 EGGYLVIKQPwpGMLRTIYGDHER----FV---DTYfSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEI 514

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   887 EGTLFKHPEVRDAVVFTYQND----KIVCFYLSKD----NTELKQEaLKTFLSESLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:TIGR02188  515 ESALVSHPAVAEAAVVGIPDDikgqAIYAFVTLKDgyepDDELRKE-LRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIM 593


                   ....
gi 446581728   959 RKKL 962
Cdd:TIGR02188  594 RRLL 597
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 479-960 2.14e-17

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 88.17  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRI 558
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  559 EYILKDSESQMIITKKEYRGLVERFAI------HTIYLEDFHYANSIENIASTHT---IEDAA-------YIIYTSGSTG 622
Cdd:PRK07470   97 AYLAEASGARAMICHADFPEHAAAVRAaspdltHVVAIGGARAGLDYEALVARHLgarVANAAvdhddpcWFFFTSGTTG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  623 LPKGVVVPHKgvvNLSYSVINtfHLGkeDVFLqfATIIFDASIMeIFPiLLCGGRMHLISEI-----------EKRSAEE 691
Cdd:PRK07470  177 RPKAAVLTHG---QMAFVITN--HLA--DLMP--GTTEQDASLV-VAP-LSHGAGIHQLCQVargaatvllpsERFDPAE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  692 FINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlkiPVLNAY-GPTETTVCAT 770
Cdd:PRK07470  246 VWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLG---KVLVQYfGLGEVTGNIT 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  771 -----MYEVNGEIQKEISniPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynR 845
Cdd:PRK07470  323 vlppaLHDAEDGPDARIG--TCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF--------R 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  846 DKkMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK------IVCfyLSKDNT 919
Cdd:PRK07470  393 DG-WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwgevgvAVC--VARDGA 469

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 446581728  920 ELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRK 960
Cdd:PRK07470  470 PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 1674-2026 5.34e-17

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 84.69  E-value: 5.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1674 DLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDkvtqfysHSFDSS-------VSEIFSTLLNGAELYLLs 1746
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD-------SWLLSLplyhvggLAILVRSLLAGAELVLL- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1747 deqrystvEYAQAIQETQAT-----ISDLPTvffnELSTSLT-KLDSEKIRSLRFIIMGG--------EAASTNAIRSWQ 1812
Cdd:cd17630    73 --------ERNQALAEDLAPpgvthVSLVPT----QLQRLLDsGQGPAALKSLRAVLLGGapippellERAADRGIPLYT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1813 NtfknqvqlvneYGPTEaTVSAMYYFIPVLEGennlLGSVpiGIPISNTKVHILNSymqycpvgcmGELYIESLGLAQGY 1892
Cdd:cd17630   141 T-----------YGMTE-TASQVATKRPDGFG----RGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGY 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1893 WKqkektkqAFISNPFSEDNskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT--- 1969
Cdd:cd17630   193 LR-------GQLVPEFNEDG---WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgvp 262

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728 1970 QTEGGMLLQAYYKTvdGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:cd17630   263 DEELGQRPVAVIVG--RGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVD 317
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 41-335 7.80e-17

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 85.83  E-value: 7.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   41 IIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRD-EKIKQLIQKNVEFDIPIKDLTAFKNTEQKSILKNFLESIVNEKF 119
Cdd:cd19547    29 VLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWALLDWSGEDPDRRAELLERLLADDRAAGL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  120 SLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKS-NVEFESPYKNLVKHEESfiDSAIY 198
Cdd:cd19547   109 SLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREpQLSPCRPYRDYVRWIRA--RTAQS 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  199 KEGSSYWKDYLQgELTPTEF---PIDfnkmNEKRYtdKNISKNINSDLFYQIQCFAKKNNISIYRVMLSTYCTLLHQMTN 275
Cdd:cd19547   187 EESERFWREYLR-DLTPSPFstaPAD----REGEF--DTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTG 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728  276 AEEIIVGIPINTRPYTEE--RNTFGYFVNTLPIRITIEKGETFKGILNKVNKSihLAITYKH 335
Cdd:cd19547   260 ARDVVHGLTIAGRPPELEgsEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRD--LATTAAH 319
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 470-965 8.22e-17

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 86.73  E-value: 8.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  470 TLDQLIDLQALKSPNQIAISmgdQSI-------TYYELQQRSNQIVNYLRENDLKKGQRVSiTM----EREIDTIVWILG 538
Cdd:PRK06018   11 LCHRIIDHAARIHGNREVVT---RSVegpivrtTYAQIHDRALKVSQALDRDGIKLGDRVA-TIawntWRHLEAWYGIMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  539 IlksGGVYVPIDPK-FPEKrIEYILKDSESQMIITKKEYRGLVERFAIH-------TIYLEDFHY-ANSIEN-IASTHTI 608
Cdd:PRK06018   87 I---GAICHTVNPRlFPEQ-IAWIINHAEDRVVITDLTFVPILEKIADKlpsveryVVLTDAAHMpQTTLKNaVAYEEWI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 ED--------------AAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLG--KEDVFLQFAT--------IIFDAS 664
Cdd:PRK06018  163 AEadgdfawktfdentAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDALGtsAADTMLPVVPlfhanswgIAFSAP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  665 IMEIfPILLCGGRMHLISEIEKRSAEefinvsqKYGITNVVlPTAFFKLIADMPKEMlLKLNSVKRLFVGGETLPAESVR 744
Cdd:PRK06018  243 SMGT-KLVMPGAKLDGASVYELLDTE-------KVTFTAGV-PTVWLMLLQYMEKEG-LKLPHLKMVVCGGSAMPRSMIK 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  745 KWQSklgLKIPVLNAYGPTETTVCATMyevnGEIQKEISNIPI----------GKPIANSEVFVISPFNTLCPSG--VVG 812
Cdd:PRK06018  313 AFED---MGVEVRHAWGMTEMSPLGTL----AALKPPFSKLPGdarldvlqkqGYPPFGVEMKITDDAGKELPWDgkTFG 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  813 ELFIGGDGVANGYLnqkeKTEGAFisLDksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFK 892
Cdd:PRK06018  386 RLKVRGPAVAAAYY----RVDGEI--LD-----DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVG 454

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581728  893 HPEVRDAVVFTYQNDK-----IVCFYLSKDNTELKQEALKtFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQ 965
Cdd:PRK06018  455 HPKVAEAAVIGVYHPKwderpLLIVQLKPGETATREEILK-YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1543-2038 9.01e-17

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 86.48  E-value: 9.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIATATE--SLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPE- 1619
Cdd:PRK05852   26 ATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIa 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1620 ----------------DRINYIVRDSEACRI------ITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKilnkPDDlAY 1677
Cdd:PRK05852  106 eqrvrsqaagarvvliDADGPHDRAEPTTRWwpltvnVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLR----PDD-AM 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1678 VIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQ----FYSHSFdssVSEIFSTLLNGAELyLLSDEQRYST 1753
Cdd:PRK05852  181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAvmplYHGHGL---IAALLATLASGGAV-LLPARGRFSA 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1754 VEYAQAIQETQAT-ISDLPTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVqlVNEYGPTEATV 1832
Cdd:PRK05852  257 HTFWDDIKAVGATwYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPV--VCAFGMTEATH 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1833 SAMYYFIP-VLEGENNLLGSVPIGIPiSNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsed 1911
Cdd:PRK05852  335 QVTTTQIEgIGQTENPVVSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--- 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1912 nskrlyRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTqtegGMLLQAYYKTV------- 1984
Cdd:PRK05852  411 ------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVF----GVPDQLYGEAVaavivpr 480

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446581728 1985 DGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDfEKLPKIEFGHE 2038
Cdd:PRK05852  481 ESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLD-RRAVAEQFGHS 533
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 1558-2030 1.39e-16

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 85.64  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQHLLEKGikrGDKVAIFLDRSMNSIVSMLGILKAGAayIPIDVKYPEDrinyiVRDSEAC----- 1632
Cdd:PRK06334   45 KLSYNQVRKAVIALATKVSKYP---DQHIGIMMPASAGAYIAYFATLLSGK--IPVMINWSQG-----LREVTACanlvg 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1633 --RIITSNKFKSHL-----NVSDYKVSIIediYRTTINDDVKILNK------------------------PDDLAYVIYT 1681
Cdd:PRK06334  115 vtHVLTSKQLMQHLaqthgEDAEYPFSLI---YMEEVRKELSFWEKcrigiymsipfewlmrwfgvsdkdPEDVAVILFT 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1682 SGSTGKPKGTLLTHKgvlNLVEWRNEVFQ-ISPNDK------VTQFYSHSFDSSVseIFSTLLNGAELYLLSDEQRYSTV 1754
Cdd:PRK06334  192 SGTEKLPKGVPLTHA---NLLANQRACLKfFSPKEDdvmmsfLPPFHAYGFNSCT--LFPLLSGVPVVFAYNPLYPKKIV 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1755 EYaqaIQETQATISDLPTVFFNELSTSLTKLDSeKIRSLRFIIMGGEAASTNAIRSWQNTFKnQVQLVNEYGPTEATvsa 1834
Cdd:PRK06334  267 EM---IDEAKVTFLGSTPVFFDYILKTAKKQES-CLPSLRFVVIGGDAFKDSLYQEALKTFP-HIQLRQGYGTTECS--- 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1835 myyfiPVL--EGENNLLGSVPIGIPISNTKVHILnSYMQYCPV--GCMGELYIESLGLAQGYWKQKEktKQAFIsnpfsE 1910
Cdd:PRK06334  339 -----PVItiNTVNSPKHESCVGMPIRGMDVLIV-SEETKVPVssGETGLVLTRGTSLFSGYLGEDF--GQGFV-----E 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1911 DNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDamLQLEGISQavvTQTEGGMLLqayykTVDGIGIE 1990
Cdd:PRK06334  406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALES--ILMEGFGQ---NAADHAGPL-----VVCGLPGE 475

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446581728 1991 KNKLAIH-------------LSNVLPEYMVPKYYSHVLE-IPITANGKIDFEKL 2030
Cdd:PRK06334  476 KVRLCLFttfptsisevndiLKNSKTSSILKISYHHQVEsIPMLGTGKPDYCSL 529
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 2164-2359 1.53e-16

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 83.10  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2164 VFLTGATGYLGAHILERLLQlPSTTIYCLVRENEDqviGAKLKErmefyfgkeilqklkERVELIEGDLslmnlgLDSKQ 2243
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLA-QGYRVRALVRSGSD---AVLLDG---------------LPVEVVEGDL------TDAAS 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2244 LDHLKKNVESIIHCGGEVR-HYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGqaERDPKEFEffESDFDRG 2321
Cdd:cd05228    56 LAAAMKGCDRVFHLAAFTSlWAKDRKELYRTNVEGTRNVLDAALEAGVrRVVHTSSIAALG--GPPDGRID--ETTPWNE 131

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 446581728 2322 QNLDNLYLESKFQGEKMVREAMEKGVRATIYRVGNLVG 2359
Cdd:cd05228   132 RPFPNDYYRSKLLAELEVLEAAAEGLDVVIVNPSAVFG 169
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 1545-1968 2.21e-16

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 84.54  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIfldRSMNSIVSMLGILKA---GAAYIPIDVKYPEDR 1621
Cdd:PRK09029   15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVAL---RGKNSPETLLAYLALlqcGARVLPLNPQLPQPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1622 INYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINddvkilnkPDDLAYVIYTSGSTGKPKGTLLTH------ 1695
Cdd:PRK09029   92 LEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQ--------PQRLATMTLTSGSTGLPKAAVHTAqahlas 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1696 -KGVLNLvewrnevFQISPNDkvTQFYS----HsfdssVSE---IFSTLLNGAELYLLSDEQRYstveyaQAIQE-TQAt 1766
Cdd:PRK09029  164 aEGVLSL-------MPFTAQD--SWLLSlplfH-----VSGqgiVWRWLYAGATLVVRDKQPLE------QALAGcTHA- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1767 iSDLPtvffnelsTSLTKLDSEKIR--SLRFIIMGG--------EAASTNAIRSWQNtfknqvqlvneYGPTEA--TVSA 1834
Cdd:PRK09029  223 -SLVP--------TQLWRLLDNRSEplSLKAVLLGGaaipveltEQAEQQGIRCWCG-----------YGLTEMasTVCA 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1835 MYYfipvlEGENNllgsvpIGIPISNTKVHILNsymqycpvgcmGELYIESLGLAQGYWKQKEKTkqafisnPFSedNSK 1914
Cdd:PRK09029  283 KRA-----DGLAG------VGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLV--NDE 331

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446581728 1915 RLYRTGDLVRWLpNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV 1968
Cdd:PRK09029  332 GWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFV 384
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 1528-2033 3.39e-16

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 84.50  E-value: 3.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1528 PYPYF----QNIQEQFYMQVDRQ---PERIAI--ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIV 1598
Cdd:cd17642     5 PGPFYpledGTAGEQLHKAMKRYasvPGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1599 SMLGILKAGAAYIPIDVKYPEDRINYIVRDSEAcRIITSNK--FKSHLNVSDyKVSIIEDIYRTTINDDVKIL------- 1669
Cdd:cd17642    85 PVIAGLFIGVGVAPTNDIYNERELDHSLNISKP-TIVFCSKkgLQKVLNVQK-KLKIIKTIIILDSKEDYKGYqclytfi 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1670 ------------------NKPDDLAYVIYTSGSTGKPKGTLLTHKGVL-NLVEWRNEVFQISPNDKVTQF----YSHSFd 1726
Cdd:cd17642   163 tqnlppgfneydfkppsfDRDEQVALIMNSSGSTGLPKGVQLTHKNIVaRFSHARDPIFGNQIIPDTAILtvipFHHGF- 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1727 sSVSEIFSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATISDL-PT--VFFNElSTSLTKLDsekIRSLRFIIMGGEAA 1803
Cdd:cd17642   242 -GMFTTLGYLICGFRVVLMY---KFEEELFLRSLQDYKVQSALLvPTlfAFFAK-STLVDKYD---LSNLHEIASGGAPL 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1804 STNAIRSWQNTFKnqVQLVNE-YGPTEATVSamyyfIPVLEGENNLLGSVPIGIPISNTKVHILNSyMQYCPVGCMGELY 1882
Cdd:cd17642   314 SKEVGEAVAKRFK--LPGIRQgYGLTETTSA-----ILITPEGDDKPGAVGKVVPFFYAKVVDLDT-GKTLGPNERGELC 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1883 IESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEG 1962
Cdd:cd17642   386 VKGPMIMKGYVNNPEATKALIDKDGW--------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPK 457

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1963 ISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNKLAIHL-SNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKI 2033
Cdd:cd17642   458 IFDAGVAgipDEDAGELPAAVVVLEAGKTMTEKEVMDYVaSQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 1560-2016 3.82e-16

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 84.08  E-value: 3.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1560 TYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGaaYIPIDVKYPEDrinyivrdseacriitsnk 1639
Cdd:cd05908    17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGG--MIAVPVSIGSN------------------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1640 fkshlnvSDYKVSIIEdIYRTTIN-----DDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKG-VLNLVEWRNEVfQISP 1713
Cdd:cd05908    76 -------EEHKLKLNK-VWNTLKNpylitEEEVLCELADELAFIQFSSGSTGDPKGVMLTHENlVHNMFAILNST-EWKT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1714 NDKVTQFYSHSFDSS-VSEIFSTLLNGAELYLLSDEQ--RYSTVeYAQAIQETQATISDLPTVFFNELSTSL--TKLDSE 1788
Cdd:cd05908   147 KDRILSWMPLTHDMGlIAFHLAPLIAGMNQYLMPTRLfiRRPIL-WLKKASEHKATIVSSPNFGYKYFLKTLkpEKANDW 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1789 KIRSLRFIIMGGEAASTNAIRSWQNTFK----NQVQLVNEYGPTEATVSAMY------YFIPVLEGENNLLGS------- 1851
Cdd:cd05908   226 DLSSIRMILNGAEPIDYELCHEFLDHMSkyglKRNAILPVYGLAEASVGASLpkaqspFKTITLGRRHVTHGEpepevdk 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1852 --------VPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAfisnpFSEDNskrLYRTGDLv 1923
Cdd:cd05908   306 kdsecltfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKV-----FTDDG---WLKTGDL- 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1924 RWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV---------TQTEGGMLLQAYYKTVDGIGIEKNKL 1994
Cdd:cd05908   377 GFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVvacgvnnsnTRNEEIFCFIEHRKSEDDFYPLGKKI 456

                         490       500       510
                  ....*....|....*....|....*....|
gi 446581728 1995 AIHL--------SNVLPEYMVPKYYSHVLE 2016
Cdd:cd05908   457 KKHLnkrggwqiNEVLPIRRIPKTTSGKVK 486
PRK13382 PRK13382
bile acid CoA ligase;
1545-2031 4.53e-16

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 84.04  E-value: 4.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK13382   55 RCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSNKFKSHLN---------------VSDYKVSIIEDIYRTTINDdvKILNKPDDLAYVIYTSGSTGKPK 1689
Cdd:PRK13382  135 VVTREGVDTVIYDEEFSATVDraladcpqatrivawTDEDHDLTVEVLIAAHAGQ--RPEPTGRKGRVILLTSGTTGTPK 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1690 GT-------LLTHKGVLNLVEWRNE--VFQISPndkvtQFysHSFDssvseiFSTLLNGAELYLLSDEQRYSTVEYA-QA 1759
Cdd:PRK13382  213 GArrsgpggIGTLKAILDRTPWRAEepTVIVAP-----MF--HAWG------FSQLVLAASLACTIVTRRRFDPEATlDL 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1760 IQETQAT-ISDLPTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQvqLVNEYGPTEATVSAMYyf 1838
Cdd:PRK13382  280 IDRHRATgLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV--IYNNYNATEAGMIATA-- 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1839 IPV-LEGENNLLGSVPIGipisnTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEK-TKQAFISnpfsednskrl 1916
Cdd:PRK13382  356 TPAdLRAAPDTAGRPAEG-----TEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKdFHDGFMA----------- 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1917 yrTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNK 1993
Cdd:PRK13382  420 --SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIgvdDEQYGQRLAAFVVLKPGASATPET 497

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 446581728 1994 LAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLP 2031
Cdd:PRK13382  498 LKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 1533-2030 4.77e-16

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 84.04  E-value: 4.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1533 QNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAayIP 1612
Cdd:COG1021    25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IP 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1613 IDVkYPEDR---INYIVRDSEACRIITS---NKFkshlnvsDY--------------KVSII----------EDIYRTTI 1662
Cdd:COG1021   103 VFA-LPAHRraeISHFAEQSEAVAYIIPdrhRGF-------DYralarelqaevpslRHVLVvgdageftslDALLAAPA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1663 nDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKvtqfY------SHSFDSSVSEIFSTL 1736
Cdd:COG1021   175 -DLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTV----YlaalpaAHNFPLSSPGVLGVL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1737 LNGAELYLLSDEQRYSTVEyaqAIQETQATISDL-PTVffneLSTSLTKLDSEK--IRSLRFIIMGGEAASTNAIRSWQN 1813
Cdd:COG1021   250 YAGGTVVLAPDPSPDTAFP---LIERERVTVTALvPPL----ALLWLDAAERSRydLSSLRVLQVGGAKLSPELARRVRP 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1814 TFKNQVQ--------LVNeY----GPTEATVSAmyyfipvlegennllgsvpIGIPIS-NTKVHILNSYMQYCPVGCMGE 1880
Cdd:COG1021   323 ALGCTLQqvfgmaegLVN-YtrldDPEEVILTT-------------------QGRPISpDDEVRIVDEDGNPVPPGEVGE 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1881 LYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRkDKQVKIR-GHRIELGEIEDAMLQ 1959
Cdd:COG1021   383 LLTRGPYTIRGYYRAPEHNARAFTPDGF--------YRTGDLVRRTPDGYLVVEGR-AKDQINRgGEKIAAEEVENLLLA 453

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728 1960 LEGISQAVVTqtegGM---LLQ----AYYkTVDGIGIEKNKLAIHLSNV-LPEYMVPKYYSHVLEIPITANGKIDFEKL 2030
Cdd:COG1021   454 HPAVHDAAVV----AMpdeYLGerscAFV-VPRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 495-902 5.74e-16

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 83.80  E-value: 5.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  495 ITYYELQQRSNQIVNYLRE--NDLKKGQRVSITMereIDTIVWIL---GILKSGGVYVPI-DPKFPEKrIEYILKDSESQ 568
Cdd:cd05927     6 ISYKEVAERADNIGSALRSlgGKPAPASFVGIYS---INRPEWIIselACYAYSLVTVPLyDTLGPEA-IEYILNHAEIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  569 MIITKKEyrglVERFAIhtIYLEDFHYANSIENIASTHtiEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFH-- 646
Cdd:cd05927    82 IVFCDAG----VKVYSL--EEFEKLGKKNKVPPPPPKP--EDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEil 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  647 --LGKEDVFLQF-------------------ATI-IFDASIMEIF-------PILLCG-----GRMH--LISEIEKRS-- 688
Cdd:cd05927   154 nkINPTDVYISYlplahifervvealflyhgAKIgFYSGDIRLLLddikalkPTVFPGvprvlNRIYdkIFNKVQAKGpl 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  689 AEEFINVSQKYGITN----VVLPTAFF-KLIADMPKEMLLklNSVKRLFVGGETLPAESVRKWQSKLGlkIPVLNAYGPT 763
Cdd:cd05927   234 KRKLFNFALNYKLAElrsgVVRASPFWdKLVFNKIKQALG--GNVRLMLTGSAPLSPEVLEFLRVALG--CPVLEGYGQT 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  764 ETTVCATMYEvngeiQKEISNIPIGKPIANSEVFVIS-P----FNTLCPSGvvGELFIGGDGVANGYLNQKEKTEGAFis 838
Cdd:cd05927   310 ECTAGATLTL-----PGDTSVGHVGGPLPCAEVKLVDvPemnyDAKDPNPR--GEVCIRGPNVFSGYYKDPEKTAEAL-- 380

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  839 ldksynrDKK-MYCTGDLVRLLANGNLEFIGRKDNQVKI-RGYRIELDEIEGTLFKHPEVRDAVVF 902
Cdd:cd05927   381 -------DEDgWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVY 439
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 1547-1938 8.46e-16

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 83.00  E-value: 8.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIAT-ATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYI 1625
Cdd:PRK07514   16 RDAPFIETpDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1626 VRDSEACRIITSNKFKSHLN--VSDYKVSIIEdiyrtTINDD----------------VKILNKPDDLAYVIYTSGSTGK 1687
Cdd:PRK07514   96 IGDAEPALVVCDPANFAWLSkiAAAAGAPHVE-----TLDADgtgslleaaaaapddfETVPRGADDLAAILYTSGTTGR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1688 PKGTLLTHKGVLN----LVE-WRnevfqISPNDKVTQ----FYSHS-FdssVSeIFSTLLNGAELYLLsdeqrySTVEYA 1757
Cdd:PRK07514  171 SKGAMLSHGNLLSnaltLVDyWR-----FTPDDVLIHalpiFHTHGlF---VA-TNVALLAGASMIFL------PKFDPD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1758 QAIQET-QAT-ISDLPTvFFNELSTSlTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNtfKNQVQLVNEYGPTEAtvsAM 1835
Cdd:PRK07514  236 AVLALMpRATvMMGVPT-FYTRLLQE-PRLTREAAAHMRLFISGSAPLLAETHREFQE--RTGHAILERYGMTET---NM 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1836 YYFIPvLEGEnNLLGSVpiGIPISNTKVHILNSYM-QYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednsk 1914
Cdd:PRK07514  309 NTSNP-YDGE-RRAGTV--GFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------ 378

                         410       420
                  ....*....|....*....|....*
gi 446581728 1915 rlYRTGDLVRWLPNGNIEFMGR-KD 1938
Cdd:PRK07514  379 --FITGDLGKIDERGYVHIVGRgKD 401
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 2164-2359 9.94e-16

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 78.88  E-value: 9.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2164 VFLTGATGYLGAHILERLLQLPSTtiyclvrenedqVIG-AKLKERMEFyfgkeilqKLKERVELIEGDLslmnlgLDSK 2242
Cdd:pfam01370    1 ILVTGATGFIGSHLVRRLLEKGYE------------VIGlDRLTSASNT--------ARLADLRFVEGDL------TDRD 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2243 QLDHLKKNVES--IIHCGGE--VRHYGER-EHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKEfeffES 2316
Cdd:pfam01370   55 ALEKLLADVRPdaVIHLAAVggVGASIEDpEDFIEANVLGTLNLLEAARKAGVkRFLFASSSEVYGDGAEIPQE----ET 130

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 446581728  2317 DFDRGQNLDNLYLESKFQGEKMVREAMEK-GVRATIYRVGNLVG 2359
Cdd:pfam01370  131 TLTGPLAPNSPYAAAKLAGEWLVLAYAAAyGLRAVILRLFNVYG 174
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1555-2025 1.15e-15

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 83.54  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1555 ATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRI 1634
Cdd:PRK06060   27 AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1635 ITS----NKFKSHlNVSDyKVSIIEDIYRTTiNDDVKILNKpDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWR-NEVF 1709
Cdd:PRK06060  107 VTSdalrDRFQPS-RVAE-AAELMSEAARVA-PGGYEPMGG-DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKAL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1710 QISPND----KVTQFYSHSFDSSV--------SEIFSTLLNGAELYLLSDEQRYSTVEYAqaiqetqatisdLPTVFfne 1777
Cdd:PRK06060  183 RLTPEDtglcSARMYFAYGLGNSVwfplatggSAVINSAPVTPEAAAILSARFGPSVLYG------------VPNFF--- 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1778 lSTSLTKLDSEKIRSLRFIIMGGEAASTnAIRSWQNTFKNQVQLVNEYGPTEatVSAMYYFIPVLEGENNLLGSVpigip 1857
Cdd:PRK06060  248 -ARVIDSCSPDSFRSLRCVVSAGEALEL-GLAERLMEFFGGIPILDGIGSTE--VGQTFVSNRVDEWRLGTLGRV----- 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1858 ISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEktkqafisnPFSEDNSkrLYRTGDLVRWLPNGNIEFMGRK 1937
Cdd:PRK06060  319 LPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEG--WLDTRDRVCIDSDGWVTYRCRA 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1938 DKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIGIEKNKLA-IH--LSNVLPEYMVPKYY 2011
Cdd:PRK06060  388 DDTEVIGGVNVDPREVERLIIEDEAVAEAAVVavrESTGASTLQAFLVATSGATIDGSVMRdLHrgLLNRLSAFKVPHRF 467

                         490
                  ....*....|....
gi 446581728 2012 SHVLEIPITANGKI 2025
Cdd:PRK06060  468 AVVDRLPRTPNGKL 481
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 1543-1968 1.60e-15

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 82.61  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQ----PERIAI------ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIP 1612
Cdd:cd05966    59 LDRHlkerGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1613 IDVKY-PE---DRINyivrDSEACRIITSNKFK----------------------------SHLNVsdyKVSIIEDiyRT 1660
Cdd:cd05966   139 VFAGFsAEslaDRIN----DAQCKLVITADGGYrggkviplkeivdealekcpsvekvlvvKRTGG---EVPMTEG--RD 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1661 TINDDVKILNKPD---------DLAYVIYTSGSTGKPKGTLLTHKGVLNLV----EWrneVFQISPNDK---------VT 1718
Cdd:cd05966   210 LWWHDLMAKQSPEcepewmdseDPLFILYTSGSTGKPKGVVHTTGGYLLYAattfKY---VFDYHPDDIywctadigwIT 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1719 qfySHSFdssvsEIFSTLLNGAELYLLSDEQRYSTVE-YAQAIQETQATIsdL---PTVFfnelsTSLTKLDSEKIR--- 1791
Cdd:cd05966   287 ---GHSY-----IVYGPLANGATTVMFEGTPTYPDPGrYWDIVEKHKVTI--FytaPTAI-----RALMKFGDEWVKkhd 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1792 --SLRfiIMG--GEAASTNAIRsWQNTF--KNQVQLVNEYGPTEaTVSAMYYFIPvlegennllGSVPIGiPISNT---- 1861
Cdd:cd05966   352 lsSLR--VLGsvGEPINPEAWM-WYYEVigKERCPIVDTWWQTE-TGGIMITPLP---------GATPLK-PGSATrpff 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1862 --KVHILNSYMQYCPVGCMGELYIESL--GLAQGYWKQKEKTKQAFISnPFsednsKRLYRTGDLVRWLPNGNIEFMGRK 1937
Cdd:cd05966   418 giEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHERYEDTYFS-KF-----PGYYFTGDGARRDEDGYYWITGRV 491

                         490       500       510
                  ....*....|....*....|....*....|.
gi 446581728 1938 DKQVKIRGHRIELGEIEDAMLQLEGISQAVV 1968
Cdd:cd05966   492 DDVINVSGHRLGTAEVESALVAHPAVAEAAV 522
PRK05857 PRK05857
fatty acid--CoA ligase;
1535-2025 1.87e-15

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 82.36  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1535 IQEQFYMQVDRQPERIAI--ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIP 1612
Cdd:PRK05857   16 VLDRVFEQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1613 IDVKYPE---DRINYIVRDS-----EACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNK-----PDDLAYVI 1679
Cdd:PRK05857   96 ADGNLPIaaiERFCQITDPAaalvaPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGnadqgSEDPLAMI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1680 YTSGSTGKPKGTLLTHKGV-----------LNLVEWRNEVFQISPndkvtqfYSHSFDSSVSEIFSTLLNGAeLYLLSDE 1748
Cdd:PRK05857  176 FTSGTTGEPKAVLLANRTFfavpdilqkegLNWVTWVVGETTYSP-------LPATHIGGLWWILTCLMHGG-LCVTGGE 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1749 QRYSTVEYAQAiqETQATISDLPTVffnelstsLTKLDSE------KIRSLRFIIMGGEAASTNAIRSWQNTFKNQVQLv 1822
Cdd:PRK05857  248 NTTSLLEILTT--NAVATTCLVPTL--------LSKLVSElksanaTVPSLRLVGYGGSRAIAADVRFIEATGVRTAQV- 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1823 neYGPTEATVSAMyyFIPVLEGENNLLGSVPIGIPISNTKVHILN------SYMQYCPVGCMGELYIESLGLAQGYWKQK 1896
Cdd:PRK05857  317 --YGLSETGCTAL--CLPTDDGSIVKIEAGAVGRPYPGVDVYLAAtdgigpTAPGAGPSASFGTLWIKSPANMLGYWNNP 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1897 EKTKQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAV---VTQTEG 1973
Cdd:PRK05857  393 ERTAEVLIDG---------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAAcyeIPDEEF 463

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728 1974 GML--LQAYYKT-VDGIGIE--KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK05857  464 GALvgLAVVASAeLDESAARalKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKV 520
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
483-972 2.20e-15

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 81.96  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGgvYVPIDPKFPEKRIE--- 559
Cdd:PRK10946   37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSElna 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  560 YIlKDSESQMIITKKEYR-----GLVERFAIHTIYLEDFHYANSIENIASTHTIEDA--------------AYIIYTSGS 620
Cdd:PRK10946  115 YA-SQIEPALLIADRQHAlfsddDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPaedftatpspadevAFFQLSGGS 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  621 TGLPKGVVVPHKgvvNLSYSV----------INTFHL--------------GKEDVFLQFATIIF--DASIMEIFPIllc 674
Cdd:PRK10946  194 TGTPKLIPRTHN---DYYYSVrrsveicgftPQTRYLcalpaahnypmsspGALGVFLAGGTVVLapDPSATLCFPL--- 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  675 ggrmhliseIEKRSaeefINVsqkygiTNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKI 754
Cdd:PRK10946  268 ---------IEKHQ----VNV------TALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  755 PvlNAYGPTETTVCATMYEVNGEI----QkeisnipiGKPIA-NSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQK 829
Cdd:PRK10946  329 Q--QVFGMAEGLVNYTRLDDSDERifttQ--------GRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSP 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  830 EKTEGAFisldksynrDKK-MYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN-- 906
Cdd:PRK10946  399 QHNASAF---------DANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDel 469

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  907 --DKIVCFYLSKDntELKQEALKTFLSE-SLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQIPSLLEN 972
Cdd:PRK10946  470 mgEKSCAFLVVKE--PLKAVQLRRFLREqGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA 536
PRK07529 PRK07529
AMP-binding domain protein; Validated
 473-965 4.45e-15

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 81.15  E-value: 4.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  473 QLIDLQALKSPNQIAISM---GD-----QSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGIlKSGG 544
Cdd:PRK07529   29 ELLSRAAARHPDAPALSFlldADpldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG-EAAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  545 VYVPIDPKFPEKRIEYILKDSESQMIITKK------------------------------EYRGLVERFAI------HTI 588
Cdd:PRK07529  108 IANPINPLLEPEQIAELLRAAGAKVLVTLGpfpgtdiwqkvaevlaalpelrtvvevdlaRYLPGPKRLAVplirrkAHA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  589 YLEDFH------YANSIENiASTHTIEDAAYIIYTSGSTGLPKgvVVPHKgVVNLSYS--VINTFHLGKEDVFLQFATII 660
Cdd:PRK07529  188 RILDFDaelarqPGDRLFS-GRPIGPDDVAAYFHTGGTTGMPK--LAQHT-HGNEVANawLGALLLGLGPGDTVFCGLPL 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  661 F--DASIMEIFPILLCGGRMHLISEIEKRSAE---EFINVSQKYGITNVV-LPTAFFKLiADMPKEMLlKLNSVKRLFVG 734
Cdd:PRK07529  264 FhvNALLVTGLAPLARGAHVVLATPQGYRGPGviaNFWKIVERYRINFLSgVPTVYAAL-LQVPVDGH-DISSLRYALCG 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  735 GETLPAESVRKWQSKLGlkIPVLNAYGPTETTVCATMYEVNGEiqKEISNIPIGKPIANSEVFVISPFNTL---CPSGVV 811
Cdd:PRK07529  342 AAPLPVEVFRRFEAATG--VRIVEGYGLTEATCVSSVNPPDGE--RRIGSVGLRLPYQRVRVVILDDAGRYlrdCAVDEV 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  812 GELFIGGDGVANGYLNQkEKTEGAFisLDKSYNRdkkmycTGDLVRLLANGNLEFIGR-KDnqVKIR-GYRIELDEIEGT 889
Cdd:PRK07529  418 GVLCIAGPNVFSGYLEA-AHNKGLW--LEDGWLN------TGDLGRIDADGYFWLTGRaKD--LIIRgGHNIDPAAIEEA 486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  890 LFKHPEVRDAVVFTyQND----KIVCFYLS-KDNTELKQEALKTFLSESLPD-FMMPNYIFHLESFPVSPSGKLDrkKLE 963
Cdd:PRK07529  487 LLRHPAVALAAAVG-RPDahagELPVAYVQlKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIF--KPA 563


                  ..
gi 446581728  964 LQ 965
Cdd:PRK07529  564 LR 565
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 1674-2025 5.34e-15

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 78.70  E-value: 5.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1674 DLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK---VTQFYsHSFDSSVSeIFSTLLNGAELYllsDEQR 1750
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRyliINPFF-HTFGYKAG-IVACLLTGATVV---PVAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1751 YSTVEYAQAIQETQATI-SDLPTVFFNELSTSltKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVQLvNEYGPTE 1829
Cdd:cd17638    76 FDVDAILEAIERERITVlPGPPTLFQSLLDHP--GRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVL-TAYGLTE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1830 ATVSAMyyfipVLEGENNLLGSVPIGIPISNTKVHILNSymqycpvgcmGELYIESLGLAQGYWKQKEKTKQAFisnpfs 1909
Cdd:cd17638   153 AGVATM-----CRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1910 eDNSKRLYrTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEG---GMLLQAYYKTVDG 1986
Cdd:cd17638   212 -DADGWLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDermGEVGKAFVVARPG 289

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 446581728 1987 IGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd17638   290 VTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1559-2025 6.41e-15

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 79.92  E-value: 6.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPidvkypedrinyivrdseACRIITSN 1638
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1639 KFKSHLNVSDYKVSIIEDIYRTtinddvkilnkpDDLAYVIYTSGSTGKPKGTLLTHK----GVLNLVEWrnevFQISPN 1714
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDENTHA------------DDPMLLYFTSGTTSKPKLVEHTHRsypvGHLSTMYW----IGLKPG 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1715 DKVTQFYSHSFDSSV-SEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELSTSLTKLDSekirSL 1793
Cdd:cd05974   127 DVHWNISSPGWAKHAwSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV----KL 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1794 RFIIMGGEAASTNAI----RSWQNTFKNQvqlvneYGPTEATVsamyyFIPVLEGENNLLGSvpIGIPISNTKVHILNsy 1869
Cdd:cd05974   203 REVVGAGEPLNPEVIeqvrRAWGLTIRDG------YGQTETTA-----LVGNSPGQPVKAGS--MGRPLPGYRVALLD-- 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1870 mqycPVG---CMGELYIE-----SLGLAQGYWKQKEKTKQAFisnpfsednSKRLYRTGDLVRWLPNGNIEFMGRKDKQV 1941
Cdd:cd05974   268 ----PDGapaTEGEVALDlgdtrPVGLMKGYAGDPDKTAHAM---------RGGYYRTGDIAMRDEDGYLTYVGRADDVF 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1942 KIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGMLL---QAYYKTVDGIGiEKNKLAIHLSNVLPEYMVPkyYSHV---- 2014
Cdd:cd05974   335 KSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLsvpKAFIVLRAGYE-PSPETALEIFRFSRERLAP--YKRIrrle 411

                         490
                  ....*....|..
gi 446581728 2015 -LEIPITANGKI 2025
Cdd:cd05974   412 fAELPKTISGKI 423
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 1545-2034 7.04e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 80.36  E-value: 7.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYP------ 1618
Cdd:PRK07788   61 RAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSgpqlae 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1619 ---EDRINYIVRDSE-------------ACRIITSNKFKSHLNVSDykVSIIEDIYRTTindDVKILNKPDDLA-YVIYT 1681
Cdd:PRK07788  141 vaaREGVKALVYDDEftdllsalppdlgRLRAWGGNPDDDEPSGST--DETLDDLIAGS---STAPLPKPPKPGgIVILT 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1682 SGSTGKPKG-------TLLTHKGVLNLVEWR-NEVFQISpndkvtqfyshsfdssvSEIFSTL----LN-----GAELYL 1744
Cdd:PRK07788  216 SGTTGTPKGaprpepsPLAPLAGLLSRVPFRaGETTLLP-----------------APMFHATgwahLTlamalGSTVVL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1745 lsdEQRYSTVEYAQAIQETQAT-ISDLPTV---FFNELSTSLTKLDsekIRSLRFIIMGGEAASTNAIRSWQNTFkNQVq 1820
Cdd:PRK07788  279 ---RRRFDPEATLEDIAKHKATaLVVVPVMlsrILDLGPEVLAKYD---TSSLKIIFVSGSALSPELATRALEAF-GPV- 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1821 LVNEYGPTE---ATVSAMYYfipvLEGENNLLGSVPIGipisnTKVHILNSYMQYCPVGCMGELYIESLGLAQGYwkqke 1897
Cdd:PRK07788  351 LYNLYGSTEvafATIATPED----LAEAPGTVGRPPKG-----VTVKILDENGNEVPRGVVGRIFVGNGFPFEGY----- 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1898 ktkqafiSNPFSEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQT---EGG 1974
Cdd:PRK07788  417 -------TDGRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVddeEFG 489

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1975 MLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIE 2034
Cdd:PRK07788  490 QRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 1540-1968 7.62e-15

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 80.75  E-value: 7.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1540 YMQVDR----QPERIAI------ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAA 1609
Cdd:TIGR02188   60 YNCVDRhleaRPDKVAIiwegdePGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAI 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1610 YipiDVKY----PE---DRINyivrDSEACRIITSNKFKSHLNVSDYK------VSIIED------IYRTTINDDVK--- 1667
Cdd:TIGR02188  140 H---SVVFggfsAEalaDRIN----DAGAKLVITADEGLRGGKVIPLKaivdeaLEKCPVsvehvlVVRRTGNPVVPwve 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1668 ---------ILNKPD----------DLAYVIYTSGSTGKPKGTLLTHKGVL----NLVEWrneVFQISPNDK-------- 1716
Cdd:TIGR02188  213 grdvwwhdlMAKASAycepepmdseDPLFILYTSGSTGKPKGVLHTTGGYLlyaaMTMKY---VFDIKDGDIfwctadvg 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1717 -VTqfySHSFdssvsEIFSTLLNGAELYLLSDEQRYSTV-EYAQAIQETQATI-SDLPTVFfnelsTSLTKLDSEKIR-- 1791
Cdd:TIGR02188  290 wIT---GHSY-----IVYGPLANGATTVMFEGVPTYPDPgRFWEIIEKHKVTIfYTAPTAI-----RALMRLGDEWVKkh 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1792 ---SLRfiIMG--GEAASTNAIRsWQNTF--KNQVQLVNEYGPTEaTVSAMYYFIPvlegennllGSVPI-----GIPIS 1859
Cdd:TIGR02188  357 dlsSLR--LLGsvGEPINPEAWM-WYYKVvgKERCPIVDTWWQTE-TGGIMITPLP---------GATPTkpgsaTLPFF 423

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  1860 NTKVHILNSYMQYCP-VGCMGELYIESL--GLAQGYWKQKEKtkqaFISNPFSEdnSKRLYRTGDLVRWLPNGNIEFMGR 1936
Cdd:TIGR02188  424 GIEPAVVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDHER----FVDTYFSP--FPGYYFTGDGARRDKDGYIWITGR 497

                          490       500       510
                   ....*....|....*....|....*....|..
gi 446581728  1937 KDKQVKIRGHRIELGEIEDAMLQLEGISQAVV 1968
Cdd:TIGR02188  498 VDDVINVSGHRLGTAEIESALVSHPAVAEAAV 529
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 1552-2025 7.91e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 79.95  E-value: 7.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1552 IATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEA 1631
Cdd:PRK08276    5 MAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1632 CRIITSNKFK--------------SHLNVSDYKVSIIEDiYRTTIND--DVKILNKP--DDLAyviYTSGSTGKPKGTL- 1692
Cdd:PRK08276   85 KVLIVSAALAdtaaelaaelpagvPLLLVVAGPVPGFRS-YEEALAAqpDTPIADETagADML---YSSGTTGRPKGIKr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1693 -LTHKGVLN--------LVEWrnevFQISPnDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDeqRYSTVEYAQAIQET 1763
Cdd:PRK08276  161 pLPGLDPDEapgmmlalLGFG----MYGGP-DSVYLSPAPLYHTAPLRFGMSALALGGTVVVME--KFDAEEALALIERY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1764 QATISDL-PTVFfnelsTSLTKLdSEKIR------SLRFIImggEAASTNAIRswqntFKNQV-----QLVNE-YGPTEA 1830
Cdd:PRK08276  234 RVTHSQLvPTMF-----VRMLKL-PEEVRarydvsSLRVAI---HAAAPCPVE-----VKRAMidwwgPIIHEyYASSEG 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1831 TVSAmyyfipVLEGENNLL--GSVpiGIPISnTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAfisnpf 1908
Cdd:PRK08276  300 GGVT------VITSEDWLAhpGSV--GKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA------ 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1909 seDNSKRLYRTGDlVRWL-PNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKTV 1984
Cdd:PRK08276  365 --RNPHGWVTVGD-VGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVfgvPDEEMGERVKAVVQPA 441

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 446581728 1985 DGIGIEK---NKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK08276  442 DGADAGDalaAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 483-968 9.89e-15

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 79.84  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQS---ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEkriE 559
Cdd:cd05908     1 PEGIIFILGDKKekfVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNE---E 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  560 YILKdsesqmiiTKKEYRGLVERFAIHTIYLEDfhyansieniastHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSY 639
Cdd:cd05908    78 HKLK--------LNKVWNTLKNPYLITEEEVLC-------------ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMF 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  640 SVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLI--SEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADM 717
Cdd:cd05908   137 AILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLmpTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKT 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  718 PKEMLLK---LNSVKRLFVGGETLPAE---SVRKWQSKLGLK-IPVLNAYGPTETTVCATMYEVN--------------- 775
Cdd:cd05908   217 LKPEKANdwdLSSIRMILNGAEPIDYElchEFLDHMSKYGLKrNAILPVYGLAEASVGASLPKAQspfktitlgrrhvth 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  776 GEIQKEISN--------IPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFisldksynRDK 847
Cdd:cd05908   297 GEPEPEVDKkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVF--------TDD 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  848 KMYCTGDLvRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLF-KHPEVRDAVVF------TYQNDKIVCFYLSKDNTE 920
Cdd:cd05908   369 GWLKTGDL-GFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEeLEGVELGRVVAcgvnnsNTRNEEIFCFIEHRKSED 447

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446581728  921 ----LKQEaLKTFLSESlpDFMMPNYIFHLESFPVSPSGKLDRKKLELQIPS 968
Cdd:cd05908   448 dfypLGKK-IKKHLNKR--GGWQINEVLPIRRIPKTTSGKVKRYELAQRYQS 496
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 43-308 1.94e-14

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 78.00  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   43 KLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLIqknveFDIPIK-------DLTAFKNTEqksilknflesiv 115
Cdd:cd19537    31 RLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSY-----SSSPPRvqrvdtlDVWKEINRP------------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  116 nekFSLEEGPLFKFHIikfSEDTFILhLMfHHIIYDGWSLGVFIRQLSNTYgellQGKSNVEFESPYknlvkheesfIDS 195
Cdd:cd19537    93 ---FDLEREDPIRVFI---SPDTLLV-VM-SHIICDLTTLQLLLREVSAAY----NGKLLPPVRREY----------LDS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  196 AIYK-----EGSSYWKDYLQGeLTPTEFPidfNKMNEKRYTDKNISKNINSDLFYQIQCFAKKNNISIYRVMLSTYCTLL 270
Cdd:cd19537   151 TAWSrpaspEDLDFWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALAL 226

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 446581728  271 HQMTNAEEIIVGIPINTRPYTEERNTFGYFVNTLPIRI 308
Cdd:cd19537   227 QDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRI 264
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 2164-2407 2.40e-14

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 73.87  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2164 VFLTGATGYLGAHILERLLQLpsttiyclvrenedqvigaklkermefyfGKEILqklkerveliegdlslmnlGLDskq 2243
Cdd:cd08946     1 ILVTGGAGFIGSHLVRRLLER-----------------------------GHEVV-------------------VID--- 29

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2244 ldhlkkNVESIIHCGGEV---RHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKEFEFFEsdfd 2319
Cdd:cd08946    30 ------RLDVVVHLAALVgvpASWDNPDEDFETNVVGTLNLLEAARKAGVkRFVYASSASVYGSPEGLPEEEETPP---- 99

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2320 rgqNLDNLYLESKFQGEKMVREAMEK-GVRATIYRVGNLVGNSKTGKFQYNINeNAFYRLLKGICLsSIAPDVNTYVDLT 2398
Cdd:cd08946   100 ---RPLSPYGVSKLAAEHLLRSYGESyGLPVVILRLANVYGPGQRPRLDGVVN-DFIRRALEGKPL-TVFGGGNQTRDFI 174


                  ....*....
gi 446581728 2399 PVDYGSLAI 2407
Cdd:cd08946   175 HVDDVVRAI 183
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 1540-1968 2.94e-14

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 78.51  E-value: 2.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1540 YMQVDR-----QPERIAI-----ATATE-SLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGA 1608
Cdd:cd05967    53 YNALDRhveagRGDQIALiydspVTGTErTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGA 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1609 AYIPI----DVKYPEDRINyivrDSEACRIITSNKFKSHLNVSDYKvSIIEDIYRTTIND--DVKILNKPD--------- 1673
Cdd:cd05967   133 IHSVVfggfAAKELASRID----DAKPKLIVTASCGIEPGKVVPYK-PLLDKALELSGHKphHVLVLNRPQvpadltkpg 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1674 -----------------------DLAYVIYTSGSTGKPKGTLLTHKGVLNLVEW--RNeVFQISPNDkvtQFYS------ 1722
Cdd:cd05967   208 rdldwsellakaepvdcvpvaatDPLYILYTSGTTGKPKGVVRDNGGHAVALNWsmRN-IYGIKPGD---VWWAasdvgw 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1723 ---HSFDssvseIFSTLLNGAelyllsdeqrySTVEYaqaiqETQATISDLPTVFF--------NELSTSLTKL------ 1785
Cdd:cd05967   284 vvgHSYI-----VYGPLLHGA-----------TTVLY-----EGKPVGTPDPGAFWrviekyqvNALFTAPTAIrairke 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1786 --DSEKIR-----SLRFIIMGGEA--ASTnaiRSW-QNTFKnqVQLVNEYGPTEaTVSAMyyfIPVLEGennlLGSVPI- 1854
Cdd:cd05967   343 dpDGKYIKkydlsSLRTLFLAGERldPPT---LEWaENTLG--VPVIDHWWQTE-TGWPI---TANPVG----LEPLPIk 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1855 ----GIPISNTKVHILNSYMQYCPVGCMGELYIE---SLGLAQGYWKQKEKTKQAFISNpfsednSKRLYRTGDLVRWLP 1927
Cdd:cd05967   410 agspGKPVPGYQVQVLDEDGEPVGPNELGNIVIKlplPPGCLLTLWKNDERFKKLYLSK------FPGYYDTGDAGYKDE 483

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 446581728 1928 NGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV 1968
Cdd:cd05967   484 DGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAV 524
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 495-901 3.39e-14

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 77.61  E-value: 3.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  495 ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPidpkfpekrieyilkdseSQMIITKK 574
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  575 EYRGLVERfAIHTIYLEDfhyansieniASTHTiEDAAYIIYTSGSTGLPKGVVVPHKgvvnlSYSV--INTFH---LGK 649
Cdd:cd05974    63 DLRDRVDR-GGAVYAAVD----------ENTHA-DDPMLLYFTSGTTSKPKLVEHTHR-----SYPVghLSTMYwigLKP 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  650 EDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPkemLLKLNSVK 729
Cdd:cd05974   126 GDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD---LASFDVKL 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  730 RLFVG-GETLPAESVRKWQSKLGLKIPvlNAYGPTETTVcatmyevngeiqkEISNIP--------IGKPIANSEVFVIS 800
Cdd:cd05974   203 REVVGaGEPLNPEVIEQVRRAWGLTIR--DGYGQTETTA-------------LVGNSPgqpvkagsMGRPLPGYRVALLD 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  801 PFNTLCPSGVVGeLFIGGD---GVANGYLNQKEKTEGAfisLDKSYnrdkkmYCTGDLVRLLANGNLEFIGRKDNQVKIR 877
Cdd:cd05974   268 PDGAPATEGEVA-LDLGDTrpvGLMKGYAGDPDKTAHA---MRGGY------YRTGDIAMRDEDGYLTYVGRADDVFKSS 337

                         410       420
                  ....*....|....*....|....
gi 446581728  878 GYRIELDEIEGTLFKHPEVRDAVV 901
Cdd:cd05974   338 DYRISPFELESVLIEHPAVAEAAV 361
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 986-1047 3.77e-14

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 69.13  E-value: 3.77e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728   986 KRLAKTWAEILNLGKYRIGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIAS 1047
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 1556-2025 4.55e-14

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 77.47  E-value: 4.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1556 TESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAG--AAYIPIDVKypEDRINYIVRDSEACR 1633
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGveTALINSNLR--LESLLHCITVSKAKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1634 IITSNKFKSHLNVSDYKVSIIediyrttinddvkILNKPDDLAYvIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISP 1713
Cdd:cd05939    79 LIFNLLDPLLTQSSTEPPSQD-------------DVNFRDKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRP 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1714 NDKV---TQFYsHSFDSSVSeIFSTLLNGAELYLlsdEQRYSTVEYAQAIQETQATISDlptvFFNELSTSL---TKLDS 1787
Cdd:cd05939   145 EDVVydcLPLY-HSAGGIMG-VGQALLHGSTVVI---RKKFSASNFWDDCVKYNCTIVQ----YIGEICRYLlaqPPSEE 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1788 EKIRSLRFIIMGGEAASTnairsWQN-TFKNQVQLVNE-YGPTEATVSAMYyfipvLEGENNLLGSVPIgIPISNTKVHI 1865
Cdd:cd05939   216 EQKHNVRLAVGNGLRPQI-----WEQfVRRFGIPQIGEfYGATEGNSSLVN-----IDNHVGACGFNSR-ILPSVYPIRL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1866 L-------------NSYMQYCPVGCMGELY---IESLGLAQ--GYWKQKEkTKQAFISNPFSEDNSkrLYRTGDLVRWLP 1927
Cdd:cd05939   285 IkvdedtgelirdsDGLCIPCQPGEPGLLVgkiIQNDPLRRfdGYVNEGA-TNKKIARDVFKKGDS--AFLSGDVLVMDE 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1928 NGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV-----TQTEGGMLLQAYYKTVDGIGIEknKLAIHLSNVL 2002
Cdd:cd05939   362 LGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygvevPGVEGRAGMAAIVDPERKVDLD--RFSAVLAKSL 439

                         490       500
                  ....*....|....*....|...
gi 446581728 2003 PEYMVPKYYSHVLEIPITANGKI 2025
Cdd:cd05939   440 PPYARPQFIRLLPEVDKTGTFKL 462
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 1560-2034 4.93e-14

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 77.51  E-value: 4.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1560 TYRQLNMSSNQVAQHLLEK-GIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSN 1638
Cdd:cd05928    43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1639 K--------------FKSHLNVSDYKVS---IIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGT-----LLTHK 1696
Cdd:cd05928   123 ElapevdsvasecpsLKTKLLVSEKSRDgwlNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAehshsSLGLG 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1697 GVLNLVEWRNevfqISPNDKvtqFYSHS----FDSSVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQATISDLPT 1772
Cdd:cd05928   203 LKVNGRYWLD----LTASDI---MWNTSdtgwIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPT 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1773 VFFNELSTSLTkldSEKIRSLRFIIMGGEAASTNAIRSWQNtfKNQVQLVNEYGPTEATVSAMYYfipvlEGENNLLGSv 1852
Cdd:cd05928   276 VYRMLVQQDLS---SYKFPSLQHCVTGGEPLNPEVLEKWKA--QTGLDIYEGYGQTETGLICANF-----KGMKIKPGS- 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1853 pIGIPISNTKVHILNSYMQYCPVGCMGELYIE-----SLGLAQGYWKQKEKTKQAFISNpfsednskrLYRTGDLVRWLP 1927
Cdd:cd05928   345 -MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAATIRGD---------FYLTGDRGIMDE 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1928 NGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQ-AVVTQ--------TEGGMLLQAYYKTVDGIGIEKnKLAIHL 1998
Cdd:cd05928   415 DGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVEsAVVSSpdpirgevVKAFVVLAPQFLSHDPEQLTK-ELQQHV 493

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 446581728 1999 SNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIE 2034
Cdd:cd05928   494 KSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 522-965 1.20e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 76.60  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  522 VSITMEREIDTIVWILGILKSGGVYVPIDPKfpeKRIEYILKD---SESQMIITKKEYRGLVERF---AIHTIYLEDFHY 595
Cdd:PRK13388   55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAALAADirrADCQLLVTDAEHRPLLDGLdlpGVRVLDVDTPAY 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  596 ANSIENIASTHTIEDAA-----YIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIF- 669
Cdd:PRK13388  132 AELVAAAGALTPHREVDamdpfMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWa 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  670 PILLCGGRMHLISeieKRSAEEFINVSQKYGIT--NVV-LPTAFFKLIADMPKEmllKLNSVKRLFvGGETLPaESVRKW 746
Cdd:PRK13388  212 PAVASGAAVALPA---KFSASGFLDDVRRYGATyfNYVgKPLAYILATPERPDD---ADNPLRVAF-GNEASP-RDIAEF 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  747 QSKLGLKipVLNAYGPTETTVCATMYEvngeiqkeisNIP---IGKPIANseVFVISPfNTLCPSGV------------- 810
Cdd:PRK13388  284 SRRFGCQ--VEDGYGSSEGAVIVVREP----------GTPpgsIGRGAPG--VAIYNP-ETLTECAVarfdahgallnad 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  811 --VGELF-IGGDGVANGYLNQKEKTEGAFisldksynRDkKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIE 887
Cdd:PRK13388  349 eaIGELVnTAGAGFFEGYYNNPEATAERM--------RH-GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIE 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  888 GTLFKHPEVRDAVVFT----YQNDKIVCFYLSKDNTELKQEALKTFLS--ESLPDFMMPNYIFHLESFPVSPSGKLDRKK 961
Cdd:PRK13388  420 RILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRE 499


                  ....
gi 446581728  962 LELQ 965
Cdd:PRK13388  500 LIAQ 503
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 493-878 1.23e-13

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 76.69  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  493 QSITYYELQQRSNQIVNYLRENDlKKGQRVSITMEREIDTIVWILGILKSGGVYVPI-DPKFP--EKRIEYILKDSESQM 569
Cdd:PRK07769   54 RDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSA 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  570 IIT--------KKEYRGL--VERFAIHTIyledfhyaNSIEN-IAST-----HTIEDAAYIIYTSGSTGLPKGVVVPHKG 633
Cdd:PRK07769  133 ILTttdsaegvRKFFRARpaKERPRVIAV--------DAVPDeVGATwvppeANEDTIAYLQYTSGSTRIPAGVQITHLN 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  634 VVNLSYSVINTFHLGKEDVFLQFATIIFDAS-IMEIFPIlLCGGRMHLISEIE-----KRSAEEFINVSQKYGITNVVLP 707
Cdd:PRK07769  205 LPTNVLQVIDALEGQEGDRGVSWLPFFHDMGlITVLLPA-LLGHYITFMSPAAfvrrpGRWIRELARKPGGTGGTFSAAP 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  708 TAFFKLIA--DMPK--EMLLKLNSVKRLFVGGETLPAESVRKWQ---SKLGL-KIPVLNAYGPTETT--VCAT------- 770
Cdd:PRK07769  284 NFAFEHAAarGLPKdgEPPLDLSNVKGLLNGSEPVSPASMRKFNeafAPYGLpPTAIKPSYGMAEATlfVSTTpmdeept 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  771 -------------MYEVNGEIQKEISNIPIGKpIANSEVFVISPFNTLC--PSGVVGELFIGGDGVANGYLNQKEKTEGA 835
Cdd:PRK07769  364 viyvdrdelnagrFVEVPADAPNAVAQVSAGK-VGVSEWAVIVDPETASelPDGQIGEIWLHGNNIGTGYWGKPEETAAT 442

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446581728  836 FIS-----LDKSYNR----DKKMYCTGDLVRLLaNGNLEFIGRKDNQVKIRG 878
Cdd:PRK07769  443 FQNilksrLSESHAEgapdDALWVRTGDYGVYF-DGELYITGRVKDLVIIDG 493
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 1546-1922 1.25e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 76.52  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1546 QPERIAI---------ATATESLTYRQLNMSSNQVAQHLLEKGIKrGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVK 1616
Cdd:PRK05850   14 QPDDAAFtfidyeqdpAGVAETLTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1617 YP---EDRINYIVRDSEACRIITSNKFKSHlnVSDY--------KVSIIE-DIYRTTINDDVKILNKP-DDLAYVIYTSG 1683
Cdd:PRK05850   93 QGgahDERVSAVLRDTSPSVVLTTSAVVDD--VTEYvapqpgqsAPPVIEvDLLDLDSPRGSDARPRDlPSTAYLQYTSG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1684 STGKPKGTLLTHKGVLNLVEwrnevfQIspndkVTQFYSH-----SFDSS-VS------------EIFSTLLNGAELYLL 1745
Cdd:PRK05850  171 STRTPAGVMVSHRNVIANFE------QL-----MSDYFGDtggvpPPDTTvVSwlpfyhdmglvlGVCAPILGGCPAVLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1746 SDE---QRYStvEYAQAIQETQATISDLPTVFFnELSTSLTK------LDsekIRSLRFIIMGGEAASTNAIRSWQNTFK 1816
Cdd:PRK05850  240 SPVaflQRPA--RWMQLLASNPHAFSAAPNFAF-ELAVRKTSdddmagLD---LGGVLGIISGSERVHPATLKRFADRFA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1817 ----NQVQLVNEYGPTEATV----------SAMYYFIP--VLEGENNLLGS------VPIGIPISNTkVHILNS-YMQYC 1873
Cdd:PRK05850  314 pfnlRETAIRPSYGLAEATVyvatrepgqpPESVRFDYekLSAGHAKRCETgggtplVSYGSPRSPT-VRIVDPdTCIEC 392

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446581728 1874 PVGCMGELYIESLGLAQGYW---KQKEKTKQAFISNPfSEDNSKRLY-RTGDL 1922
Cdd:PRK05850  393 PAGTVGEIWVHGDNVAAGYWqkpEETERTFGATLVDP-SPGTPEGPWlRTGDL 444
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 1543-1968 1.41e-13

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 76.25  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAIAT------ATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVK 1616
Cdd:PRK13295   34 VASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1617 YPEDRINYIVRDSEACRIITSNKFK------------------SHLNV--SDYKVS---IIEDIYRTTINDDVKILNK-- 1671
Cdd:PRK13295  114 FRERELSFMLKHAESKVLVVPKTFRgfdhaamarrlrpelpalRHVVVvgGDGADSfeaLLITPAWEQEPDAPAILARlr 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 --PDDLAYVIYTSGSTGKPKGTLLTHKGVL-NLVEWRNE--------VFQISPNDKVTQFyshsfdssvseifstlLNGA 1740
Cdd:PRK13295  194 pgPDDVTQLIYTSGTTGEPKGVMHTANTLMaNIVPYAERlglgaddvILMASPMAHQTGF----------------MYGL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1741 ELYLLSdeqRYSTV-----EYAQA---IQETQATISDLPTVFFNELsTSLTKLDSEKIRSLR-FIIMGGEAASTNAIRSW 1811
Cdd:PRK13295  258 MMPVML---GATAVlqdiwDPARAaelIRTEGVTFTMASTPFLTDL-TRAVKESGRPVSSLRtFLCAGAPIPGALVERAR 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1812 QNTfknQVQLVNEYGPTE-ATVSAmyyfipVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQ 1890
Cdd:PRK13295  334 AAL---GAKIVSAWGMTEnGAVTL------TKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFG 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1891 GYWKQKEKTKqafisnpfseDNSKRLYRTGDLVRWLPNGNIEFMGRkDKQVKIRG-HRIELGEIEDAMLQLEGISQ-AVV 1968
Cdd:PRK13295  405 GYLKRPQLNG----------TDADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQvAIV 473
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 2164-2360 1.45e-13

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 71.28  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2164 VFLTGATGYLGAHILERLLQLPSttiyclvrenedQVIG-AKLKERMEFYFGkeilqklkERVELIEGDLslmnlgLDSK 2242
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGH------------EVTLlVRNTKRLSKEDQ--------EPVAVVEGDL------RDLD 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2243 QLDHLKKNVESIIHCGGEVRhygEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQaerDPKEFEFFESDFdrg 2321
Cdd:cd05226    55 SLSDAVQGVDVVIHLAGAPR---DTRDFCEVDVEGTRNVLEAAKEAGVkHFIFISSLGAYGD---LHEETEPSPSSP--- 125

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446581728 2322 qnldnlYLESKFQGEKMVREAmekGVRATIYRVGNLVGN 2360
Cdd:cd05226   126 ------YLAVKAKTEAVLREA---SLPYTIVRPGVIYGD 155
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 1678-2026 1.55e-13

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 74.23  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1678 VIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDK----VTQFYSHSFDSSvseiFSTLLNGAELYLLSdeqRYST 1753
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVylnmLPLFHIAGLNLA----LATFHAGGANVVME---KFDP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1754 VEYAQAIQETQAT-ISDLPTVffneLSTSLTKLDSE--KIRSLRfIIMGGEAASTnaIRSWQNTfkNQVQLVNEYGPTEA 1830
Cdd:cd17637    78 AEALELIEEEKVTlMGSFPPI----LSNLLDAAEKSgvDLSSLR-HVLGLDAPET--IQRFEET--TGATFWSLYGQTET 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1831 tvSAMYYFIPVLEGEnnllGSVpiGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpfse 1910
Cdd:cd17637   149 --SGLVTLSPYRERP----GSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF------- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1911 DNSkrLYRTGDLVRWLPNGNIEFMGRK-DKQ-VKIRGHRIELGEIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKTVD 1985
Cdd:cd17637   214 RNG--WHHTGDLGRFDEDGYLWYAGRKpEKElIKPGGENVYPAEVEKVILEHPAIAEVCVigvPDPKWGEGIKAVCVLKP 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 446581728 1986 GIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:cd17637   292 GATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSID 332
PRK08315 PRK08315
AMP-binding domain protein; Validated
 1533-2025 2.02e-13

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 75.62  E-value: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1533 QNIQEQFYMQVDRQPERIAIATATESL--TYRQLNMSSNQVAQHLLEKGIKRGDKVAIFldrSMNSI---VSMLGILKAG 1607
Cdd:PRK08315   16 QTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIW---APNVPewvLTQFATAKIG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1608 AAYIPIDVKYPEDRINYIVRDSEACRIITSNKFKShlnvSDYkVSIIEDI-------------------YRTTI------ 1662
Cdd:PRK08315   93 AILVTINPAYRLSELEYALNQSGCKALIAADGFKD----SDY-VAMLYELapelatcepgqlqsarlpeLRRVIflgdek 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1663 ---------------NDDVKILN------KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKV---T 1718
Cdd:PRK08315  168 hpgmlnfdellalgrAVDDAELAarqatlDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLcipV 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1719 QFYsHSFdSSVSEIFSTLLNGAELYLLSDEqrYSTVEYAQAIQETQAT-ISDLPTVFFNELS-TSLTKLDsekIRSLRFI 1796
Cdd:PRK08315  248 PLY-HCF-GMVLGNLACVTHGATMVYPGEG--FDPLATLAAVEEERCTaLYGVPTMFIAELDhPDFARFD---LSSLRTG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1797 IMGGeaaSTNAIRswqnTFKNQVQLVN--E----YGPTEATvsamyyfiPV---------LEGENNLLGSV-PigipisN 1860
Cdd:PRK08315  321 IMAG---SPCPIE----VMKRVIDKMHmsEvtiaYGMTETS--------PVstqtrtddpLEKRVTTVGRAlP------H 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1861 TKVHILN-SYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpfsedNSKRLYRTGDLVRWLPNGNIEFMGR-KD 1938
Cdd:PRK08315  380 LEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI--------DADGWMHTGDLAVMDEEGYVNIVGRiKD 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1939 kqVKIRGhrielG------EIEDAMLQLEGISQAvvtQTEG------GMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYM 2006
Cdd:PRK08315  452 --MIIRG-----GeniyprEIEEFLYTHPKIQDV---QVVGvpdekyGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYK 521

                         570
                  ....*....|....*....
gi 446581728 2007 VPKYYSHVLEIPITANGKI 2025
Cdd:PRK08315  522 IPRYIRFVDEFPMTVTGKI 540
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 1558-1922 2.38e-13

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 75.46  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQHLLEK-GIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV--------RD 1628
Cdd:cd05905    14 TLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLgtckvrvaLT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1629 SEACRIITSNKFKSHLNV--SDYKV---SIIE----DIYRTTINDDV--KILNKPDDLAYVIYTSGSTGKPKGTLLTHKG 1697
Cdd:cd05905    94 VEACLKGLPKKLLKSKTAaeIAKKKgwpKILDfvkiPKSKRSKLKKWgpHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1698 VLNLVEWRNEVFQISPNDKVTQFYSHSfdSSVSEIFSTLL---NGAELYLLSdeqrYSTVE-----YAQAIQE-----TQ 1764
Cdd:cd05905   174 LLAHCRALKEACELYESRPLVTVLDFK--SGLGLWHGCLLsvySGHHTILIP----PELMKtnpllWLQTLSQykvrdAY 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1765 ATISDLPTVfFNELSTSLTKLDSEKI--RSLRFIIM-GGEAASTNAIRSWQNTFKNQ----VQLVNEYG----------- 1826
Cdd:cd05905   248 VKLRTLHWC-LKDLSSTLASLKNRDVnlSSLRMCMVpCENRPRISSCDSFLKLFQTLglspRAVSTEFGtrvnpficwqg 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1827 -----PTEATVS--AMYYFIPVLEGEnNLLGSVPI---GIPISNTKVHILNSYMQY-CPVGCMGELYIESLGLAQGYW-- 1893
Cdd:cd05905   327 tsgpePSRVYLDmrALRHGVVRLDER-DKPNSLPLqdsGKVLPGAQVAIVNPETKGlCKDGEIGEIWVNSPANASGYFll 405

                         410       420       430
                  ....*....|....*....|....*....|.
gi 446581728 1894 -KQKEKTKQAFISNPFSEDNSKRLY-RTGDL 1922
Cdd:cd05905   406 dGETNDTFKVFPSTRLSTGITNNSYaRTGLL 436
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 609-896 3.01e-13

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 75.54  E-value: 3.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTF-HLGKEDVFLQFATIifdASIMEIFP--ILLCGGrmhliSEIE 685
Cdd:PLN02387  250 NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPL---AHILELAAesVMAAVG-----AAIG 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  686 KRSAEEFINVSQKY-----GITNVVLPTaffkLIADMP-----------KEMLLKLNSVKRLF----------VGGETLP 739
Cdd:PLN02387  322 YGSPLTLTDTSNKIkkgtkGDASALKPT----LMTAVPaildrvrdgvrKKVDAKGGLAKKLFdiaykrrlaaIEGSWFG 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  740 A---ESV-------RKWQSKLGLKI------------------------PVLNAYGPTETTVCATMYEVNgeiqkEISNI 785
Cdd:PLN02387  398 AwglEKLlwdalvfKKIRAVLGGRIrfmlsggaplsgdtqrfiniclgaPIGQGYGLTETCAGATFSEWD-----DTSVG 472

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  786 PIGKPIANSEVFVISpfntlCPSGVV---------GELFIGGDGVANGYLNQKEKTEGAFisldKSYNRDKKMYCTGDLV 856
Cdd:PLN02387  473 RVGPPLPCCYVKLVS-----WEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVY----KVDERGMRWFYTGDIG 543

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 446581728  857 RLLANGNLEFIGRKDNQVKIR-GYRIELDEIEGTLFKHPEV 896
Cdd:PLN02387  544 QFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYV 584
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 1545-2025 3.21e-13

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 75.06  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK07059   35 QYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEH 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSNKFKS------------HLNVSD------YKVSIIEDIYR--------------TTINDDV-----K 1667
Cdd:PRK07059  115 QLKDSGAEAIVVLENFATtvqqvlaktavkHVVVASmgdllgFKGHIVNFVVRrvkkmvpawslpghVRFNDALaegarQ 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1668 ILNK----PDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVE----WRNEVFQISPNDKVTQF------YsHSFDSSVSEIF 1733
Cdd:PRK07059  195 TFKPvklgPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeaWLQPAFEKKPRPDQLNFvcalplY-HIFALTVCGLL 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1734 STLLNGaeLYLLSDEQRystvEYAQAIQETQA-TISDLPTV--FFNEL--STSLTKLDsekIRSLRFIIMGGEAASTNAI 1808
Cdd:PRK07059  274 GMRTGG--RNILIPNPR----DIPGFIKELKKyQVHIFPAVntLYNALlnNPDFDKLD---FSKLIVANGGGMAVQRPVA 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1809 RSWQNtfKNQVQLVNEYGPTEATVSAMYYfiPVLEGENNllGSvpIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGL 1888
Cdd:PRK07059  345 ERWLE--MTGCPITEGYGLSETSPVATCN--PVDATEFS--GT--IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQV 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1889 AQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAV- 1967
Cdd:PRK07059  417 MAGYWNRPDETAKVMTADGF--------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAa 488

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1968 --VTQTEGGMLLQAYYKTVDGIGIEKNKLAiHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK07059  489 vgVPDEHSGEAVKLFVVKKDPALTEEDVKA-FCKERLTNYKRPKFVEFRTELPKTNVGKI 547
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 1543-1902 3.31e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 74.73  E-value: 3.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQPERIAI--ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPED 1620
Cdd:PRK13391    7 AQTTPDKPAVimASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1621 RINYIVRDSEACRIITSnkfKSHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVI------------------YTS 1682
Cdd:PRK13391   87 EAAYIVDDSGARALITS---AAKLDVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVaglpatpiadeslgtdmlYSS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1683 GSTGKPKGTL--LTHKGV----------LNLVEWRNEVFQISPndkvTQFYsHSFDSSVSEIFSTLlnGAELYLLsdeQR 1750
Cdd:PRK13391  164 GTTGRPKGIKrpLPEQPPdtplpltaflQRLWGFRSDMVYLSP----APLY-HSAPQRAVMLVIRL--GGTVIVM---EH 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1751 YSTVEYAQAIQETQATISDL-PTVFFNELSTSLTKLDSEKIRSLRFIIMGgeAA------STNAIRSWQntfknqvQLVN 1823
Cdd:PRK13391  234 FDAEQYLALIEEYGVTHTQLvPTMFSRMLKLPEEVRDKYDLSSLEVAIHA--AApcppqvKEQMIDWWG-------PIIH 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1824 E-YGPTEATVSAmyyfipVLEGENNL-----LGSVPIGIPisntkvHILNSYMQYCPVGCMGELYIESlGLAQGYWKQKE 1897
Cdd:PRK13391  305 EyYAATEGLGFT------ACDSEEWLahpgtVGRAMFGDL------HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPA 371


                  ....*
gi 446581728 1898 KTKQA 1902
Cdd:PRK13391  372 KTAEA 376
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 1547-1936 3.55e-13

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 75.16  E-value: 3.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIAT-----ATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYP--- 1618
Cdd:cd05921     9 PDRTWLAEregngGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlms 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1619 --EDRINYI----------VRDSEACRIITSNKFKSHLNV-------SDYKVSIIEDIYRTTINDDV-KILNK--PDDLA 1676
Cdd:cd05921    89 qdLAKLKHLfellkpglvfAQDAAPFARALAAIFPLGTPLvvsrnavAGRGAISFAELAATPPTAAVdAAFAAvgPDTVA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1677 YVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQIsPNDKVTQF-----YSHSFDSSVSeIFSTLLNGAELYLlsDEQRY 1751
Cdd:cd05921   169 KFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPF-FGEEPPVLvdwlpWNHTFGGNHN-FNLVLYNGGTLYI--DDGKP 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1752 StveyAQAIQETQATISDL-PTVFFN------ELSTSLTK---LDSEKIRSLRFIIMGGEAASTNAIRSWQN----TFKN 1817
Cdd:cd05921   245 M----PGGFEETLRNLREIsPTVYFNvpagweMLVAALEKdeaLRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1818 QVQLVNEYGPTE-ATVSAMYYFIPVLEGEnnllgsvpIGIPISNTKVHILnsymqycPVGCMGELYIESLGLAQGYWKQK 1896
Cdd:cd05921   321 RIPMMAGLGATEtAPTATFTHWPTERSGL--------IGLPAPGTELKLV-------PSGGKYEVRVKGPNVTPGYWRQP 385

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 446581728 1897 EKTKQAFISNPFsednskrlYRTGDLVRWL----PNGNIEFMGR 1936
Cdd:cd05921   386 ELTAQAFDEEGF--------YCLGDAAKLAdpddPAKGLVFDGR 421
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 1674-2026 5.60e-13

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 72.44  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1674 DLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSdeqRYST 1753
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFNP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1754 VEYAQAIQETQAT-ISDLPTVFFNELSTSLTKLdseKIRSlrfIIMGGEAASTNAIRSWQNTFkNQVQLVNEYGPTEATv 1832
Cdd:cd17633    78 KSWIRKINQYNATvIYLVPTMLQALARTLEPES---KIKS---IFSSGQKLFESTKKKLKNIF-PKANLIEFYGTSELS- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1833 samyyFIPVL-EGENNLLGSVpiGIPISNTKVHILNSymqycPVGCMGELYIESLGLAQGYWKQKEKTKQAFISnpfsed 1911
Cdd:cd17633   150 -----FITYNfNQESRPPNSV--GRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGWMS------ 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1912 nskrlyrTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKtvdGIG 1988
Cdd:cd17633   212 -------VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVvgiPDARFGEIAVALYS---GDK 281

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 446581728 1989 IEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:cd17633   282 LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 483-969 6.25e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 74.21  E-value: 6.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  483 PNQIAISMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSItMEREIDTIVWI-LGILKSGGVYVPIDPKFPEKRIEYI 561
Cdd:PRK08162   32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAV-LLPNIPAMVEAhFGVPMAGAVLNTLNTRLDAASIAFM 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  562 LKDSESQMIITKKEYRGLVERFA-----------------------IHTIYLEDFHYANSIENIASTHTIE-DAAYIIYT 617
Cdd:PRK08162  111 LRHGEAKVLIVDTEFAEVAREALallpgpkplvidvddpeypggrfIGALDYEAFLASGDPDFAWTLPADEwDAIALNYT 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  618 SGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQfatiifdasimeIFPILLCGGRMHLISeiekrsaeefinVSQ 697
Cdd:PRK08162  191 SGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLW------------TLPMFHCNGWCFPWT------------VAA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  698 KYGiTNVVL----PTAFFKLIAD------------------MPKEMLLKLNSVKRLFVGGETlPAESVRKWQSKLGLKip 755
Cdd:PRK08162  247 RAG-TNVCLrkvdPKLIFDLIREhgvthycgapivlsalinAPAEWRAGIDHPVHAMVAGAA-PPAAVIAKMEEIGFD-- 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  756 VLNAYGPTET----TVCATmyevngeiQKEISNIPIGKPIA-----------NSEVFVISPfNTLCP----SGVVGELFI 816
Cdd:PRK08162  323 LTHVYGLTETygpaTVCAW--------QPEWDALPLDERAQlkarqgvryplQEGVTVLDP-DTMQPvpadGETIGEIMF 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  817 GGDGVANGYLNQKEKTEGAFISldksynrdkKMYCTGDLVRLLANGNLEFIGR-KDnqVKIR-GYRIELDEIEGTLFKHP 894
Cdd:PRK08162  394 RGNIVMKGYLKNPKATEEAFAG---------GWFHTGDLAVLHPDGYIKIKDRsKD--IIISgGENISSIEVEDVLYRHP 462

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  895 EVRDAVVFTYQNDK---IVCFYLS-KDNTELKQEALKTFLSESLPDFMMPNYIFhLESFPVSPSGKLDRKKLELQIPSL 969
Cdd:PRK08162  463 AVLVAAVVAKPDPKwgeVPCAFVElKDGASATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVLREQAKSL 540
PRK09274 PRK09274
peptide synthase; Provisional
 1545-1949 9.95e-13

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 73.39  E-value: 9.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIAT----------ATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAayIPI- 1613
Cdd:PRK09274   18 ERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA--VPVl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1614 -----DVKypedRINYIVRDSEA-----------CRIITSNKFKShlnvSDYKVSI----------IEDIYRTTINDDVK 1667
Cdd:PRK09274   96 vdpgmGIK----NLKQCLAEAQPdafigipkahlARRLFGWGKPS----VRRLVTVggrllwggttLATLLRDGAAAPFP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1668 I-LNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDkvtqfyshsFDSSVSEIFStlLNGAELYLLS 1746
Cdd:PRK09274  168 MaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGE---------IDLPTFPLFA--LFGPALGMTS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1747 -----DEQRYSTVEYA---QAIQETQATisdlpTVFFN-ELSTSLT---KLDSEKIRSLRFIIMGGEAASTNAIRSWQNT 1814
Cdd:PRK09274  237 vipdmDPTRPATVDPAklfAAIERYGVT-----NLFGSpALLERLGrygEANGIKLPSLRRVISAGAPVPIAVIERFRAM 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1815 FKNQVQLVNEYGPTEAtvsamyyfIPV--LEGENNLLGSVPI---------GIPISNTKVHILN---------SYMQYCP 1874
Cdd:PRK09274  312 LPPDAEILTPYGATEA--------LPIssIESREILFATRAAtdngagicvGRPVDGVEVRIIAisdapipewDDALRLA 383

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1875 VGCMGELYIESLGLAQGYWKQKEKTKQAFIsnpfSEDNSKRLYRTGDLVRWLPNGNIEFMGRKdkqvkirGHRIE 1949
Cdd:PRK09274  384 TGEIGEIVVAGPMVTRSYYNRPEATRLAKI----PDGQGDVWHRMGDLGYLDAQGRLWFCGRK-------AHRVE 447
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 852-1060 1.06e-12

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 71.32  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  852 TGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF-----TYQNDKIVCFYLSKDNTELKQEAL 926
Cdd:COG3433    81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAvlaalRGAGVGLLLIVGAVAALDGLAAAA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  927 KTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLElqiPSLLENMQKQYVPP-----ISETEKRLAKTWAEILNLGKY 1001
Cdd:COG3433   161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAP---ALAAAEALLAAASPapaleTALTEEELRADVAELLGVDPE 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728 1002 RIGRDDDFFKLGGHSLIAVQVLNQIQKEfHLKIEIRDIFEHTTIASLSAYIDKLMAVNH 1060
Cdd:COG3433   238 EIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1671-2033 2.30e-12

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 72.82  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1671 KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKvtqFYS-----HSFDSSVSeIFSTLLNGAELYLL 1745
Cdd:PRK08043  363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDR---FMSalplfHSFGLTVG-LFTPLLTGAEVFLY 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1746 SDEQRYSTVeyAQAIQETQATISDLPTVFFNELSTSLTKLDSEKirsLRFIIMGGEAASTNAIRSWQNTFKnqVQLVNEY 1825
Cdd:PRK08043  439 PSPLHYRIV--PELVYDRNCTVLFGTSTFLGNYARFANPYDFAR---LRYVVAGAEKLQESTKQLWQDKFG--LRILEGY 511

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1826 GPTEATvsamyyfiPVlegennllgsVPIGIPISnTKVHIlnsymqycpVGCM-----------------GELYIESLGL 1888
Cdd:PRK08043  512 GVTECA--------PV----------VSINVPMA-AKPGT---------VGRIlpgmdarllsvpgieqgGRLQLKGPNI 563

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1889 AQGYWKQKektKQAFISNPFSEDNSKRL----YRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGIS 1964
Cdd:PRK08043  564 MNGYLRVE---KPGVLEVPTAENARGEMergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDK 640

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446581728 1965 Q-AVVTQTEG--GMLLQAYykTVDGiGIEKNKL-AIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKI 2033
Cdd:PRK08043  641 QhATAIKSDAskGEALVLF--TTDS-ELTREKLqQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 1545-2025 2.55e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 72.08  E-value: 2.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK06164   22 ARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSNKFKShlnvSDYkVSIIEDI------------------------------------YRTTINDDVKI 1668
Cdd:PRK06164  102 ILGRGRARWLVVWPGFKG----IDF-AAILAAVppdalpplraiavvddaadatpapapgarvqlfalpDPAPPAAAGER 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1669 LNKPDDLAYVIYTSGSTGKPK------GTLLTHkgvlnlvewrnevfqispNDKVTQFYSHSFDSSVSEI--------FS 1734
Cdd:PRK06164  177 AADPDAGALLFTTSGTTSGPKlvlhrqATLLRH------------------ARAIARAYGYDPGAVLLAAlpfcgvfgFS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1735 TLL----NGAELYLlsdEQRYSTVEYAQAIQETQATisdlPTVFFNELSTSLTKLDSEK--IRSLRFIIMGGEAASTNAI 1808
Cdd:PRK06164  239 TLLgalaGGAPLVC---EPVFDAARTARALRRHRVT----HTFGNDEMLRRILDTAGERadFPSARLFGFASFAPALGEL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1809 RSWQNTfkNQVQLVNEYGPTE--ATVSAMYYFIPVLEGENnllgsvPIGIPIS-NTKVHILNSYM-QYCPVGCMGELYIE 1884
Cdd:PRK06164  312 AALARA--RGVPLTGLYGSSEvqALVALQPATDPVSVRIE------GGGRPASpEARVRARDPQDgALLPDGESGEIEIR 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1885 SLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGI- 1963
Cdd:PRK06164  384 APSLMRGYLDNPDATARALTDDGY--------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVa 455

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728 1964 -SQAVVTQTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPIT--ANG-KI 2025
Cdd:PRK06164  456 aAQVVGATRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKI 521
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
495-968 2.71e-12

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 72.37  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  495 ITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIITKK 574
Cdd:PRK06060   31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  575 EYRglvERFAIHTIY--LEDFHYANSIEniASTHTI---EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVI-NTFHLG 648
Cdd:PRK06060  111 ALR---DRFQPSRVAeaAELMSEAARVA--PGGYEPmggDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  649 KEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKrSAEEFINVSQK------YGITNvvlptaFFKLIADMPKEML 722
Cdd:PRK06060  186 PEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPV-TPEAAAILSARfgpsvlYGVPN------FFARVIDSCSPDS 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  723 LKlnSVKRLFVGGETLPAESVRKWQSKLGlKIPVLNAYGPTETTvcatmyevngeiQKEISNI-------PIGKPIANSE 795
Cdd:PRK06060  259 FR--SLRCVVSAGEALELGLAERLMEFFG-GIPILDGIGSTEVG------------QTFVSNRvdewrlgTLGRVLPPYE 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  796 VFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEK--TEGAFISldksynrdkkmycTGDLVRLLANGNLEFIGRKDNQ 873
Cdd:PRK06060  324 IRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSpvANEGWLD-------------TRDRVCIDSDGWVTYRCRADDT 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  874 VKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN----DKIVCFYLSKDNTELKQEALKTF---LSESLPDFMMPNYIFHL 946
Cdd:PRK06060  391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAVREstgaSTLQAFLVATSGATIDGSVMRDLhrgLLNRLSAFKVPHRFAVV 470

                         490       500
                  ....*....|....*....|..
gi 446581728  947 ESFPVSPSGKLDRKKLELQIPS 968
Cdd:PRK06060  471 DRLPRTPNGKLVRGALRKQSPT 492
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 1553-2025 4.21e-12

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 71.41  E-value: 4.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1553 ATATESLTYRQLNMSSNQVAQHLLEK-GIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEA 1631
Cdd:PLN02574   61 SSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSV 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1632 CRIITS----NKFKShLNVSDYKV---------SIIEDIYRTTINDDVKILNKP----DDLAYVIYTSGSTGKPKGTLLT 1694
Cdd:PLN02574  141 GLAFTSpenvEKLSP-LGVPVIGVpenydfdskRIEFPKFYELIKEDFDFVPKPvikqDDVAAIMYSSGTTGASKGVVLT 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1695 HKGVLNLVE----WRNEVFQISPNDKV-----TQFYSHSFDSSVSEIFSTllnGAELYLLsdeQRYSTVEYAQAIQETQA 1765
Cdd:PLN02574  220 HRNLIAMVElfvrFEASQYEYPGSDNVylaalPMFHIYGLSLFVVGLLSL---GSTIVVM---RRFDASDMVKVIDRFKV 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1766 TisDLPTV--FFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYFipvle 1843
Cdd:PLN02574  294 T--HFPVVppILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPH-VDFIQGYGMTESTAVGTRGF----- 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1844 GENNLLGSVPIGIPISNTKVHILN-SYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDL 1922
Cdd:PLN02574  366 NTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW--------LRTGDI 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1923 VRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQT---EGGMLLQAYYKTVDGIGIEKNKLAIHLS 1999
Cdd:PLN02574  438 AYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVpdkECGEIPVAFVVRRQGSTLSQEAVINYVA 517

                         490       500
                  ....*....|....*....|....*.
gi 446581728 2000 NVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PLN02574  518 KQVAPYKKVRKVVFVQSIPKSPAGKI 543
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 470-962 4.31e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 71.25  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  470 TLDQLidLQALKSPNQIAISMGDQSITYYELQQRSNQIVNYLRenDLKKGQR---VSITMEREIDTIVWILGILKSGGVY 546
Cdd:PRK07867    6 TVAEL--LLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALR--ARLDPTRpphVGVLLDNTPEFSLLLGAAALSGIVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  547 VPIDPKfpeKRIEYILKD---SESQMIITKKEYRGLVE--RFAIHTIYLEDFHYANSI------ENIASTHTIEDAAYII 615
Cdd:PRK07867   82 VGLNPT---RRGAALARDiahADCQLVLTESAHAELLDglDPGVRVINVDSPAWADELaahrdaEPPFRVADPDDLFMLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  616 YTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIF-PILLCGGRMHLiseIEKRSAEEFIN 694
Cdd:PRK07867  159 FTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWaVALAAGASIAL---RRKFSASGFLP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  695 VSQKYGIT--NVV-LPTAFFKLIADMPKEmllKLNSVKRLFvGGETLPAEsVRKWQSKLGLKipVLNAYGPTETTVCatm 771
Cdd:PRK07867  236 DVRRYGATyaNYVgKPLSYVLATPERPDD---ADNPLRIVY-GNEGAPGD-IARFARRFGCV--VVDGFGSTEGGVA--- 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  772 yevngeIQKEISNIP--IGKPIANseVFVISP-FNTLCPSGV------------VGELF-IGGDGVANGYLNQKEKTEGA 835
Cdd:PRK07867  306 ------ITRTPDTPPgaLGPLPPG--VAIVDPdTGTECPPAEdadgrllnadeaIGELVnTAGPGGFEGYYNDPEADAER 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  836 FisldksynRDkKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQN----DKIVC 911
Cdd:PRK07867  378 M--------RG-GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpvvgDQVMA 448

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446581728  912 FYLSKDNTELKQEALKTFLSESlPDF---MMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK07867  449 ALVLAPGAKFDPDAFAEFLAAQ-PDLgpkQWPSYVRVCAELPRTATFKVLKRQL 501
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 1532-2025 5.55e-12

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 71.01  E-value: 5.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1532 FQNIQEQFYMQVDRQPERIAIATATESLTYRQLNMSSNQVAQHLLEK-GIKRGDKVAIFLDRSMNSIVSMLGILKAGAAY 1610
Cdd:PRK12492   23 YKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1611 IPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLN--VSDYKVS-IIE----DIYRT-------TINDDVKIL------- 1669
Cdd:PRK12492  103 VNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQevLPDTGIEyLIEakmgDLLPAakgwlvnTVVDKVKKMvpayhlp 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1670 ----------------NKP-----DDLAYVIYTSGSTGKPKGTLLTHKG-VLNLVEWRNEVFQISPNdkvtqfySHSFDS 1727
Cdd:PRK12492  183 qavpfkqalrqgrglsLKPvpvglDDIAVLQYTGGTTGLAKGAMLTHGNlVANMLQVRACLSQLGPD-------GQPLMK 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1728 SVSEIFSTLLNGAELYLLSDEQRYSTVEYAQAIQETQAtiSDLPTvFFNELS----TSLTKL--------DSEKIRSLRF 1795
Cdd:PRK12492  256 EGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNP--RDIPG-FIKELGkwrfSALLGLntlfvalmDHPGFKDLDF 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1796 IIM-----GGEAASTNAIRSWQNTfkNQVQLVNEYGPTEAT--VSAMYYfipvleGENNLLGSVpiGIPISNTKVHILNS 1868
Cdd:PRK12492  333 SALkltnsGGTALVKATAERWEQL--TGCTIVEGYGLTETSpvASTNPY------GELARLGTV--GIPVPGTALKVIDD 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1869 YMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFisnpfsedNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRI 1948
Cdd:PRK12492  403 DGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL--------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNV 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1949 ELGEIEDAMLQLEGISQAV---VTQTEGGMLLQAYYKTVDGiGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK12492  475 YPNEIEDVVMAHPKVANCAaigVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
PLN02246 PLN02246
4-coumarate--CoA ligase
 1532-1835 8.02e-12

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 70.39  E-value: 8.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1532 FQNIQEqfymqVDRQPERIAIATAtESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYI 1611
Cdd:PLN02246   30 FERLSE-----FSDRPCLIDGATG-RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1612 PIDVKYPEDRINYIVRDSEACRIIT----SNKFKSHLNVSDYKVSIIEDI------YRTTINDD------VKIlnKPDDL 1675
Cdd:PLN02246  104 TANPFYTPAEIAKQAKASGAKLIITqscyVDKLKGLAEDDGVTVVTIDDPpegclhFSELTQADenelpeVEI--SPDDV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1676 AYVIYTSGSTGKPKGTLLTHKG----VLNLVEWRNEVFQISPNDKV----TQFYSHSFDSSvseIFSTLLNGAELYLLsd 1747
Cdd:PLN02246  182 VALPYSSGTTGLPKGVMLTHKGlvtsVAQQVDGENPNLYFHSDDVIlcvlPMFHIYSLNSV---LLCGLRVGAAILIM-- 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1748 eQRYSTVEYAQAIQETQATISDL--PTVFFNELSTSLTKLDsekIRSLRFIIMGgeAAS-----TNAIRSwqnTFKNQVq 1820
Cdd:PLN02246  257 -PKFEIGALLELIQRHKVTIAPFvpPIVLAIAKSPVVEKYD---LSSIRMVLSG--AAPlgkelEDAFRA---KLPNAV- 326

                         330
                  ....*....|....*.
gi 446581728 1821 LVNEYGPTEA-TVSAM 1835
Cdd:PLN02246  327 LGQGYGMTEAgPVLAM 342
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
609-958 9.13e-12

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 70.89  E-value: 9.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQfATIIFDASIMEI--FPILLCGGRMHLI-SEIE 685
Cdd:PRK08043  365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMS-ALPLFHSFGLTVglFTPLLTGAEVFLYpSPLH 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  686 KRSAEEFI---NVSQKYGiTNVVL--------PTAFFKLiadmpkemllklnsvkRLFVGGETLPAESVRK-WQSKLGLK 753
Cdd:PRK08043  444 YRIVPELVydrNCTVLFG-TSTFLgnyarfanPYDFARL----------------RYVVAGAEKLQESTKQlWQDKFGLR 506

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  754 IpvLNAYGPTEttvCATMYEVNGEIQKEISNIpiGKPIANSEVFVISPfntlcpSGVV--GELFIGGDGVANGYLN---- 827
Cdd:PRK08043  507 I--LEGYGVTE---CAPVVSINVPMAAKPGTV--GRILPGMDARLLSV------PGIEqgGRLQLKGPNIMNGYLRvekp 573

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  828 ------QKEKTEGafisldksyNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFK-HPEVRDAV 900
Cdd:PRK08043  574 gvlevpTAENARG---------EMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKQHAT 644

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  901 VFTYQNDKIVCFYLSKDNTELKQEALKTFLSES-LPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:PRK08043  645 AIKSDASKGEALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 1557-1969 1.41e-11

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 69.80  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1557 ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIdvkYPE---DRINYIVRDSEaCR 1633
Cdd:cd05932     5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTlnpDTIRYVLEHSE-SK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1634 IITSNKFKSHLN----VSDYKVSIIEDIYRTTINDDV-------------KILNKPDDLAYVIYTSGSTGKPKGTLLTHK 1696
Cdd:cd05932    81 ALFVGKLDDWKAmapgVPEGLISISLPPPSAANCQYQwddliaqhppleeRPTRFPEQLATLIYTSGTTGQPKGVMLTFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1697 GVLNLVEWRNEVFQISPNDKVTQFY--SHSFDSSVSEIfSTLLNGAELYLLsdEQRYSTVEYAQAIQET----------- 1763
Cdd:cd05932   161 SFAWAAQAGIEHIGTEENDRMLSYLplAHVTERVFVEG-GSLYGGVLVAFA--ESLDTFVEDVQRARPTlffsvprlwtk 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1764 --QATISDLPTVFFNEL-----STSLTK------LDSEKIRslrfIIMGGEAASTNAIRSWqntFKNQVQLVNE-YGPTE 1829
Cdd:cd05932   238 fqQGVQDKIPQQKLNLLlkipvVNSLVKrkvlkgLGLDQCR----LAGCGSAPVPPALLEW---YRSLGLNILEaYGMTE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1830 A-TVSAMYYfipvlEGENNLlGSVpiGIPISNTKVHIlnsymqycpvGCMGELYIESLGLAQGYWKQKEKTKQAFISNPF 1908
Cdd:cd05932   311 NfAYSHLNY-----PGRDKI-GTV--GNAGPGVEVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTADGF 372

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728 1909 sednskrlYRTGDLVRWLPNGNIEFMGRKDKQVKI-RGHRIELGEIEDAMLQLEGISQAVVT 1969
Cdd:cd05932   373 --------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 610-962 1.46e-11

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 69.77  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVV--NLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEkr 687
Cdd:cd05915   154 AACGMAYTTGTTGLPKGVVYSHRALVlhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRL-- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  688 SAEEFINVSQKYGITNVVLPTAFFKLIADmpkemllKLNSVKRLF------VGGETLPAESVRKWQsKLGlKIPVLNAYG 761
Cdd:cd05915   232 DPASLVELFDGEGVTFTAGVPTVWLALAD-------YLESTGHRLktlrrlVVGGSAAPRSLIARF-ERM-GVEVRQGYG 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  762 PTET----TVCATMYEVNGEIQKEISNIPIGKPIAN--SEVFVISPFNTLCP--SGVVGELFIGGDGVANGYLNQKEKTE 833
Cdd:cd05915   303 LTETspvvVQNFVKSHLESLSEEEKLTLKAKTGLPIplVRLRVADEEGRPVPkdGKALGEVQLKGPWITGGYYGNEEATR 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  834 GAFISLDKSYNRDKKMyctgdlvrLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKI---V 910
Cdd:cd05915   383 SALTPDGFFRTGDIAV--------WDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWqerP 454

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446581728  911 CFYLSKDNTELKQEALKTFLSESLPDF-MMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:cd05915   455 LAVVVPRGEKPTPEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRAL 507
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 1545-1936 2.00e-11

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 69.52  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATAT-----ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFldrSMNSI---VSMLGILKAGAAYIPIDVK 1616
Cdd:PRK08180   51 EAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMIL---SGNSIehaLLALAAMYAGVPYAPVSPA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1617 Y---PED--RINYIVR-----------------------DSEACRIITSNKFKSHLNVSdykvsiIEDIYRTTINDDVKI 1668
Cdd:PRK08180  128 YslvSQDfgKLRHVLElltpglvfaddgaafaralaavvPADVEVVAVRGAVPGRAATP------FAALLATPPTAAVDA 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1669 LNK---PDDLAYVIYTSGSTGKPKGTLLTHKGV-LN-----------------LVEWrnevfqiSPndkvtqfYSHSFDS 1727
Cdd:PRK08180  202 AHAavgPDTIAKFLFTSGSTGLPKAVINTHRMLcANqqmlaqtfpflaeeppvLVDW-------LP-------WNHTFGG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1728 SVseIFS-TLLNGAELYLlsDEQRYStveyAQAIQETQATISDL-PTVFFN------ELSTSLTKlDSEKIRS----LRF 1795
Cdd:PRK08180  268 NH--NLGiVLYNGGTLYI--DDGKPT----PGGFDETLRNLREIsPTVYFNvpkgweMLVPALER-DAALRRRffsrLKL 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1796 IIMGGEAASTNAirsW-------QNTFKNQVQLVNEYGPTEATVSAMYyfipvLEGENNLLGsvPIGIPISNTKVHILns 1868
Cdd:PRK08180  339 LFYAGAALSQDV---WdrldrvaEATCGERIRMMTGLGMTETAPSATF-----TTGPLSRAG--NIGLPAPGCEVKLV-- 406

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728 1869 ymqycPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWL----PNGNIEFMGR 1936
Cdd:PRK08180  407 -----PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY--------YRSGDAVRFVdpadPERGLMFDGR 465
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 1512-1968 1.24e-10

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 66.93  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1512 SQEEESLYKKVnHTERPYPYFQNIQEQFYMQVDRQPERIAIATAT--ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIF 1589
Cdd:PLN02330    8 QEDNEHIFRSR-YPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVtgKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1590 LDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKIL 1669
Cdd:PLN02330   87 LPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEEKIEGAVNWKELL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1670 NKPD--------------DLAYVIYTSGSTGKPKGTLLTHKG-VLNLVewrNEVFQISPN--DKVTQF----YSHSFdSS 1728
Cdd:PLN02330  167 EAADragdtsdneeilqtDLCALPFSSGTTGISKGVMLTHRNlVANLC---SSLFSVGPEmiGQVVTLglipFFHIY-GI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1729 VSEIFSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATISDL-PTVFFNELSTSLT-KLDSEKIRsLRFIIMGGEAASTN 1806
Cdd:PLN02330  243 TGICCATLRNKGKVVVMS---RFELRTFLNALITQEVSFAPIvPPIILNLVKNPIVeEFDLSKLK-LQAIMTAAAPLAPE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1807 AIRSWQNTFKNqVQLVNEYGPTEATVSAMYYFIPvlEGENNLLGSVPIGIPISNTKVHILNSYM-QYCPVGCMGELYIES 1885
Cdd:PLN02330  319 LLTAFEAKFPG-VQVQEAYGLTEHSCITLTHGDP--EKGHGIAKKNSVGFILPNLEVKFIDPDTgRSLPKNTPGELCVRS 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1886 LGLAQGYWKQKEKTKQAFisnpfseDNSKRLYrTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQ 1965
Cdd:PLN02330  396 QCVMQGYYNNKEETDRTI-------DEDGWLH-TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVED 467


                  ...
gi 446581728 1966 AVV 1968
Cdd:PLN02330  468 AAV 470
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 1547-2025 1.76e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 66.19  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATAT--ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK13390   11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSNKFKSHLNVS----DYKVSIIEDI-----YRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTL--L 1693
Cdd:PRK13390   91 IVGDSGARVLVASAALDGLAAKVgadlPLRLSFGGEIdgfgsFEAALAGAGPRLTEQPCGAVMLYSSGTTGFPKGIQpdL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1694 THKGVlnlvewrnevfqISPNDKVTQFYSHSFDSSVSEIF---STLLNGAELYLLSD----------EQRYSTVEYAQAI 1760
Cdd:PRK13390  171 PGRDV------------DAPGDPIVAIARAFYDISESDIYyssAPIYHAAPLRWCSMvhalggtvvlAKRFDAQATLGHV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1761 QETQATISDL-PTVFfnelsTSLTKLDSE-----KIRSLRFIIMGGEAASTNAIRSwqntfknqvqLVNEYGPT--EATV 1832
Cdd:PRK13390  239 ERYRITVTQMvPTMF-----VRLLKLDADvrtryDVSSLRAVIHAAAPCPVDVKHA----------MIDWLGPIvyEYYS 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1833 SAMYYFIPVLEGENNLLGSVPIGIPISNTkVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQA-FISNPFsed 1911
Cdd:PRK13390  304 STEAHGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAqHPAHPF--- 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1912 nskrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT---QTEGGMLLQAYYKTVDGIG 1988
Cdd:PRK13390  380 ----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgvpDPEMGEQVKAVIQLVEGIR 455

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 446581728 1989 iEKNKLAIHLSNV----LPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK13390  456 -GSDELARELIDYtrsrIAHYKAPRSVEFVDELPRTPTGKL 495
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
 2163-2375 1.95e-10

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 64.76  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLPSTTIYCLVRENEDQVIGAKLKERMEFyfgkeilqklkervelIEGDLslmnlgldsK 2242
Cdd:cd05241     1 SVLVTGGSGFFGERLVKQLLERGGTYVRSFDIAPPGEALSAWQHPNIEF----------------LKGDI---------T 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2243 QLDHLKKNVESI---IHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVV--GQAERDPKEFEFFES 2316
Cdd:cd05241    56 DRNDVEQALSGAdcvFHTAAIVPLAGPRDLYWEVNVGGTQNVLDACQRCGVqKFVYTSSSSVIfgGQNIHNGDETLPYPP 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581728 2317 DFdrgqnlDNLYLESKFQGEKMVREAMEKGV-------RATIY------RVGNLVGNSKTG--KFQYNINENAF 2375
Cdd:cd05241   136 LD------SDMYAETKAIAEIIVLEANGRDDlltcalrPAGIFgpgdqgLVPILFEWAEKGlvKFVFGRGNNLV 203
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 1559-1946 2.56e-10

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 65.92  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1559 LTYRQLNMSSNQVAQHLlEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVkyPE-----DRINYIVRDSEACR 1633
Cdd:PRK12476   69 LTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFA--PElpghaERLDTALRDAEPTV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1634 IITS-------NKFKSHLNVSDY-KVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGV-LNLVEW 1704
Cdd:PRK12476  146 VLTTtaaaeavEGFLRNLPRLRRpRVIAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVgTNLVQM 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1705 rneVFQISPNDKVTQFYS-----HsfDSSVSEIFSTLLNGAELYLLSD------EQRYstveyaqaIQETQATISDLPTV 1773
Cdd:PRK12476  226 ---ILSIDLLDRNTHGVSwlplyH--DMGLSMIGFPAVYGGHSTLMSPtafvrrPQRW--------IKALSEGSRTGRVV 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1774 -----FFNELSTS--LTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFK----NQVQLVNEYGPTEATV---------- 1832
Cdd:PRK12476  293 taapnFAYEWAAQrgLPAEGDDIDLSNVVLIIGSEPVSIDAVTTFNKAFApyglPRTAFKPSYGIAEATLfvatiapdae 372

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1833 -SAMY---------YFIPVLEGENNLLGSVPIGIPISNTKVHILNSYM-QYCPVGCMGELYIESLGLAQGYWKQKEKTKQ 1901
Cdd:PRK12476  373 pSVVYldreqlgagRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETER 452

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1902 AFI----------SNPFSEDNSKRLYRTGDLVRWLpNGNIEFMGRKDKQVKIRGH 1946
Cdd:PRK12476  453 TFGaklqsrlaegSHADGAADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGR 506
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 1560-1963 2.88e-10

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 65.81  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1560 TYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNK 1639
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1640 -----FKSHLNVSDYKVSIIE--DIYRTTINDDVKI----------------------LNKPDDLAYVIYTSGSTGKPKG 1690
Cdd:PLN02614  161 kiselFKTCPNSTEYMKTVVSfgGVSREQKEEAETFglviyawdeflklgegkqydlpIKKKSDICTIMYTSGTTGDPKG 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1691 TLLTHK-------GVLNLVEWRNEvfQISPNDKVTQFY--SHSFDSSVSEIFstLLNGAEL--------YLLSD------ 1747
Cdd:PLN02614  241 VMISNEsivtliaGVIRLLKSANA--ALTVKDVYLSYLplAHIFDRVIEECF--IQHGAAIgfwrgdvkLLIEDlgelkp 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1748 ----------EQRYSTVEYAQA--------------------IQETQATISDLPtvFFNELSTSLTKLD-SEKIRslrfI 1796
Cdd:PLN02614  317 tifcavprvlDRVYSGLQKKLSdggflkkfvfdsafsykfgnMKKGQSHVEASP--LCDKLVFNKVKQGlGGNVR----I 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1797 IMGGEAASTNAIRSWQNTFKNqVQLVNEYGPTEATVSAMYYFipvlEGENNLLGSVpiGIPISNTKVHILN-SYMQYCPV 1875
Cdd:PLN02614  391 ILSGAAPLASHVESFLRVVAC-CHVLQGYGLTESCAGTFVSL----PDELDMLGTV--GPPVPNVDIRLESvPEMEYDAL 463

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1876 GCM--GELYIESLGLAQGYWKQKEKTKQAFISNpfsednskrLYRTGDLVRWLPNGNIEFMGRKDKQVKI-RGHRIELGE 1952
Cdd:PLN02614  464 ASTprGEICIRGKTLFSGYYKREDLTKEVLIDG---------WLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVEN 534

                         490
                  ....*....|.
gi 446581728 1953 IEDAMLQLEGI 1963
Cdd:PLN02614  535 IENIYGEVQAV 545
PRK05857 PRK05857
fatty acid--CoA ligase;
471-962 2.99e-10

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 65.41  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  471 LDQLIDlQALKSPNQIAI--SMGDQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVP 548
Cdd:PRK05857   17 LDRVFE-QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  549 IDPKFPEKRIEYILKDSESQMIITKKEYR--------GLVERFAIHTIYLEDFHYANSIENIASTHT-----IEDAAYII 615
Cdd:PRK05857   96 ADGNLPIAAIERFCQITDPAAALVAPGSKmassavpeALHSIPVIAVDIAAVTRESEHSLDAASLAGnadqgSEDPLAMI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  616 YTSGSTGLPKGVVVPHKG------------------VVN-LSYSVINTFHLGkedvflqfatiifdaSIMEIFPILLCGG 676
Cdd:PRK05857  176 FTSGTTGEPKAVLLANRTffavpdilqkeglnwvtwVVGeTTYSPLPATHIG---------------GLWWILTCLMHGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  677 RmhLISEIEKRSAEEFINVSQKYGITNVVlPTAFFKLIADMpKEMLLKLNSVKRLFVGGETLPAESVRKWQSKlGLKipV 756
Cdd:PRK05857  241 L--CVTGGENTTSLLEILTTNAVATTCLV-PTLLSKLVSEL-KSANATVPSLRLVGYGGSRAIAADVRFIEAT-GVR--T 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  757 LNAYGPTETTVCATMYEVNGEIQKEISNIPIGKPIANSEVFVISP------FNTLCPSGVVGELFIGGDGVANGYLNQKE 830
Cdd:PRK05857  314 AQVYGLSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATdgigptAPGAGPSASFGTLWIKSPANMLGYWNNPE 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  831 KTEGAFIslDKSYNrdkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDK-- 908
Cdd:PRK05857  394 RTAEVLI--DGWVN-------TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEfg 464

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728  909 -------IVCFYLSKDNT-ELKQEALKTFLSESlPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK05857  465 alvglavVASAELDESAArALKHTIAARFRRES-EPMARPSTIVIVTDIPRTQSGKVMRASL 525
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 20-323 3.00e-10

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 65.14  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   20 QEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKKRDEKIKQLI--QKNVEFDIPIKDLTA 97
Cdd:cd19540     8 QQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLTVVDVTE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   98 FKNTEQksilknfLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGksnve 177
Cdd:cd19540    88 DELAAR-------LAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAG----- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  178 fESP--------YKN--LVKHE----ESFIDSAIYKEgSSYWKDYLQG---ELT-PT---------------EFPIDfnk 224
Cdd:cd19540   156 -RAPdwaplpvqYADyaLWQREllgdEDDPDSLAARQ-LAYWRETLAGlpeELElPTdrprpavasyrggtvEFTID--- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  225 mnekrytdkniskninSDLFYQIQCFAKKNNISIYRVMLSTYCTLLHQMTNAEEIIVGIPINTRpyTEER--NTFGYFVN 302
Cdd:cd19540   231 ----------------AELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGR--GDEAldDLVGMFVN 292

                         330       340
                  ....*....|....*....|.
gi 446581728  303 TLPIRITIEKGETFKGILNKV 323
Cdd:cd19540   293 TLVLRTDVSGDPTFAELLARV 313
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 1556-2025 3.01e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 65.53  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1556 TESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPI----DVKYPEDRINYIVRDsea 1631
Cdd:PTZ00237   90 TIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLfdgySVKSLIDRIETITPK--- 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1632 cRIITSN-------------KFKSHLNVSDYKVSIIEDIYRTTIND--DVKILNK----PDDLA---------------- 1676
Cdd:PTZ00237  167 -LIITTNygilndeiitftpNLKEAIELSTFKPSNVITLFRNDITSesDLKKIETiptiPNTLSwydeikkikennqspf 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1677 ------------YVIYTSGSTGKPKGTLLTHKGvlNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSeiFSTLLNGaelyL 1744
Cdd:PTZ00237  246 yeyvpvesshplYILYTSGTTGNSKAVVRSNGP--HLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS--FHGFLYG----S 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1745 LSDEQrySTVEYAQAIQETQATISDL-PTVFFNELSTSLT---------KLD--SEKIRS------LRFIIMGGEAASTN 1806
Cdd:PTZ00237  318 LSLGN--TFVMFEGGIIKNKHIEDDLwNTIEKHKVTHTLTlpktiryliKTDpeATIIRSkydlsnLKEIWCGGEVIEES 395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1807 AIRSWQNTFKnqVQLVNEYGPTEATVSAMYYFIPVLEGENNLlgsvpiGIPISNTKVHILNSYMQYCPVGCMGELYIE-- 1884
Cdd:PTZ00237  396 IPEYIENKLK--IKSSRGYGQTEIGITYLYCYGHINIPYNAT------GVPSIFIKPSILSEDGKELNVNEIGEVAFKlp 467

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1885 -SLGLAQGYWKQKEKTKQAFISNPfsednskRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQ---- 1959
Cdd:PTZ00237  468 mPPSFATTFYKNDEKFKQLFSKFP-------GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKhplv 540

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728 1960 LE----GISQAVVTQTEGGMLLQAYYKTVDGIGIE--KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PTZ00237  541 LEccsiGIYDPDCYNVPIGLLVLKQDQSNQSIDLNklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 613-896 3.64e-10

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 65.53  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  613 YIIYTSGSTGLPKGVVVPHKG-VVNLSYSVINTFHLGKEDVFLQFATIIFdASIMEIFPILLCGGRMHLISEI----EKR 687
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGPhLVGLKYYWRSIIEKDIPTVVFSHSSIGW-VSFHGFLYGSLSLGNTFVMFEGgiikNKH 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  688 SAEEFINVSQKYGITN-VVLPTAFFKLIADMPKEMLLK----LNSVKRLFVGGETLpAESVRKW-QSKLglKIPVLNAYG 761
Cdd:PTZ00237  337 IEDDLWNTIEKHKVTHtLTLPKTIRYLIKTDPEATIIRskydLSNLKEIWCGGEVI-EESIPEYiENKL--KIKSSRGYG 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  762 PTETTvCATMYEVNgeiqkeISNIPI---GKPIANSEVFVISPFNTLCPSGVVGELFIG---GDGVANGYLNQKEKtega 835
Cdd:PTZ00237  414 QTEIG-ITYLYCYG------HINIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEK---- 482

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728  836 fisLDKSYNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEV 896
Cdd:PTZ00237  483 ---FKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 1522-1938 3.72e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 65.52  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1522 VNHTERpypyfqNIQEQ----FYMQVDRQPERIAIATateSLTYRQLNMSSNQVAQHLlEKGIKRGDKVAIFLDRSMNSI 1597
Cdd:PRK07769   24 VRHVER------WAKVRgdklAYRFLDFSTERDGVAR---DLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1598 VSMLGILKAGAAYIPI-DVKYP--EDRINYIVRDSEACRIITSN-------KFKSHLNVSDYKVSIIEDiyrtTINDDVK 1667
Cdd:PRK07769   94 IAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTdsaegvrKFFRARPAKERPRVIAVD----AVPDEVG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1668 ILNKP-----DDLAYVIYTSGSTGKPKGTLLTHKGVL-NLVEWRNEVfQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAE 1741
Cdd:PRK07769  170 ATWVPpeaneDTIAYLQYTSGSTRIPAGVQITHLNLPtNVLQVIDAL-EGQEGDRGVSWLPFFHDMGLITVLLPALLGHY 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1742 LYLLSDE---QR-YSTV-EYAQAIQETQATISDLPTVFFNELST-SLTK-----LDSEKIRSLrfiIMGGEAASTNAIRS 1810
Cdd:PRK07769  249 ITFMSPAafvRRpGRWIrELARKPGGTGGTFSAAPNFAFEHAAArGLPKdgeppLDLSNVKGL---LNGSEPVSPASMRK 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1811 WQNTFK----NQVQLVNEYGPTEAT--VSA---------MY---------YFIPVLEGENNLLGSVPIG-IPISNTKVHI 1865
Cdd:PRK07769  326 FNEAFApyglPPTAIKPSYGMAEATlfVSTtpmdeeptvIYvdrdelnagRFVEVPADAPNAVAQVSAGkVGVSEWAVIV 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1866 LNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAF---ISNPFSEDNSK------RLYRTGDLVRWLpNGNIEFMGR 1936
Cdd:PRK07769  406 DPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSESHAEgapddaLWVRTGDYGVYF-DGELYITGR 484


                  ...
gi 446581728 1937 -KD 1938
Cdd:PRK07769  485 vKD 487
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 1547-2025 4.86e-10

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 64.63  E-value: 4.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIV 1626
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1627 RDSEACRIITSNKFkshlnvsDYKVSIIEDiyrttiNDDVKILnKPDDLAYVI---YTSGSTGKPKGTLLTHKG-----V 1698
Cdd:cd12118    98 RHSEAKVLFVDREF-------EYEDLLAEG------DPDFEWI-PPADEWDPIalnYTSGTTGRPKGVVYHHRGaylnaL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1699 LNLVEW------------------------------------RN----EVFQISPNDKVTQFyshsfdSSVSEIFSTLLN 1738
Cdd:cd12118   164 ANILEWemkqhpvylwtlpmfhcngwcfpwtvaavggtnvclRKvdakAIYDLIEKHKVTHF------CGAPTVLNMLAN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1739 GAELYLLSDEQRystveyaqaIQETQATISDLPTVFfnelstsltkldsEKIRSLRFIIMGG----EAASTNAIRSWQ-- 1812
Cdd:cd12118   238 APPSDARPLPHR---------VHVMTAGAPPPAAVL-------------AKMEELGFDVTHVygltETYGPATVCAWKpe 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1813 --------NTFKNQVQLVNEYGPTEATVsamyyfipvleGENNLLGSVPigipiSNTKVhilnsymqycpvgcMGELYIE 1884
Cdd:cd12118   296 wdelpteeRARLKARQGVRYVGLEEVDV-----------LDPETMKPVP-----RDGKT--------------IGEIVFR 345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1885 SLGLAQGYWKQKEKTKQAFisnpfsEDNskrLYRTGDLVRWLPNGNIEFMGRKdKQVKIR-GHRIELGEIEDAMLQLEGI 1963
Cdd:cd12118   346 GNIVMKGYLKNPEATAEAF------RGG---WFHSGDLAVIHPDGYIEIKDRS-KDIIISgGENISSVEVEGVLYKHPAV 415

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1964 SQAVVTQTEG---GMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYShVLEIPITANGKI 2025
Cdd:cd12118   416 LEAAVVARPDekwGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKI 479
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 51-174 5.33e-10

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 64.20  E-value: 5.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   51 EVLKKALTTIVQSHPALRTIFKKRDEKIKQLIQKNVE--FDIPIKDLTAFKNTEQksilknfLESIVNE---KFSLEEGP 125
Cdd:cd19534    37 DALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelFRLEVVDLSSLAQAAA-------IEALAAEaqsSLDLEEGP 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 446581728  126 LFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQGKS 174
Cdd:cd19534   110 LLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
 2166-2302 7.23e-10

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 63.29  E-value: 7.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2166 LTGATGYLGAHILERLLQlpsttiyclvRENE-------DQVIGAKLKErmefYFGKeilQKLKERVELIEGDLslmnlg 2238
Cdd:cd09811     4 VTGGGGFLGQHIIRLLLE----------RKEElkeirvlDKAFGPELIE----HFEK---SQGKTYVTDIEGDI------ 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728 2239 LDSKQLDHLKKNVESIIHCGGEVRHYG--EREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSVVG 2302
Cdd:cd09811    61 KDLSFLFRACQGVSVVIHTAAIVDVFGppNYEELEEVNVNGTQAVLEACVQNNVKrLVYTSSIEVAG 127
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
567-958 7.84e-10

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 64.60  E-value: 7.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  567 SQMIITKKEYRGLVE--RFAIHTIYLEDF----HYANSIEN-IASTHTI--------EDAAYIIYTSGSTGLPKGVVVPH 631
Cdd:PRK06814  736 SRAFIEKARLGPLIEalEFGIRIIYLEDVraqiGLADKIKGlLAGRFPLvyfcnrdpDDPAVILFTSGSEGTPKGVVLSH 815

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  632 KGVVNLSYSVINTFHLGKEDvflqfatIIFDAsiMEIF-----------PiLLCGGRMHLI-SEIEKRSAEEFInvsqkY 699
Cdd:PRK06814  816 RNLLANRAQVAARIDFSPED-------KVFNA--LPVFhsfgltgglvlP-LLSGVKVFLYpSPLHYRIIPELI-----Y 880

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  700 GiTN--VVLPTAFFkliadmpkemllkLN------------SVKRLFVGGETLPAESVRKWQSKLGLKIpvLNAYGPTET 765
Cdd:PRK06814  881 D-TNatILFGTDTF-------------LNgyaryahpydfrSLRYVFAGAEKVKEETRQTWMEKFGIRI--LEGYGVTET 944

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  766 TVCatmyevngeiqkeisnIPIGKPIAN--SEVFVISPfntlcpsGVV------------GELFIGGDGVANGYLnqKEK 831
Cdd:PRK06814  945 APV----------------IALNTPMHNkaGTVGRLLP-------GIEyrlepvpgidegGRLFVRGPNVMLGYL--RAE 999

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  832 TEGAFISLDKSYnrdkkmYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIE---GTLFkhPEVRDAVVFT---YQ 905
Cdd:PRK06814 1000 NPGVLEPPADGW------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEelaAELW--PDALHAAVSIpdaRK 1071

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446581728  906 NDKIVCFYLSKDNTelKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLD 958
Cdd:PRK06814 1072 GERIILLTTASDAT--RAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
 2163-2375 9.85e-10

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 62.76  E-value: 9.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLPSTTIYCL-VRENEdqvigaklkermefyfgkEILQKLKERVELIEGDLSlmnlglDS 2241
Cdd:cd09813     1 SCLVVGGSGFLGRHLVEQLLRRGNPTVHVFdIRPTF------------------ELDPSSSGRVQFHTGDLT------DP 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLD--HLKKNVESIIHCGGEVrHYGEREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSVV--GQAERDPKEfeffes 2316
Cdd:cd09813    57 QDLEkaFNEKGPNVVFHTASPD-HGSNDDLYYKVNVQGTRNVIEACRKCGVKkLVYTSSASVVfnGQDIINGDE------ 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728 2317 DFDRGQNLDNLYLESKFQGEKMVREA-----------------MEKGVRATIYRVGNLVGNSKTgKFQYNINENAF 2375
Cdd:cd09813   130 SLPYPDKHQDAYNETKALAEKLVLKAndpesglltcalrpagiFGPGDRQLVPGLLKAAKNGKT-KFQIGDGNNLF 204
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 517-836 9.97e-10

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 63.99  E-value: 9.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  517 KKGQRVSITMEREIDTIVWILGILKSGGVYVPI-DPKFP--EKRIEYILKDSESQMIITKKEYRGLVERF---------- 583
Cdd:PRK12476   90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEAVEGFlrnlprlrrp 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  584 ------AIHTIYLEDFHYANSieniasthTIEDAAYIIYTSGSTGLPKGVVVPHKGV-VNLSYSVINTFHLGKEDVFLQF 656
Cdd:PRK12476  170 rviaidAIPDSAGESFVPVEL--------DTDDVSHLQYTSGSTRPPVGVEITHRAVgTNLVQMILSIDLLDRNTHGVSW 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  657 ATIIFDAS-IMEIFPIlLCGGRMHLISEIE-KRSAEEFI---NVSQKYGITNVVLPTAFFKLIAD--MPKE-MLLKLNSV 728
Cdd:PRK12476  242 LPLYHDMGlSMIGFPA-VYGGHSTLMSPTAfVRRPQRWIkalSEGSRTGRVVTAAPNFAYEWAAQrgLPAEgDDIDLSNV 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  729 KrLFVGGETLPAESVRKWQSKL---GLKIPVLN-AYGPTETTV-CATM---------------------YEVNGEIQKEI 782
Cdd:PRK12476  321 V-LIIGSEPVSIDAVTTFNKAFapyGLPRTAFKpSYGIAEATLfVATIapdaepsvvyldreqlgagraVRVAADAPNAV 399

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  783 SNIPIGKpIANSEVFVISPFNTLC--PSGVVGELFIGGDGVANGYLNQKEKTEGAF 836
Cdd:PRK12476  400 AHVSCGQ-VARSQWAVIVDPDTGAelPDGEVGEIWLHGDNIGRGYWGRPEETERTF 454
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 47-209 1.15e-09

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 63.28  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   47 NLQIEVLKKALTTIVQSHPALRTIFkkrDEKIKQLIQKNV-EFDIPIKDLTAFKNTEQKSILKNFLESIVNEKFSLEEGP 125
Cdd:cd19535    36 DLDPDRLERAWNKLIARHPMLRAVF---LDDGTQQILPEVpWYGITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  126 LFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGEllQGKSNVEFESPYKNLVKHEESFIDSAiYKEGSSYW 205
Cdd:cd19535   113 LFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYED--PGEPLPPLELSFRDYLLAEQALRETA-YERARAYW 189


                  ....
gi 446581728  206 KDYL 209
Cdd:cd19535   190 QERL 193
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 494-869 1.24e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 63.53  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  494 SITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFP-----EKRIEYILKDSESQ 568
Cdd:PRK12582   80 KVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSlmshdHAKLKHLFDLVKPR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  569 MIITkkEYRGLVERfAIHTIYLED---FHYANSIENIASTHTIE----------DAAY----------IIYTSGSTGLPK 625
Cdd:PRK12582  160 VVFA--QSGAPFAR-ALAALDLLDvtvVHVTGPGEGIASIAFADlaatpptaavAAAIaaitpdtvakYLFTSGSTGMPK 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  626 GVVVPHK---GVVNLSYSVINTFHLGKEDVFLQF--------ATIIFDasimeifPILLCGGRMHL-------------I 681
Cdd:PRK12582  237 AVINTQRmmcANIAMQEQLRPREPDPPPPVSLDWmpwnhtmgGNANFN-------GLLWGGGTLYIddgkplpgmfeetI 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  682 SEIEKRSAEEFINVsqkygitnvvlPTAFFKLIADMPKEMLLKLNSVKRL---FVGGETLPAESVRKWQ----SKLGLKI 754
Cdd:PRK12582  310 RNLREISPTVYGNV-----------PAGYAMLAEAMEKDDALRRSFFKNLrlmAYGGATLSDDLYERMQalavRTTGHRI 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  755 PVLNAYGPTET--TVCATMY--EVNGEIqkeisnipiGKPIANSEVfvispfnTLCPSGVVGELFIGGDGVANGYLNQKE 830
Cdd:PRK12582  379 PFYTGYGATETapTTTGTHWdtERVGLI---------GLPLPGVEL-------KLAPVGDKYEVRVKGPNVTPGYHKDPE 442

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 446581728  831 KTEGAFisldksynrDKK-MYCTGDLVRLLANGNLE----FIGR 869
Cdd:PRK12582  443 LTAAAF---------DEEgFYRLGDAARFVDPDDPEkgliFDGR 477
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 603-1050 1.27e-09

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 63.95  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  603 ASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLIS 682
Cdd:COG3319   134 AAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLL 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  683 EIEKRSAEEFINVSQKYGITNVVLPTAFFKLIADMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGLKIPVLNAYGP 762
Cdd:COG3319   214 LLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGG 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  763 TETTVCATMYEVNGEIQKEISNIPIGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTEGAFISLDKS 842
Cdd:COG3319   294 TATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAG 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  843 YNRDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQNDKIVCFYLSKDNTELK 922
Cdd:COG3319   374 AGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAA 453

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  923 QEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLELQIPSLLENMQkQYVPPISETEKRLAKTWAEILNLGkyR 1002
Cdd:COG3319   454 LAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAA-AAPAPAAALELALALLLLLLLGLG--L 530

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 446581728 1003 IGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIASLSA 1050
Cdd:COG3319   531 VGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAA 578
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 2163-2360 1.40e-09

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 60.63  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLPSTTIyCLVReNEDQVigAKLKERmefyfgkeilqklkeRVELIEGDLslmnlgLDSK 2242
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLARGHPVR-ALVR-DPEKA--AALAAA---------------GVEVVQGDL------DDPE 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2243 QLDHLKKNVESIIHCggevRHYGEREHFQkVNVQSTKYLLELAKNTNV-RFHYistLSVVGqAERDPkefeffesdfdrg 2321
Cdd:COG0702    56 SLAAALAGVDAVFLL----VPSGPGGDFA-VDVEGARNLADAAKAAGVkRIVY---LSALG-ADRDS------------- 113

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446581728 2322 qnlDNLYLESKFQGEKMVREAmekGVRATIYRVGNLVGN 2360
Cdd:COG0702   114 ---PSPYLRAKAAVEEALRAS---GLPYTILRPGWFMGN 146
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 1558-1969 2.75e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 62.31  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQhllekGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITS 1637
Cdd:PRK07787   25 VLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1638 NKfkshlnvSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKV 1717
Cdd:PRK07787  100 AP-------DDPAGLPHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1718 TQ----FYSHSFdssVSEIFSTLLNGAELYLLSdeqRYSTVEYAQAIQETQATISDLPTVFfnelstSLTKLDSEKIRSL 1793
Cdd:PRK07787  173 VHglplFHVHGL---VLGVLGPLRIGNRFVHTG---RPTPEAYAQALSEGGTLYFGVPTVW------SRIAADPEAARAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1794 R--FIIMGGEAASTNAIRSWQNTFKNQvQLVNEYGPTEA--TVSAMyyfipvLEGENNLlGSVpiGIPISNTKVHILNSy 1869
Cdd:PRK07787  241 RgaRLLVSGSAALPVPVFDRLAALTGH-RPVERYGMTETliTLSTR------ADGERRP-GWV--GLPLAGVETRLVDE- 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1870 mQYCPVGC----MGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKDKQ-VKIR 1944
Cdd:PRK07787  310 -DGGPVPHdgetVGELQVRGPTLFDGYLNRPDATAAAFTADGW--------FRTGDVAVVDPDGMHRIVGRESTDlIKSG 380

                         410       420
                  ....*....|....*....|....*
gi 446581728 1945 GHRIELGEIEDAMLQLEGISQAVVT 1969
Cdd:PRK07787  381 GYRIGAGEIETALLGHPGVREAAVV 405
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 1545-2031 2.95e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 62.32  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINY 1624
Cdd:PRK13383   47 RWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1625 IVRDSEACRIITSNKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDlAYVIYTSGSTGKPKGT-----LLTHKGVL 1699
Cdd:PRK13383  127 ALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG-RIVLLTSGTTGKPKGVprapqLRSAVGVW 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1700 NLVEWRNEVFQISPNDKVTQFYsHSFDSSVSeIFSTLLNGAelyLLSDEQRYSTVEYAQAIQETQATISDLPTVFFNELS 1779
Cdd:PRK13383  206 VTILDRTRLRTGSRISVAMPMF-HGLGLGML-MLTIALGGT---VLTHRHFDAEAALAQASLHRADAFTAVPVVLARILE 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1780 TSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqvQLVNEYGPTEATVSAMYYFIPVLEGENNllgsvpIGIPIS 1859
Cdd:PRK13383  281 LPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGD--ILYNGYGSTEVGIGALATPADLRDAPET------VGKPVA 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1860 NTKVHILNSYMQycPVG--CMGELYIESLGLAQGYwkqKEKTKQAFISNPFSednskrlyrTGDLVRWLPNGNIEFMGRK 1937
Cdd:PRK13383  353 GCPVRILDRNNR--PVGprVTGRIFVGGELAGTRY---TDGGGKAVVDGMTS---------TGDMGYLDNAGRLFIVGRE 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1938 DKQVKIRGHRIELGEIEDAMLQLEGISQ-AV--VTQTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHV 2014
Cdd:PRK13383  419 DDMIISGGENVYPRAVENALAAHPAVADnAVigVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIV 498

                         490
                  ....*....|....*..
gi 446581728 2015 LEIPITANGKIDFEKLP 2031
Cdd:PRK13383  499 SSIPRNPTGKVLRKELP 515
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1545-2026 3.30e-09

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 62.31  E-value: 3.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1545 RQPERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAyiPIDVKYPEDR--I 1622
Cdd:PRK10946   35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRseL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1623 NYIVRDSEACRIITS--------NKFKSHLNVSDYKVSIIEDIYRTTINDDVKILNKP-----------DDLAYVIYTSG 1683
Cdd:PRK10946  113 NAYASQIEPALLIADrqhalfsdDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPaedftatpspaDEVAFFQLSGG 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1684 STGKPKGTLLTHKGVLNLVEWRNEVFQISPNdkvTQFY-----SHSFDSSVSEIFSTLLNGAELYLLSDEqrySTVEYAQ 1758
Cdd:PRK10946  193 STGTPKLIPRTHNDYYYSVRRSVEICGFTPQ---TRYLcalpaAHNYPMSSPGALGVFLAGGTVVLAPDP---SATLCFP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1759 AIQETQATISDL--PTVFFnELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNQVQLVneYGPTEATVSamy 1836
Cdd:PRK10946  267 LIEKHQVNVTALvpPAVSL-WLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQV--FGMAEGLVN--- 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1837 yFIPVLEGENNLLGSVpiGIPIS-NTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskr 1915
Cdd:PRK10946  341 -YTRLDDSDERIFTTQ--GRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------- 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1916 lYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGMLLQ---AYYKTVDGIgiekN 1992
Cdd:PRK10946  411 -YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEkscAFLVVKEPL----K 485

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 446581728 1993 KLAI--HLSNV-LPEYMVPKYYSHVLEIPITANGKID 2026
Cdd:PRK10946  486 AVQLrrFLREQgIAEFKLPDRVECVDSLPLTAVGKVD 522
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 610-901 3.58e-09

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 61.16  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVV--NLSYSVINTfhLGKEDVFLQFATIIFDASIMEIFPILLCGGRMHLISEIEKR 687
Cdd:cd17636     1 DPVLAIYTAAFSGRPNGALLSHQALLaqALVLAVLQA--IDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  688 SAEEFInVSQKYGITNVVLPTafFKLIADMPKEMLLKLNSVK--RLFVGGETLPAESVRKWQSKLGlkipvlnAYGPTET 765
Cdd:cd17636    79 EVLELI-EAERCTHAFLLPPT--IDQIVELNADGLYDLSSLRssPAAPEWNDMATVDTSPWGRKPG-------GYGQTEV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  766 TVCATMYEVNGeiqKEISNIpiGKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEktegafisLDKSYNR 845
Cdd:cd17636   149 MGLATFAALGG---GAIGGA--GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPE--------VNARRTR 215

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  846 DkKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVV 901
Cdd:cd17636   216 G-GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAV 270
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1107-1387 5.32e-09

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 60.91  E-value: 5.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1107 YIEPSL----NKDILQ---DTIRFLVERHEMLRTVFI-ERNGEPRQVIL-------NSIAIDLIHDEIEHMskkeqQEYI 1171
Cdd:cd19544    24 YLLRSLlafdSRARLDaflAALQQVIDRHDILRTAILwEGLSEPVQVVWrqaelpvEELTLDPGDDALAQL-----RARF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1172 rttinQTDHTPFDLEKGPLFRIRI-FNLNKKKSYLYINLHHIITDEWSVRNLLDELMkvysAFAKRRNPELPTiSNRYVD 1250
Cdd:cd19544    99 -----DPRRYRLDLRQAPLLRAHVaEDPANGRWLLLLLFHHLISDHTSLELLLEEIQ----AILAGRAAALPP-PVPYRN 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1251 YAewEQVQLNLGRWDTEkSYWMAELA------APLPILNLPLDFSRNRQSTnkgtvfeMKLDNEMKESLKQVCEQENISM 1324
Cdd:cd19544   169 FV--AQARLGASQAEHE-AFFREMLGdvdeptAPFGLLDVQGDGSDITEAR-------LALDAELAQRLRAQARRLGVSP 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 1325 YMLFLAAYIQLLHYLTDQKDIIVGTPVVGRNH--QEFEKIQGFFVNTLAIRTQLNDV----------KNLTQLLQ 1387
Cdd:cd19544   239 ASLFHLAWALVLARCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLRVRLGGRsvreavrqthARLAELLR 313
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1852-2118 5.66e-09

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 60.15  E-value: 5.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1852 VPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSEDNSKRLYRTGDLVRWLPNGNI 1931
Cdd:COG3433    18 PVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1932 EFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYY 2011
Cdd:COG3433    98 GLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2012 SHVLEIPITANGKIDFEKLPKIEF---GHEQKDECKLKPQTKVQKDIAKVWSEVLNVK--SIGLKDDFFNLGGHSLKVMp 2086
Cdd:COG3433   178 VVALDALLLLALKVVARAAPALAAaeaLLAAASPAPALETALTEEELRADVAELLGVDpeEIDPDDNLFDLGLDSIRLM- 256

                         250       260       270
                  ....*....|....*....|....*....|...
gi 446581728 2087 ALV-KLKPLYPNLKIQDFFKYRTIEKLASHIEE 2118
Cdd:COG3433   257 QLVeRWRKAGLDVSFADLAEHPTLAAWWALLAA 289
PLN02654 PLN02654
acetate-CoA ligase
 492-962 8.69e-09

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 61.07  E-value: 8.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  492 DQSITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMII 571
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  572 TKKEyrglVERfAIHTIYLED-------------------FHYANS---------------------IENIASTHTIE-- 609
Cdd:PLN02654  198 TCNA----VKR-GPKTINLKDivdaaldesakngvsvgicLTYENQlamkredtkwqegrdvwwqdvVPNYPTKCEVEwv 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 ---DAAYIIYTSGSTGLPKGVVVPHKG-VVNLSYSVINTFHLGKEDVFLQFATI--IFDASIMEIFPILlcGGRMHLISE 683
Cdd:PLN02654  273 daeDPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCgwITGHSYVTYGPML--NGATVLVFE 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  684 IEKR--SAEEFINVSQKYGITNV-VLPTAFFKLIADMPKemLLKLNSVKRLFV---GGETLPAESVRKWQSKLG-LKIPV 756
Cdd:PLN02654  351 GAPNypDSGRCWDIVDKYKVTIFyTAPTLVRSLMRDGDE--YVTRHSRKSLRVlgsVGEPINPSAWRWFFNVVGdSRCPI 428

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  757 LNAYGPTETTvcATMyevngeiqkeISNIPIGKPIA-NSEVFvisPFNTLCPSgVVGELFIGGDGVANGYLNQKEKTEGA 835
Cdd:PLN02654  429 SDTWWQTETG--GFM----------ITPLPGAWPQKpGSATF---PFFGVQPV-IVDEKGKEIEGECSGYLCVKKSWPGA 492

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  836 FISLDKSYNRDKKMYC--------TGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND 907
Cdd:PLN02654  493 FRTLYGDHERYETTYFkpfagyyfSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728  908 ----KIVCFYLSKDNTELKQEALKTFLS---ESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PLN02654  573 vkgqGIYAFVTLVEGVPYSEELRKSLILtvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 885-956 9.18e-09

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 54.09  E-value: 9.18e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728   885 EIEGTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGK 956
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELkgeaPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
733-963 9.29e-09

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 60.06  E-value: 9.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  733 VGGETLPAESVRKwQSKLGlkIPVLNAYGPTETTV-CatMYEvngeiqkeisnipiGKPIANSEVFVISpfntlcpsgvv 811
Cdd:PRK07824  158 VGGGPAPAPVLDA-AAAAG--INVVRTYGMSETSGgC--VYD--------------GVPLDGVRVRVED----------- 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  812 GELFIGGDGVANGYLNQKE----KTEGAFISLDksynrdkkmycTGDLVrllaNGNLEFIGRKDNQVKIRGYRIELDEIE 887
Cdd:PRK07824  208 GRIALGGPTLAKGYRNPVDpdpfAEPGWFRTDD-----------LGALD----DGVLTVLGRADDAISTGGLTVLPQVVE 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  888 GTLFKHPEVRDAVVFTYQNDK----IVCFYLSKDNTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLE 963
Cdd:PRK07824  273 AALATHPAVADCAVFGLPDDRlgqrVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
PLN02654 PLN02654
acetate-CoA ligase
 1558-2042 1.18e-08

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 60.68  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1558 SLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITS 1637
Cdd:PLN02654  120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITC 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1638 NKFKSHLnvsdyKVSIIEDIYRTTINDDVK-----------------------------------ILNKP---------- 1672
Cdd:PLN02654  200 NAVKRGP-----KTINLKDIVDAALDESAKngvsvgicltyenqlamkredtkwqegrdvwwqdvVPNYPtkcevewvda 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1673 DDLAYVIYTSGSTGKPKGTLLTHKGVLnlvEWRNEVFQISPNDKVTQFY----------SHSFDSsvseiFSTLLNGAEL 1742
Cdd:PLN02654  275 EDPLFLLYTSGSTGKPKGVLHTTGGYM---VYTATTFKYAFDYKPTDVYwctadcgwitGHSYVT-----YGPMLNGATV 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1743 YLLSDEQRYSTVEYAQAIQETQATisdlpTVFFN--ELSTSLTKLDSEKI-----RSLRFIIMGGEAASTNAIRSWQNTF 1815
Cdd:PLN02654  347 LVFEGAPNYPDSGRCWDIVDKYKV-----TIFYTapTLVRSLMRDGDEYVtrhsrKSLRVLGSVGEPINPSAWRWFFNVV 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1816 -KNQVQLVNEYGPTEatvSAMYYFIPVLEGENNLLGSVPigIPISNTKVHILNSYMQYCPVGCMGELYIESL--GLAQGY 1892
Cdd:PLN02654  422 gDSRCPISDTWWQTE---TGGFMITPLPGAWPQKPGSAT--FPFFGVQPVIVDEKGKEIEGECSGYLCVKKSwpGAFRTL 496

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1893 WKQKEKTKQAFISnPFsednsKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTE 1972
Cdd:PLN02654  497 YGDHERYETTYFK-PF-----AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIE 570

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728 1973 ---GGMLLQAYYKTVDGIGIE---KNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIefGHEQKDE 2042
Cdd:PLN02654  571 hevKGQGIYAFVTLVEGVPYSeelRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI--ASRQLDE 644
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 525-858 1.78e-08

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 59.75  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  525 TMEREIDTIVWILGILKSGGVYVPIDPKFpEKRIEYILKDSESQMIItkkeYRGLVERFAIHTIYLEDFHYANSIENIAS 604
Cdd:cd05921    86 LMSQDLAKLKHLFELLKPGLVFAQDAAPF-ARALAAIFPLGTPLVVS----RNAVAGRGAISFAELAATPPTAAVDAAFA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  605 THTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKED--VFLQFA--TIIFDASIMeIFPILLCGGRMHL 680
Cdd:cd05921   161 AVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLpwNHTFGGNHN-FNLVLYNGGTLYI 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  681 IS--EIEKRSAEEFINVSQkygitnvVLPTAFFK-------LIADMPKEMLLK---LNSVKRLFVGGETLPAESVRKWQS 748
Cdd:cd05921   240 DDgkPMPGGFEETLRNLRE-------ISPTVYFNvpagwemLVAALEKDEALRrrfFKRLKLMFYAGAGLSQDVWDRLQA 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  749 ----KLGLKIPVLNAYGPTETTVCATMYEvngEIQKEISNIpiGKPIANSEVfvispfnTLCPSGVVGELFIGGDGVANG 824
Cdd:cd05921   313 lavaTVGERIPMMAGLGATETAPTATFTH---WPTERSGLI--GLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPG 380

                         330       340       350
                  ....*....|....*....|....*....|....
gi 446581728  825 YLNQKEKTEGAFisldksynRDKKMYCTGDLVRL 858
Cdd:cd05921   381 YWRQPELTAQAF--------DEEGFYCLGDAAKL 406
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 484-628 1.82e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 59.77  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  484 NQIAI-----SMGDQ-SITYYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWIL-----GILKS---GGvyvpi 549
Cdd:PRK00174   82 DKVAIiwegdDPGDSrKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLacariGAVHSvvfGG----- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  550 dpkF-PE---KRIEyilkDSESQMIITKKE-YRG------------------------LVERFAIHTIYLE--DFHYANS 598
Cdd:PRK00174  157 ---FsAEalaDRII----DAGAKLVITADEgVRGgkpiplkanvdealancpsvekviVVRRTGGDVDWVEgrDLWWHEL 229

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 446581728  599 IENIASTHT-----IEDAAYIIYTSGSTGLPKGVV 628
Cdd:PRK00174  230 VAGASDECEpepmdAEDPLFILYTSGSTGKPKGVL 264
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 1672-1968 2.65e-08

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 59.43  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 PDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDkvtqFYSHSFD----SSVSEIFSTLLNGAELYLLSd 1747
Cdd:PLN02860  171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDD----VYLHTAPlchiGGLSSALAMLMVGACHVLLP- 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1748 eqRYSTVEYAQAIQETQAT-ISDLPTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTFKNqVQLVNEYG 1826
Cdd:PLN02860  246 --KFDAKAALQAIKQHNVTsMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPN-AKLFSAYG 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1827 PTEA--TVSAMYYFIPVLE--------------GENNLLGSVPIGIPISNTKVHIlnsymqyCPVGCMGELYIESLG--L 1888
Cdd:PLN02860  323 MTEAcsSLTFMTLHDPTLEspkqtlqtvnqtksSSVHQPQGVCVGKPAPHVELKI-------GLDESSRVGRILTRGphV 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1889 AQGYWKQKEKTkqafisnpfSEDNSKRLY-RTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAV 1967
Cdd:PLN02860  396 MLGYWGQNSET---------ASVLSNDGWlDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVV 466


                  .
gi 446581728 1968 V 1968
Cdd:PLN02860  467 V 467
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1672-2027 3.29e-08

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 58.16  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 PDDLaYVIYTSGSTGKPKGTLLTH-------KGVLNLVEWRNEVFQISPNDKVTQFYSHSF-------DSSVSEIFSTLL 1737
Cdd:cd05924     3 ADDL-YILYTGGTTGMPKGVMWRQedifrmlMGGADFGTGEFTPSEDAHKAAAAAAGTVMFpapplmhGTGSWTAFGGLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1738 NGAELYLLSDeqRYSTVEYAQAIQETQAT-ISDLPTVFFNELSTSLTKLDSEKIRSLRFIIMGGeAASTNAIRSWQNTFK 1816
Cdd:cd05924    82 GGQTVVLPDD--RFDPEEVWRTIEKHKVTsMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGG-ALLSPEVKQGLLELV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1817 NQVQLVNEYGPTEATvsamyyfipvlegeNNLLGSVPIGIPISNTKVHI------LNSYMQYCPVGCMGELYIESLGL-A 1889
Cdd:cd05924   159 PNITLVDAFGSSETG--------------FTGSGHSAGSGPETGPFTRAnpdtvvLDDDGRVVPPGSGGVGWIARRGHiP 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1890 QGYWKQKEKTKqafisNPFSEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVT 1969
Cdd:cd05924   225 LGYYGDEAKTA-----ETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV 299

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728 1970 ---QTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDF 2027
Cdd:cd05924   300 grpDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADY 360
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 609-902 4.68e-08

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 58.59  E-value: 4.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHLGKEDVFLQFATIifdASIME-IFPI---LLCGGRMHLISEi 684
Cdd:cd17641   158 EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPL---PWIGEqMYSVgqaLVCGFIVNFPEE- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  685 ekrsAEEFINVSQKYGITNVVLP----------------------TAFFKLIADMPKEML-------------------- 722
Cdd:cd17641   234 ----PETMMEDLREIGPTFVLLPprvwegiaadvrarmmdatpfkRFMFELGMKLGLRALdrgkrgrpvslwlrlaswla 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  723 -----------LKLNSVKRLFVGGETLPAESVRKWQSklgLKIPVLNAYGPTETTVCATMYEvNGEIQKEIsnipIGKPI 791
Cdd:cd17641   310 dallfrplrdrLGFSRLRSAATGGAALGPDTFRFFHA---IGVPLKQLYGQTELAGAYTVHR-DGDVDPDT----VGVPF 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  792 ANSEVFVISpfntlcpsgvVGELFIGGDGVANGYLNQKEKTEGAFIsldksynRDKKMYcTGDLVRLLANGNLEFIGR-K 870
Cdd:cd17641   382 PGTEVRIDE----------VGEILVRSPGVFVGYYKNPEATAEDFD-------EDGWLH-TGDAGYFKENGHLVVIDRaK 443

                         330       340       350
                  ....*....|....*....|....*....|..
gi 446581728  871 DNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF 902
Cdd:cd17641   444 DVGTTSDGTRFSPQFIENKLKFSPYIAEAVVL 475
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 1557-1957 5.39e-08

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 58.59  E-value: 5.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1557 ESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIIT 1636
Cdd:PLN02387  105 EWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1637 SNK-FKSHLNVSDYKVSIIEDIYRTTINDDVK----------------------------ILNKPDDLAYVIYTSGSTGK 1687
Cdd:PLN02387  185 DSKqLKKLIDISSQLETVKRVIYMDDEGVDSDsslsgssnwtvssfseveklgkenpvdpDLPSPNDIAVIMYTSGSTGL 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1688 PKGTLLTHKGVLNLVEW-RNEVFQISPNDkVTQFY---SHSF----DSSVSEIFSTLLNGAELYLL--SDEQRYSTVEYA 1757
Cdd:PLN02387  265 PKGVMMTHGNIVATVAGvMTVVPKLGKND-VYLAYlplAHILelaaESVMAAVGAAIGYGSPLTLTdtSNKIKKGTKGDA 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1758 QAIQETQATIsdLPTVFFNELSTSLTKLDSE----------------------------------------KIRSL---- 1793
Cdd:PLN02387  344 SALKPTLMTA--VPAILDRVRDGVRKKVDAKgglakklfdiaykrrlaaiegswfgawglekllwdalvfkKIRAVlggr 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1794 -RFIIMGGEAASTNAIRswqntFKN---QVQLVNEYGPTEATVSAMYYfipvlEGENNLLGSVpiGIPISNTKVHILN-- 1867
Cdd:PLN02387  422 iRFMLSGGAPLSGDTQR-----FINiclGAPIGQGYGLTETCAGATFS-----EWDDTSVGRV--GPPLPCCYVKLVSwe 489

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1868 --SYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFIsnpfSEDNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIR- 1944
Cdd:PLN02387  490 egGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYK----VDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQh 565

                         490
                  ....*....|...
gi 446581728 1945 GHRIELGEIEDAM 1957
Cdd:PLN02387  566 GEYVSLGKVEAAL 578
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 852-964 6.60e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 57.74  E-value: 6.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  852 TGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND---KIVCFYLSKDnTELKQEALKT 928
Cdd:PRK08308  295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvagERVKAKVISH-EEIDPVQLRE 373

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446581728  929 FLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKLEL 964
Cdd:PRK08308  374 WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 1557-1943 1.02e-07

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 57.47  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1557 ESLTYRQLNMSSNQVA-QHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSE----- 1630
Cdd:cd17632    66 ETITYAELWERVGAVAaAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEprlla 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1631 --------ACRIITSNKFKSHLNVSDYKVSIieDIYR-----------------TTINDDVKILNK------------PD 1673
Cdd:cd17632   146 vsaehldlAVEAVLEGGTPPRLVVFDHRPEV--DAHRaalesarerlaavgipvTTLTLIAVRGRDlppaplfrpepdDD 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1674 DLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFY---SHSFDSSVseIFSTLLNGAELY------- 1743
Cdd:cd17632   224 PLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFmpmSHIAGRIS--LYGTLARGGTAYfaaasdm 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1744 --LLSD-------------------EQRYSTVE----YAQAIQETQATisdlptvffnELSTSLtkldSEKIRSLRFII- 1797
Cdd:cd17632   302 stLFDDlalvrptelflvprvcdmlFQRYQAELdrrsVAGADAETLAE----------RVKAEL----RERVLGGRLLAa 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1798 MGGEAASTNAIRSW-QNTFknQVQLVNEYGPTEATVSAMYYFI---PVLEGEnnlLGSVP-IGIpISNTKVHilnsymqy 1872
Cdd:cd17632   368 VCGSAPLSAEMKAFmESLL--DLDLHDGYGSTEAGAVILDGVIvrpPVLDYK---LVDVPeLGY-FRTDRPH-------- 433

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728 1873 cPvgcMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKDKQVKI 1943
Cdd:cd17632   434 -P---RGELLVKTDTLFPGYYKRPEVTAEVFDEDGF--------YRTGDVMAELGPDRLVYVDRRNNVLKL 492
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1003-1052 1.64e-07

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 51.10  E-value: 1.64e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 446581728   1003 IGRDDDFFKLGGHSLIAVQVLNQIQKEFHLKIEIRDIFEHTTIASLSAYI 1052
Cdd:smart00823   33 IDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 12-221 1.94e-07

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 56.33  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   12 EELDVTVGQEALWIAHQMEIEIGMNNEPIIIKLKGNLQIEVLKKALTTIVQSHPALRTIFKkrdEKIKQLIQKNVEFDIP 91
Cdd:cd19546     3 DEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFP---GDGGDVHQRILDADAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   92 IKDLTAFKNTEQKsiLKNFLESIVNEKFSLEEGPLFKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSNTYGELLQ 171
Cdd:cd19546    80 RPELPVVPATEEE--LPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARRE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728  172 GKS------NVEF------ESPYKNLVKHEESFIDSAIykegsSYWKDYLQGELTPTEFPID 221
Cdd:cd19546   158 GRAperaplPLQFadyalwERELLAGEDDRDSLIGDQI-----AYWRDALAGAPDELELPTD 214
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
 2167-2342 3.25e-07

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 54.30  E-value: 3.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2167 TGATGYLGAHILERLLQlpsttiyclvRENEDQVIGAKLKERMEFyfgKEILQKLKeRVELIEGDLslmnlgLDSKQLDH 2246
Cdd:pfam01073    3 TGGGGFLGRHIIKLLVR----------EGELKEVRVFDLRESPEL---LEDFSKSN-VIKYIQGDV------TDKDDLDN 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2247 LKKNVESIIH--CGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSVVG-----QAERDPKEFEFFESDF 2318
Cdd:pfam01073   63 ALEGVDVVIHtaSAVDVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRvLVYTSSAEVVGpnsygQPILNGDEETPYESTH 142

                          170       180
                   ....*....|....*....|....
gi 446581728  2319 drgqnlDNLYLESKFQGEKMVREA 2342
Cdd:pfam01073  143 ------QDAYPRSKAIAEKLVLKA 160
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 1543-1715 3.35e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 55.92  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1543 VDRQ----PERIAI------ATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYip 1612
Cdd:PRK00174   73 LDRHlktrGDKVAIiwegddPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH-- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1613 iDVKY----PE---DRINyivrDSEACRIITSNKF-----KSHL--NVsDYKVSIIEDI-----YRTTIND-------DV 1666
Cdd:PRK00174  151 -SVVFggfsAEalaDRII----DAGAKLVITADEGvrggkPIPLkaNV-DEALANCPSVekvivVRRTGGDvdwvegrDL 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581728 1667 ---------------KILNKPDDLaYVIYTSGSTGKPKGTLLTHKGVLNLV----EWrneVFQISPND 1715
Cdd:PRK00174  225 wwhelvagasdecepEPMDAEDPL-FILYTSGSTGKPKGVLHTTGGYLVYAamtmKY---VFDYKDGD 288
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 479-889 4.75e-07

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 55.33  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  479 ALKSPNQIAISMGD---------QSITYYELQQRSNQIVNYLRENDlKKGQRVSITMEREIDTIVWILGILKSGGVYVPI 549
Cdd:PRK05850   11 ASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAVPL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  550 DPKFP---EKRIEYILKDSESQMIITKKEYRGLVERFA----------IHTIYLEDFHYANSIEniASTHTIEDAAYIIY 616
Cdd:PRK05850   90 SVPQGgahDERVSAVLRDTSPSVVLTTSAVVDDVTEYVapqpgqsappVIEVDLLDLDSPRGSD--ARPRDLPSTAYLQY 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  617 TSGSTGLPKGVVVPHKGV-VNLSySVINTFHLGKEDVFLQFATII----F--DASIME--IFPIlLCGGRMHLISEIE-- 685
Cdd:PRK05850  168 TSGSTRTPAGVMVSHRNViANFE-QLMSDYFGDTGGVPPPDTTVVswlpFyhDMGLVLgvCAPI-LGGCPAVLTSPVAfl 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  686 KRSAeEFINVSQKYGITNVVLPTAFFKLIA------DMPKemlLKLNSVKRLFVGGETLPAESVRKWQ---SKLGLKIPV 756
Cdd:PRK05850  246 QRPA-RWMQLLASNPHAFSAAPNFAFELAVrktsddDMAG---LDLGGVLGIISGSERVHPATLKRFAdrfAPFNLRETA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  757 LN-AYGPTEttvcATMYEVNGEIQK----------EISN--------------IPIGKPiANSEVFVISP-FNTLCPSGV 810
Cdd:PRK05850  322 IRpSYGLAE----ATVYVATREPGQppesvrfdyeKLSAghakrcetgggtplVSYGSP-RSPTVRIVDPdTCIECPAGT 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  811 VGELFIGGDGVANGYLNQKEKTE---GAFIsLDKS-------YNRdkkmycTGDLvRLLANGNLEFIGRKDNQVKIRGYR 880
Cdd:PRK05850  397 VGEIWVHGDNVAAGYWQKPEETErtfGATL-VDPSpgtpegpWLR------TGDL-GFISEGELFIVGRIKDLLIVDGRN 468


                  ....*....
gi 446581728  881 IELDEIEGT 889
Cdd:PRK05850  469 HYPDDIEAT 477
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 1912-2025 4.87e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 54.66  E-value: 4.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1912 NSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVtqteggmllqayYKTVDGIGIEK 1991
Cdd:PRK08308  288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVV------------YRGKDPVAGER 355

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 446581728 1992 NKLAIHLSNV-------------LPEYMVPKYYSHVLEIPITANGKI 2025
Cdd:PRK08308  356 VKAKVISHEEidpvqlrewciqhLAPYQVPHEIESVTEIPKNANGKV 402
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 2047-2118 5.74e-07

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 49.08  E-value: 5.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728 2047 PQTKVQKDIAKVWSEVLNVK--SIGLKDDFFN-LGGHSLKVMPALVKLKPLYP-NLKIQDFFKYRTIEKLASHIEE 2118
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDpeEITPDDSFFEdLGLDSLDAVELIAALEEEFGiELPDTELFEYPTVADLADYLEE 77
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
 2163-2345 6.95e-07

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 53.43  E-value: 6.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQlpstTIYclvrenedQVIG--------AKLKERMEFYFGkeilqklKERVELIEGDLSl 2234
Cdd:cd05227     1 LVLVTGATGFIASHIVEQLLK----AGY--------KVRGtvrslsksAKLKALLKAAGY-------NDRLEFVIVDDL- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2235 mnlgLDSKQLDHLKKNVESIIHCGGEVRHYG---EREHFqKVNVQSTKYLLELAKNT-NV-RFHYISTLSVVGQAERDPK 2309
Cdd:cd05227    61 ----TAPNAWDEALKGVDYVIHVASPFPFTGpdaEDDVI-DPAVEGTLNVLEAAKAAgSVkRVVLTSSVAAVGDPTAEDP 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 446581728 2310 EFEFFESDF----DRGQNLDNLYLESKFQGEKMVREAMEK 2345
Cdd:cd05227   136 GKVFTEEDWndltISKSNGLDAYIASKTLAEKAAWEFVKE 175
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 1560-1835 1.01e-06

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 53.99  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1560 TYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRIITSNK 1639
Cdd:PRK06018   41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1640 F----------------------KSHLNVSDYKVSIIEDIYRTTINDDVKILNKPDDLAYVI-YTSGSTGKPKGTLLTHK 1696
Cdd:PRK06018  121 FvpilekiadklpsveryvvltdAAHMPQTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMcYTSGTTGDPKGVLYSHR 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1697 G-VLN-LVEWRNEVFQISPNDK----VTQFYSHSFDSSVSEIFS--------TLLNGAELY-LLSDEQrystVEYAQAIq 1761
Cdd:PRK06018  201 SnVLHaLMANNGDALGTSAADTmlpvVPLFHANSWGIAFSAPSMgtklvmpgAKLDGASVYeLLDTEK----VTFTAGV- 275

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581728 1762 etqatisdlPTVFFnELSTSLTKlDSEKIRSLRFIIMGGEAASTNAIRSWQNTfknQVQLVNEYGPTE----ATVSAM 1835
Cdd:PRK06018  276 ---------PTVWL-MLLQYMEK-EGLKLPHLKMVVCGGSAMPRSMIKAFEDM---GVEVRHAWGMTEmsplGTLAAL 339
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 1628-1949 1.02e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 54.34  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1628 DSEACRIITSNKFKSHlnvsDYKVSIIE-DIYRTTINDDVKILN-KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVE-- 1703
Cdd:PTZ00342  261 DKEKLEKIKDLKEKAK----KLGISIILfDDMTKNKTTNYKIQNeDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVpl 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1704 WRNEVFQiSPNDKVTQFY---SHSFDSSVseIFSTLLNGAELYLLSDEQRYstveYAQAIQETQATI-SDLPTVFFNELS 1779
Cdd:PTZ00342  337 CKHSIFK-KYNPKTHLSYlpiSHIYERVI--AYLSFMLGGTINIWSKDINY----FSKDIYNSKGNIlAGVPKVFNRIYT 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1780 TSLTKLD-----------------------------------SEKIR-----SLRFIIMGGEAASTNAIRSWQNTFknQV 1819
Cdd:PTZ00342  410 NIMTEINnlpplkrflvkkilslrksnnnggfskflegithiSSKIKdkvnpNLEVILNGGGKLSPKIAEELSVLL--NV 487

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1820 QLVNEYGPTEATVsamyyfiPVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCPVGCM--GELYIESLGLAQGYWKQKE 1897
Cdd:PTZ00342  488 NYYQGYGLTETTG-------PIFVQHADDNNTESIGGPISPNTKYKVRTWETYKATDTLpkGELLIKSDSIFSGYFLEKE 560

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446581728 1898 KTKQAFISNPFsednskrlYRTGDLVRWLPNGNIEFMGRKDKQVKI-RGHRIE 1949
Cdd:PTZ00342  561 QTKNAFTEDGY--------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 1671-1968 1.10e-06

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 53.95  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1671 KPDDLAYVIYTSGSTGKPKGTLLTHkgvlnlvewRNEVFQISPNDKVTQFYshsfdssVSEIFSTLLNGAELYllsdeQR 1750
Cdd:PLN02736  219 KPEDVATICYTSGTTGTPKGVVLTH---------GNLIANVAGSSLSTKFY-------PSDVHISYLPLAHIY-----ER 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1751 YS---TVEYAQAIQETQATISDL--------PTVF------FNELSTSLT------------------------------ 1783
Cdd:PLN02736  278 VNqivMLHYGVAVGFYQGDNLKLmddlaalrPTIFcsvprlYNRIYDGITnavkesgglkerlfnaaynakkqalengkn 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1784 ------KLDSEKIRS-----LRFIIMGGEAASTNAIRSWQNTFKNQVqlVNEYGPTEAT--VSAMYyfipvlEGEnNLLG 1850
Cdd:PLN02736  358 pspmwdRLVFNKIKAklggrVRFMSSGASPLSPDVMEFLRICFGGRV--LEGYGMTETScvISGMD------EGD-NLSG 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1851 SVpiGIPISNTKVHILN-SYMQYC------PvgcMGELYIESLGLAQGYWKQKEKTKQAFisnpfseDNSKRLYrTGDLV 1923
Cdd:PLN02736  429 HV--GSPNPACEVKLVDvPEMNYTsedqpyP---RGEICVRGPIIFKGYYKDEVQTREVI-------DEDGWLH-TGDIG 495

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 446581728 1924 RWLPNGNIEFMGRKDKQVKI-RGHRIELGEIEDAMLQLEGISQAVV 1968
Cdd:PLN02736  496 LWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYAKCKFVAQCFV 541
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 600-869 1.23e-06

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 53.90  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  600 ENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTFHL-----GKEDV--FLQFATIIfdASIMEIFPIL 672
Cdd:cd05933   141 DAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLrpatvGQESVvsYLPLSHIA--AQILDIWLPI 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  673 LCGGRMH----------LISEIEKRSAEEFINVSQKYG------ITNVVLPTAFFKLIADMPKEMLLKLNSVK------- 729
Cdd:cd05933   219 KVGGQVYfaqpdalkgtLVKTLREVRPTAFMGVPRVWEkiqekmKAVGAKSGTLKRKIASWAKGVGLETNLKLmggesps 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  730 -------------------------RLFVGGETLPAESVrkwQSKLGLKIPVLNAYGPTETTVCATMyevNGEIQKEISN 784
Cdd:cd05933   299 plfyrlakklvfkkvrkalgldrcqKFFTGAAPISRETL---EFFLSLNIPIMELYGMSETSGPHTI---SNPQAYRLLS 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  785 ipIGKPIANSEVFVISPfntlcPSGVVGELFIGGDGVANGYLNQKEKTEGAfisLDKsynrDKKMYcTGDLVRLLANGNL 864
Cdd:cd05933   373 --CGKALPGCKTKIHNP-----DADGIGEICFWGRHVFMGYLNMEDKTEEA---IDE----DGWLH-SGDLGKLDEDGFL 437


                  ....*
gi 446581728  865 EFIGR 869
Cdd:cd05933   438 YITGR 442
dTDP_GD_SDR_e cd05246
dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4, ...
 2162-2359 1.38e-06

dTDP-D-glucose 4,6-dehydratase, extended (e) SDRs; This subgroup contains dTDP-D-glucose 4,6-dehydratase and related proteins, members of the extended-SDR family, with the characteristic Rossmann fold core region, active site tetrad and NAD(P)-binding motif. dTDP-D-glucose 4,6-dehydratase is closely related to other sugar epimerases of the SDR family. dTDP-D-dlucose 4,6,-dehydratase catalyzes the second of four steps in the dTDP-L-rhamnose pathway (the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose) in the synthesis of L-rhamnose, a cell wall component of some pathogenic bacteria. In many gram negative bacteria, L-rhamnose is an important constituent of lipopoylsaccharide O-antigen. The larger N-terminal portion of dTDP-D-Glucose 4,6-dehydratase forms a Rossmann fold NAD-binding domain, while the C-terminus binds the sugar substrate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187557 [Multi-domain]  Cd Length: 315  Bit Score: 52.94  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQlpsttiyclvRENEDQVIGA-KLKermefYFG-KEILQKLKE--RVELIEGDLSlmnl 2237
Cdd:cd05246     1 MKILVTGGAGFIGSNFVRYLLN----------KYPDYKIINLdKLT-----YAGnLENLEDVSSspRYRFVKGDIC---- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2238 glDSKQLDHL--KKNVESIIHCGGEV---RHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPkef 2311
Cdd:cd05246    62 --DAELVDRLfeEEKIDAVIHFAAEShvdRSISDPEPFIRTNVLGTYTLLEAARKYGVkRFVHISTDEVYGDLLDDG--- 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 446581728 2312 EFFESDfdrGQNLDNLYLESKFQGEKMVREAMEK-GVRATIYRVGNLVG 2359
Cdd:cd05246   137 EFTETS---PLAPTSPYSASKAAADLLVRAYHRTyGLPVVITRCSNNYG 182
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 2164-2444 1.53e-06

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 52.24  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2164 VFLTGATGYLGAHILERLLQLPSTTIYCLVRENEDQVIgaklkermefyfgkEILQKLKERvELIegdlslmnlglDSKQ 2243
Cdd:cd05254     2 ILITGATGMLGRALVRLLKERGYEVIGTGRSRASLFKL--------------DLTDPDAVE-EAI-----------RDYK 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2244 LDHlkknvesIIHCGGEVRH---YGEREHFQKVNVQSTKYLLELAKNTNVRFHYISTLSVVgqaerDPKEFEFFESDFdr 2320
Cdd:cd05254    56 PDV-------IINCAAYTRVdkcESDPELAYRVNVLAPENLARAAKEVGARLIHISTDYVF-----DGKKGPYKEEDA-- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2321 gQNLDNLYLESKFQGEKMVREAMEkgvRATIYRVGNLVGNSKTGkfqyninENA---FYRLLKGICLSSIAPDV---NTY 2394
Cdd:cd05254   122 -PNPLNVYGKSKLLGEVAVLNANP---RYLILRTSWLYGELKNG-------ENFvewMLRLAAERKEVNVVHDQigsPTY 190

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446581728 2395 V-DLTPvdygslAITELSYKaNTVNKTMHICNPNQLKWDQFINSL-QAFGYD 2444
Cdd:cd05254   191 AaDLAD------AILELIER-NSLTGIYHLSNSGPISKYEFAKLIaDALGLP 235
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 1660-2033 1.67e-06

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 53.07  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1660 TTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQIspnDKVtqfysHSFD-------SSVSEI 1732
Cdd:PRK07445  107 PPPLPSQGILPNLETGWIMIPTGGSSGQIRFAIHTWETLTASVQGFQRYFQL---QQV-----NSFCvlplyhvSGLMQF 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1733 FSTLLNGAELYLLSdeqrYSTVEYAQAIQETQAT--ISDLPT---VFFNELSTSLtkldsekiRSLRFIIMGGEAAstna 1807
Cdd:PRK07445  179 MRSFLTGGKLVILP----YKRLKSGQELPPNPSDffLSLVPTqlqRLLQLRPQWL--------AQFRTILLGGAPA---- 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1808 irsW----QNTFKNQVQLVNEYGPTEaTVSamyyFIPVLEGENNLLGSVPIGIPISNTKVHILNsymqycpvGCMGELYI 1883
Cdd:PRK07445  243 ---WpsllEQARQLQLRLAPTYGMTE-TAS----QIATLKPDDFLAGNNSSGQVLPHAQITIPA--------NQTGNITI 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1884 ESLGLAQGYWKQKEktkqafisnpfsedNSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQlegi 1963
Cdd:PRK07445  307 QAQSLALGYYPQIL--------------DSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA---- 368

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728 1964 SQAV-------VTQTEGGMLLQAYYKTVDGIgIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKI 2033
Cdd:PRK07445  369 TGLVqdvcvlgLPDPHWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
ArgR-Cyc_NRPS-like cd20480
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ...
 47-288 1.74e-06

Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to Cyc-domains there are various other subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380470 [Multi-domain]  Cd Length: 406  Bit Score: 52.89  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728   47 NLQIEVLKKALTTIVQSHPALRTIFKkrDEKIKQLIQKNVEFDIPIKDLTafknteqksilkNFLESIVNEKFSLEEGPL 126
Cdd:cd20480    36 NISVDTLERCLTVLINHHPMLHALLS--DDFYLHINSKNQIDAFAVNDLS------------SASEQEAAEQLARTRATL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  127 --------FKFHIIKFSEDTFILHLMFHHIIYDGWSLGVFIRQLSntygELLQGkSNVEFESPYKNLVKHEEsFIDSAIY 198
Cdd:cd20480   102 tksrskatISVVLSLLPANKIRLHVRFNSVVVDHPSVNLFFEQLC----QLLRG-SLLSFLAQEQVILAHNQ-LVISELQ 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  199 KEG--SSYWKDYLQGELTPTEFPI--DFNKMNEKRYTDKNISknINSDLFYQIQCFAKKNNISIYRVMLSTYCTLLHQMT 274
Cdd:cd20480   176 STGlsSAFWNEQILQLPSSANLPTvcEPEKLRETGITRRTLT--LSSDKWQQLVTISKQHNVTPELTLASIFSAVLSLWG 253

                         250
                  ....*....|....
gi 446581728  275 NAEEIIVGIPINTR 288
Cdd:cd20480   254 NQKDMMLRFDLNKK 267
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 2163-2367 1.84e-06

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 51.08  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLpSTTIYCLVRENEdqviGAKLKERMEfyfgkeilqklkerVELIEGDLSlmnlglDSK 2242
Cdd:cd05243     1 KVLVVGATGKVGRHVVRELLDR-GYQVRALVRDPS----QAEKLEAAG--------------AEVVVGDLT------DAE 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2243 QLDHLKKNVESIIHCGGEVRHYGERehFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVvgQAERDPKEFEFfesdfdrg 2321
Cdd:cd05243    56 SLAAALEGIDAVISAAGSGGKGGPR--TEAVDYDGNINLIDAAKKAGVkRFVLVSSIGA--DKPSHPLEALG-------- 123

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446581728 2322 qnldnLYLESKFQGEKMVREAmekGVRATIYRVGNLV-GNSKTGKFQ 2367
Cdd:cd05243   124 -----PYLDAKRKAEDYLRAS---GLDYTIVRPGGLTdDPAGTGRVV 162
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 1555-1709 1.99e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 53.44  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1555 ATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYPEDRINYIVRDSEACRI 1634
Cdd:PTZ00216  118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1635 ITSNKfkshlNVSD----YKVSIIED---IYRTTINDDVK-----------------------ILNKP---DDLAYVIYT 1681
Cdd:PTZ00216  198 VCNGK-----NVPNllrlMKSGGMPNttiIYLDSLPASVDtegcrlvawtdvvakghsagshhPLNIPennDDLALIMYT 272

                         170       180       190
                  ....*....|....*....|....*....|..
gi 446581728 1682 SGSTGKPKGTLLTH----KGVLNLVEWRNEVF 1709
Cdd:PTZ00216  273 SGTTGDPKGVMHTHgsltAGILALEDRLNDLI 304
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
 2162-2308 2.17e-06

UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 52.25  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQLpSTTIYCLvrENedqvigaklkermeFYFG-KEILQKL--KERVELIEGDLSlmnlg 2238
Cdd:cd05230     1 KRILITGGAGFLGSHLCDRLLED-GHEVICV--DN--------------FFTGrKRNIEHLigHPNFEFIRHDVT----- 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446581728 2239 ldskqlDHLKKNVESIIH--CGGEVRHYGERE-HFQKVNVQSTKYLLELAKNTNVRFHYISTLSVVGQAERDP 2308
Cdd:cd05230    59 ------EPLYLEVDQIYHlaCPASPVHYQYNPiKTLKTNVLGTLNMLGLAKRVGARVLLASTSEVYGDPEVHP 125
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 461-631 2.86e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 52.67  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  461 NALTYPNLKTLDQ--LIDLQALKSPNQIAISMGDQSITYYELQQRsnqIVNY---LRENDLKKGQRVSITMEREIDTIVW 535
Cdd:PTZ00216   86 RALAYRPVERVEKevVKDADGKERTMEVTHFNETRYITYAELWER---IVNFgrgLAELGLTKGSNVAIYEETRWEWLAS 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  536 ILGILKSGGVYVPIDPKFPEKRIEYILKDSESQMIIT-----KKEYRGLVERFAIHT--IYLEDF--------------- 593
Cdd:PTZ00216  163 IYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCngknvPNLLRLMKSGGMPNTtiIYLDSLpasvdtegcrlvawt 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446581728  594 ------HYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPH 631
Cdd:PTZ00216  243 dvvakgHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTH 286
PRK09192 PRK09192
fatty acyl-AMP ligase;
497-907 2.87e-06

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 52.70  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  497 YYELQQRSNQIVNYLRENDLKKGQRVSITMEREIDTIVWILGILKSGGVYVPID-PKFPEKRIEYI------LKDSESQM 569
Cdd:PRK09192   52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYIaqlrgmLASAQPAA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  570 IITKKEYRGLVE-----RFAIHTIYLEDFHYANSIENIASTHTIEDAAYIIYTSGSTGLPKGVVVPHKGVV-NLSYSVIN 643
Cdd:PRK09192  132 IITPDELLPWVNeathgNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMaNLRAISHD 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  644 TFHLGKEDVFLQFATIIFDASIMEIF--PI-------LLCGG----RMHL-ISEIEKRSAEefINVSQKYGitnvvlpta 709
Cdd:PRK09192  212 GLKVRPGDRCVSWLPFYHDMGLVGFLltPVatqlsvdYLPTRdfarRPLQwLDLISRNRGT--ISYSPPFG--------- 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  710 fFKLIA---DMPKEMLLKLNSVKRLFVGGETLPAESVRKWQSKLGlkiPV-------LNAYGPTETTVCATMYEVNGEIQ 779
Cdd:PRK09192  281 -YELCArrvNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFA---PAgfddkafMPSYGLAEATLAVSFSPLGSGIV 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  780 KEISNIPI-----------------------GKPIANSEVFVISPFNTLCPSGVVGELFIGGDGVANGYLNQKEKTegAF 836
Cdd:PRK09192  357 VEEVDRDRleyqgkavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQ--DV 434

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446581728  837 ISLDKSYNrdkkmycTGDLvRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVR--DAVVFTYQND 907
Cdd:PRK09192  435 LAADGWLD-------TGDL-GYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE 499
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 1546-2025 3.40e-06

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 52.66  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1546 QPERIAIATATES----LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLG------------------- 1602
Cdd:cd05943    82 ADDPAAIYAAEDGerteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLAtasigaiwsscspdfgvpg 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1603 -----------ILKAGAAYI----PIDVkypEDRINYIVR---DSEACRIITSNKFKSHLNVSDY-KVSIIEDIYRTTin 1663
Cdd:cd05943   162 vldrfgqiepkVLFAVDAYTyngkRHDV---REKVAELVKglpSLLAVVVVPYTVAAGQPDLSKIaKALTLEDFLATG-- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1664 DDVKILNKP---DDLAYVIYTSGSTGKPKGTLLTHKGVLnLVEWRNEVFQ--ISPNDKVtqFYshsfdssvseiFST--- 1735
Cdd:cd05943   237 AAGELEFEPlpfDHPLYILYSSGTTGLPKCIVHGAGGTL-LQHLKEHILHcdLRPGDRL--FY-----------YTTcgw 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1736 ---------LLNGAELyLLSDEQ--RYSTVEYAQAIQETQATISDLPTVFFNELSTS-LTKLDSEKIRSLRFIIMGGEAA 1803
Cdd:cd05943   303 mmwnwlvsgLAVGATI-VLYDGSpfYPDTNALWDLADEEGITVFGTSAKYLDALEKAgLKPAETHDLSSLRTILSTGSPL 381

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1804 STNAIRSWQNTFKNQVQLVNEYGPTEaTVSAmyyFI------PVLEGEnnllgsvpIGIPISNTKVHILNsYMQYCPVGC 1877
Cdd:cd05943   382 KPESFDYVYDHIKPDVLLASISGGTD-IISC---FVggnpllPVYRGE--------IQCRGLGMAVEAFD-EEGKPVWGE 448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1878 MGELYIESLGLAQ--GYWKQKEKTKqaFISNPFSEDNSkrLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIED 1955
Cdd:cd05943   449 KGELVCTKPFPSMpvGFWNDPDGSR--YRAAYFAKYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYR 524

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1956 AMLQLEGISQAVVT-----QTEGGMLLqaYYKTVDGIGIE-------KNKLAIHLSnvlPEYmVPKYYSHVLEIPITANG 2023
Cdd:cd05943   525 VVEKIPEVEDSLVVgqewkDGDERVIL--FVKLREGVELDdelrkriRSTIRSALS---PRH-VPAKIIAVPDIPRTLSG 598


                  ..
gi 446581728 2024 KI 2025
Cdd:cd05943   599 KK 600
PRK09192 PRK09192
fatty acyl-AMP ligase;
1556-1716 4.67e-06

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 51.93  E-value: 4.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1556 TESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGAAYIPIDVKYP-------EDRINYIVRD 1628
Cdd:PRK09192   47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLAS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1629 SEACRIITSNKFKSHLN---VSDYKVSII--EDIYRTTINDDVKILNKPDDLAYVIYTSGSTGKPKGTLLTHKGVL-NLV 1702
Cdd:PRK09192  127 AQPAAIITPDELLPWVNeatHGNPLLHVLshAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMaNLR 206

                         170
                  ....*....|....
gi 446581728 1703 EWRNEVFQISPNDK 1716
Cdd:PRK09192  207 AISHDGLKVRPGDR 220
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
 2164-2310 5.31e-06

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 51.07  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2164 VFLTGATGYLGAHILERLLqlpsttiyclvrENEDQVIGAKlkermEFYFGKEI-LQKLKERVELIEGDLSlmnlglDSK 2242
Cdd:cd05256     2 VLVTGGAGFIGSHLVERLL------------ERGHEVIVLD-----NLSTGKKEnLPEVKPNVKFIEGDIR------DDE 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446581728 2243 QLDHLKKNVESIIH---CGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPKE 2310
Cdd:cd05256    59 LVEFAFEGVDYVFHqaaQASVPRSIEDPIKDHEVNVLGTLNLLEAARKAGVkRFVYASSSSVYGDPPYLPKD 130
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 614-884 6.79e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 51.64  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  614 IIYTSGSTGLPKGVVVPHK----GVVNLS-YSVINTFHLGKEDVFLQFATIiFDASImeIFPILLCGGRMHLISEIEKRS 688
Cdd:PTZ00342  309 IVYTSGTSGKPKGVMLSNKnlynTVVPLCkHSIFKKYNPKTHLSYLPISHI-YERVI--AYLSFMLGGTINIWSKDINYF 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  689 AEEFINvSQKYGITNVvlPTAFFKLIADMPKEmLLKLNSVKRLFV------------GGETLPAESVRKWQSKLGLKI-P 755
Cdd:PTZ00342  386 SKDIYN-SKGNILAGV--PKVFNRIYTNIMTE-INNLPPLKRFLVkkilslrksnnnGGFSKFLEGITHISSKIKDKVnP 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  756 VLN---------------------------AYGPTETTvcatmyevnGEI----QKEISNIPIGKPIANSEVFVISPFNT 804
Cdd:PTZ00342  462 NLEvilngggklspkiaeelsvllnvnyyqGYGLTETT---------GPIfvqhADDNNTESIGGPISPNTKYKVRTWET 532

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  805 LCPSGVV--GELFIGGDGVANGYLNQKEKTEGAFIsldksynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKI-RGYRI 881
Cdd:PTZ00342  533 YKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFT--------EDGYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYI 604


                  ...
gi 446581728  882 ELD 884
Cdd:PTZ00342  605 ETD 607
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 752-962 1.48e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 49.99  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  752 LKIPVLNAYGPTETT--VCATMYE--VNGeiqkeisNIPIGKPIANSEVfvispfnTLCPsGVVGELFIGGDGVANGYLN 827
Cdd:PRK07445  253 LQLRLAPTYGMTETAsqIATLKPDdfLAG-------NNSSGQVLPHAQI-------TIPA-NQTGNITIQAQSLALGYYP 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  828 QKEKTEGAFIsldksynrdkkmycTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVF----T 903
Cdd:PRK07445  318 QILDSQGIFE--------------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLglpdP 383

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728  904 YQNDKIVCFYLSKDnTELKQEALKTFLSESLPDFMMPNYIFHLESFPVSPSGKLDRKKL 962
Cdd:PRK07445  384 HWGEVVTAIYVPKD-PSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 2162-2353 1.60e-05

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 49.17  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQlPSTTIYCLVREnedqvigaklkermEFYFGKEILQKLKERVELIEGDlsLMNLGLDS 2241
Cdd:cd05271     1 MVVTVFGATGFIGRYVVNRLAK-RGSQVIVPYRC--------------EAYARRLLVMGDLGQVLFVEFD--LRDDESIR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHlkknVESIIHCGGevRHYGERE-HFQKVNVQSTKYLLELAKNTNV-RFHYISTLsvvGQAERDPKEfeffesdfd 2319
Cdd:cd05271    64 KALEG----SDVVINLVG--RLYETKNfSFEDVHVEGPERLAKAAKEAGVeRLIHISAL---GADANSPSK--------- 125

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 446581728 2320 rgqnldnlYLESKFQGEKMVREA-MEkgvrATIYR 2353
Cdd:cd05271   126 --------YLRSKAEGEEAVREAfPE----ATIVR 148
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 2164-2359 2.02e-05

UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 49.22  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2164 VFLTGATGYLGAHILERLLQLPSTtiyclVRENEDQVIGAKLKERMEFYfgkeilqklKERVELIEGDLSLMNLGLDSKQ 2243
Cdd:cd05234     2 ILVTGGAGFIGSHLVDRLLEEGNE-----VVVVDNLSSGRRENIEPEFE---------NKAFRFVKRDLLDTADKVAKKD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2244 LD---HLKKNVesiihcggEVRhYGE---REHFQKvNVQSTKYLLELAKNTNV-RFHYISTLSVVGqaerDPKEFEFFEs 2316
Cdd:cd05234    68 GDtvfHLAANP--------DVR-LGAtdpDIDLEE-NVLATYNVLEAMRANGVkRIVFASSSTVYG----EAKVIPTPE- 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446581728 2317 dfDRGQNLDNLYLESKFQGEKMVREAMEK-GVRATIYRVGNLVG 2359
Cdd:cd05234   133 --DYPPLPISVYGASKLAAEALISAYAHLfGFQAWIFRFANIVG 174
RfbB COG1088
dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];
2162-2297 2.23e-05

dTDP-D-glucose 4,6-dehydratase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440705 [Multi-domain]  Cd Length: 333  Bit Score: 48.93  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQlpsttiyclvRENEDQVIG-AKLkermeFYFG-KEILQKLK--ERVELIEGDLSlmnl 2237
Cdd:COG1088     2 MRILVTGGAGFIGSNFVRYLLA----------KYPGAEVVVlDKL-----TYAGnLENLADLEddPRYRFVKGDIR---- 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446581728 2238 glDSKQLDHL--KKNVESIIHCGGEV---RHYGEREHFQKVNVQSTKYLLELAK---NTNVRFHYIST 2297
Cdd:COG1088    63 --DRELVDELfaEHGPDAVVHFAAEShvdRSIDDPAAFVETNVVGTFNLLEAARkywVEGFRFHHVST 128
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 1547-2042 2.27e-05

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 49.63  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1547 PERIAIATATESLTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRS-----MNSIVSMLGIL------KAGAAYIPIDV 1615
Cdd:PLN03102   28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTpamyeMHFAVPMAGAVlnpintRLDATSIAAIL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1616 KYPEDRINYIVRD-----SEACRIITSNKFKSHLNV-------SDYKVSIIEDIYRTTINDD----------VKILNKPD 1673
Cdd:PLN03102  108 RHAKPKILFVDRSfeplaREVLHLLSSEDSNLNLPVifiheidFPKRPSSEELDYECLIQRGeptpslvarmFRIQDEHD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1674 DLAyVIYTSGSTGKPKGTLLTHKGVL-----NLVEWRNEVFQISPNdKVTQFYSHSFdssvSEIFSTLLNGAELYLLsde 1748
Cdd:PLN03102  188 PIS-LNYTSGTTADPKGVVISHRGAYlstlsAIIGWEMGTCPVYLW-TLPMFHCNGW----TFTWGTAARGGTSVCM--- 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1749 qRYSTV-EYAQAIQETQAT-ISDLPTVFFNELSTSltKLDSEKIRSLRFIIMGGEAASTNAIRSWQNTfknQVQLVNEYG 1826
Cdd:PLN03102  259 -RHVTApEIYKNIEMHNVThMCCVPTVFNILLKGN--SLDLSPRSGPVHVLTGGSPPPAALVKKVQRL---GFQVMHAYG 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1827 PTEATVsamyyfiPVLEGE-----NNLLGSVPI------GIPISN-TKVHILNSYMQ-YCPVG--CMGELYIESLGLAQG 1891
Cdd:PLN03102  333 LTEATG-------PVLFCEwqdewNRLPENQQMelkarqGVSILGlADVDVKNKETQeSVPRDgkTMGEIVIKGSSIMKG 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1892 YWKQKEKTKQAFisnpfsednSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVV--- 1968
Cdd:PLN03102  406 YLKNPKATSEAF---------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVvam 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1969 ---TQTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNV-------LPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFGHE 2038
Cdd:PLN03102  477 phpTWGETPCAFVVLEKGETTKEDRVDKLVTRERDLieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLV 556


                  ....
gi 446581728 2039 QKDE 2042
Cdd:PLN03102  557 VEDE 560
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 610-906 2.78e-05

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 49.63  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVVNLSYSVINTF-----HLGKEDVFLQFATI--IFDASIMEIF------------- 669
Cdd:PLN02614  224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksanaALTVKDVYLSYLPLahIFDRVIEECFiqhgaaigfwrgd 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  670 ------------PILLCG----------GRMHLISE---IEKR---SAEEFINVSQKYGITNVVLPTAFFKLIADMPKEm 721
Cdd:PLN02614  304 vklliedlgelkPTIFCAvprvldrvysGLQKKLSDggfLKKFvfdSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQ- 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  722 llKLNSVKRLFVGGETLPAESVRKWQSKLGLkIPVLNAYGPTETtvCATMYevnGEIQKEISNI-PIGKPIANSEVFVIS 800
Cdd:PLN02614  383 --GLGGNVRIILSGAAPLASHVESFLRVVAC-CHVLQGYGLTES--CAGTF---VSLPDELDMLgTVGPPVPNVDIRLES 454

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  801 ----PFNTLCpSGVVGELFIGGDGVANGYLNQKEKTEGAFIsldksynrDKKMYcTGDLVRLLANGNLEFIGRKDNQVKI 876
Cdd:PLN02614  455 vpemEYDALA-STPRGEICIRGKTLFSGYYKREDLTKEVLI--------DGWLH-TGDVGEWQPNGSMKIIDRKKNIFKL 524

                         330       340       350
                  ....*....|....*....|....*....|.
gi 446581728  877 -RGYRIELDEIEgTLFKHPEVRDAvVFTYQN 906
Cdd:PLN02614  525 sQGEYVAVENIE-NIYGEVQAVDS-VWVYGN 553
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 2163-2366 3.51e-05

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 48.30  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQlpsttiyclvrENEDQVIGAKLKERMefyfgKEILQKL-KERVELIEGDLslmnlgLDS 2241
Cdd:cd05247     1 KVLVTGGAGYIGSHTVVELLE-----------AGYDVVVLDNLSNGH-----REALPRIeKIRIEFYEGDI------RDR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHL--KKNVESIIHCGG--EVrhyGER-----EHFQkVNVQSTKYLLELAKNTNV-RFHYISTLSVVGQAERDPkef 2311
Cdd:cd05247    59 AALDKVfaEHKIDAVIHFAAlkAV---GESvqkplKYYD-NNVVGTLNLLEAMRAHGVkNFVFSSSAAVYGEPETVP--- 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728 2312 eFFESDfdrGQNLDNLYLESKFQGEKMVR-EAMEKGVRATIYRVGNLVGNSKTGKF 2366
Cdd:cd05247   132 -ITEEA---PLNPTNPYGRTKLMVEQILRdLAKAPGLNYVILRYFNPAGAHPSGLI 183
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 1671-1954 5.26e-05

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 48.66  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1671 KPDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEwRNEVFQISPNDKVTQ---FYS-----HSFDSSVSEIFstLLNGA-- 1740
Cdd:PLN02430  218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVR-GVDLFMEQFEDKMTHddvYLSflplaHILDRMIEEYF--FRKGAsv 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1741 -----ELYLLSDEqrystveyaqaIQETQAT-ISDLPTVF---------------------FNEL--------------- 1778
Cdd:PLN02430  295 gyyhgDLNALRDD-----------LMELKPTlLAGVPRVFerihegiqkalqelnprrrliFNALykyklawmnrgyshk 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1779 --STSLTKLDSEKIRS-----LRFIIMGGEAASTNA---IRSWQNTFknqvqLVNEYGPTEATVSAMYYFipvlEGENNL 1848
Cdd:PLN02430  364 kaSPMADFLAFRKVKAklggrLRLLISGGAPLSTEIeefLRVTSCAF-----VVQGYGLTETLGPTTLGF----PDEMCM 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1849 LGSVpiGIPISNTKVHILN-SYMQYCPVG--CMGELYIESLGLAQGYWKQKEKTKQAFISNPFsednskrlyRTGDLVRW 1925
Cdd:PLN02430  435 LGTV--GAPAVYNELRLEEvPEMGYDPLGepPRGEICVRGKCLFSGYYKNPELTEEVMKDGWF---------HTGDIGEI 503

                         330       340       350
                  ....*....|....*....|....*....|
gi 446581728 1926 LPNGNIEFMGRKDKQVKI-RGHRIELGEIE 1954
Cdd:PLN02430  504 LPNGVLKIIDRKKNLIKLsQGEYVALEYLE 533
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 1672-2082 6.59e-05

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 48.55  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1672 PDDLAYVIYTSGSTGKPKGTLLTHKGVLNLVEWRNEVFQISPNDKVTQFYSHSFDSSVSEIFSTLLNGAELYLLSDEQRY 1751
Cdd:COG3319   144 AAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLL 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1752 STVEYAQAIQETQATISDLPTVFFNELSTSLTKLDSEKIRSLRFIIMGGEAASTNAIRswqntfknQVQLVNEYGPTEAT 1831
Cdd:COG3319   224 LALLAAAALLALLLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALL--------LLAAAAALAAGGTA 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1832 VSAMYYFIPVLEGENNLLGSVPIGIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISNPFSED 1911
Cdd:COG3319   296 TTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAG 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1912 NSKRLYRTGDLVRWLPNGNIEFMGRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGmLLQAYYKTVDGIGIEK 1991
Cdd:COG3319   376 ARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAA-AAAAALAAAVVAAAAL 454

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1992 NKLAIHLSNVLPEYMVPKYYSHVLEIPITANGKIDFEKLPKIEFGHEQKDECKLKPQTKVQKDIAKVWSEVLNVKSIGLK 2071
Cdd:COG3319   455 AAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDD 534

                         410
                  ....*....|.
gi 446581728 2072 DDFFNLGGHSL 2082
Cdd:COG3319   535 DDFFGGGGGSL 545
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 610-887 8.71e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 47.68  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  610 DAAYIIYTSGSTGLPKGVVVPHKGVV-NLSYSVINTFHLGKEDVFLQFATIIFDASIMEIFPILLCGGrmhliSEIEKRS 688
Cdd:PRK07768  153 DLALMQLTSGSTGSPKAVQITHGNLYaNAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFG-----AELVKVT 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  689 AEEFIN-------VSQKYGITNVVLPTAFFKLIA----DMPKEMLLKLNSVKRLFVGGETLPAESVRKW---QSKLGLKi 754
Cdd:PRK07768  228 PMDFLRdpllwaeLISKYRGTMTAAPNFAYALLArrlrRQAKPGAFDLSSLRFALNGAEPIDPADVEDLldaGARFGLR- 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  755 P--VLNAYGPTETTVCATMYEV-NGEIQKEISN--------------------IPIGKPIANSEVFVISPFNTLCPSGVV 811
Cdd:PRK07768  307 PeaILPAYGMAEATLAVSFSPCgAGLVVDEVDAdllaalrravpatkgntrrlATLGPPLPGLEVRVVDEDGQVLPPRGV 386

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  812 GELFIGGDGVANGYLnqkekTEGAFISLDKsynrDKKMYCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIE 887
Cdd:PRK07768  387 GVIELRGESVTPGYL-----TMDGFIPAQD----ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
CC3_like_SDR_a cd05250
CC3(TIP30)-like, atypical (a) SDRs; Atypical SDRs in this subgroup include CC3 (also known as ...
 2162-2360 9.82e-05

CC3(TIP30)-like, atypical (a) SDRs; Atypical SDRs in this subgroup include CC3 (also known as TIP30) which is implicated in tumor suppression. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine rich NAD(P)-binding motif that resembles the extended SDRs, and have an active site triad of the SDRs (YXXXK and upstream Ser), although the upstream Asn of the usual SDR active site is substituted with Asp. For CC3, the Tyr of the triad is displaced compared to the usual SDRs and the protein is monomeric, both these observations suggest that the usual SDR catalytic activity is not present. NADP appears to serve an important role as a ligand, and may be important in the interaction with other macromolecules. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187560 [Multi-domain]  Cd Length: 214  Bit Score: 46.13  E-value: 9.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQLP-STTIYCLVREnedqvigaklkermefyfgKEILQKLKERVELIEGDLSLmnlgLD 2240
Cdd:cd05250     1 KTALVLGATGLVGKHLLRELLKSPyYSKVTAIVRR-------------------KLTFPEAKEKLVQIVVDFER----LD 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2241 SKQLDHLKKNVeSIIHCGGEVRHYGEREHFQKVNVQSTKYLLELAKNTNVR-FHYISTLSVvgqaerDPKefeffeSDFd 2319
Cdd:cd05250    58 EYLEAFQNPDV-GFCCLGTTRKKAGSQENFRKVDHDYVLKLAKLAKAAGVQhFLLVSSLGA------DPK------SSF- 123

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446581728 2320 rgqnldnLYLESKfqGEkMVREAMEKGV-RATIYRVGNLVGN 2360
Cdd:cd05250   124 -------LYLKVK--GE-VERDLQKLGFeRLTIFRPGLLLGE 155
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
 2162-2338 1.10e-04

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 46.95  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLqlpsttiyclvrENEDQVIG---------AKLKERMefyfgKEILQKLkERVELIEGDL 2232
Cdd:cd05253     1 MKILVTGAAGFIGFHVAKRLL------------ERGDEVVGidnlndyydVRLKEAR-----LELLGKS-GGFKFVKGDL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2233 SlmnlglDSKQLDHLKKNV--ESIIHCGGE--VRHYGEREH-FQKVNVQSTKYLLELAKNTNVR-FHYISTLSVVGQAER 2306
Cdd:cd05253    63 E------DREALRRLFKDHefDAVIHLAAQagVRYSLENPHaYVDSNIVGFLNLLELCRHFGVKhLVYASSSSVYGLNTK 136

                         170       180       190
                  ....*....|....*....|....*....|..
gi 446581728 2307 DPkefefFESDfDRGQNLDNLYLESKFQGEKM 2338
Cdd:cd05253   137 MP-----FSED-DRVDHPISLYAATKKANELM 162
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 1952-2024 1.22e-04

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 42.53  E-value: 1.22e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  1952 EIEDAMLQLEGISQAVV---TQTEGGMLLQAYYKTVDGIGIEKNKLAIHLSNVLPEYMVPKYYSHVLEIPITANGK 2024
Cdd:pfam13193    1 EVESALVSHPAVAEAAVvgvPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 1917-1975 1.45e-04

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 46.68  E-value: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728 1917 YRTGDLVRWLP--------NGNIEF-MGRKDKQVKIRGHRIELGEIEDAMLQLEGIS---QAVVTqTEGGM 1975
Cdd:COG1541   297 YRTGDLTRLLPepcpcgrtHPRIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGpeyQIVVD-REGGL 366
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2053-2110 1.69e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 41.78  E-value: 1.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446581728  2053 KDIAKVWSEVLNV--KSIGLKDDFFNLGGHSLKVMPALVKL-KPLYPNLKIQDFFKYRTIE 2110
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLeEEFGVEIPPSDLFEHPTLA 61
PLN02996 PLN02996
fatty acyl-CoA reductase
 2162-2255 3.40e-04

fatty acyl-CoA reductase


Pssm-ID: 215538 [Multi-domain]  Cd Length: 491  Bit Score: 45.85  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2162 KTVFLTGATGYLGAHILERLLQL-PSTT-IYCLVRENE---------DQVIGAKLKERMEFYFGKEILQKLKERVELIEG 2230
Cdd:PLN02996   12 KTILVTGATGFLAKIFVEKILRVqPNVKkLYLLLRASDaksatqrlhDEVIGKDLFKVLREKLGENLNSLISEKVTPVPG 91

                          90       100
                  ....*....|....*....|....*.
gi 446581728 2231 DLSLMNLGL-DSKQLDHLKKNVESII 2255
Cdd:PLN02996   92 DISYDDLGVkDSNLREEMWKEIDIVV 117
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 609-902 4.31e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 45.86  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  609 EDAAYIIYTSGSTGLPKGVVVPHKGVV-NLSYSVINTfHLGKEDVFLQFATIifdASIMEIFPILLC-----------GG 676
Cdd:PLN02736  221 EDVATICYTSGTTGTPKGVVLTHGNLIaNVAGSSLST-KFYPSDVHISYLPL---AHIYERVNQIVMlhygvavgfyqGD 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  677 RMHLISEIEKRSAEEFINVSQKY-----GITNVVLPTAFFkliadmpKEMLLKL--NSVKRLFVGGETLPAESVR----K 745
Cdd:PLN02736  297 NLKLMDDLAALRPTIFCSVPRLYnriydGITNAVKESGGL-------KERLFNAayNAKKQALENGKNPSPMWDRlvfnK 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  746 WQSKLG--------------------LKI----PVLNAYGPTETT-VCATMYEvngeiqKEISNIPIGKPIANSEVFVIS 800
Cdd:PLN02736  370 IKAKLGgrvrfmssgasplspdvmefLRIcfggRVLEGYGMTETScVISGMDE------GDNLSGHVGSPNPACEVKLVD 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  801 -----------PFntlcPSgvvGELFIGGDGVANGYLNQKEKTEGAFisldksyNRDKKMYcTGDLVRLLANGNLEFIGR 869
Cdd:PLN02736  444 vpemnytsedqPY----PR---GEICVRGPIIFKGYYKDEVQTREVI-------DEDGWLH-TGDIGLWLPGGRLKIIDR 508

                         330       340       350
                  ....*....|....*....|....*....|....
gi 446581728  870 KDNQVKI-RGYRIELDEIEGTLFKHPEVRDAVVF 902
Cdd:PLN02736  509 KKNIFKLaQGEYIAPEKIENVYAKCKFVAQCFVY 542
CAPF_like_SDR_e cd05261
capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of ...
 2164-2370 6.07e-04

capsular polysaccharide assembling protein (CAPF) like, extended (e) SDRs; This subgroup of extended SDRs, includes some members which have been identified as capsular polysaccharide assembling proteins, such as Staphylococcus aureus Cap5F which is involved in the biosynthesis of N-acetyl-l-fucosamine, a constituent of surface polysaccharide structures of S. aureus. This subgroup has the characteristic active site tetrad and NAD-binding motif of extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187571 [Multi-domain]  Cd Length: 248  Bit Score: 43.89  E-value: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2164 VFLTGATGYLGAHILERLLQLPSTTIYCLVRENEDQvigaklkermefyfgkeilqklkerveliegdlslmnlgldskQ 2243
Cdd:cd05261     3 ILITGAKGFIGKNLIARLKEQKDDDIFFYDRESDES-------------------------------------------E 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2244 LDHLKKNVESIIHCGGEVRHYGEREhFQKVNVQSTKYLLELAKNTNVRFHYISTLSVvgQAErdpkefeffesdfdrgqn 2323
Cdd:cd05261    40 LDDFLQGADFIFHLAGVNRPKDEAE-FESGNVGLTERLLDALTRNGKKPPILLSSSI--QAA------------------ 98

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446581728 2324 LDNLYLESKFQGEKMVRE-AMEKGVRATIYRVGNLVG-------NSKTGKFQYNI 2370
Cdd:cd05261    99 LDNPYGKSKLAAEELLQEyARETGAPVYIYRLPNVFGkwcrpnyNSAVATFCYNI 153
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
2165-2308 6.99e-04

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 44.46  E-value: 6.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2165 FLTGATGYLGAHILERLLQLPStTIYCLVRENEdqvigaklkermEFYFGK-EILQK--LKERVELIEGDLSlmnlglDS 2241
Cdd:pfam16363    1 LITGITGQDGSYLAELLLEKGY-EVHGIVRRSS------------SFNTGRlEHLYDdhLNGNLVLHYGDLT------DS 61

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446581728  2242 KQLDHLKKNVES--IIHCGGEV---RHYGEREHFQKVNVQSTKYLLELAKNTN----VRFHYISTLSVVGQAERDP 2308
Cdd:pfam16363   62 SNLVRLLAEVQPdeIYNLAAQShvdVSFEQPEYTADTNVLGTLRLLEAIRSLGlekkVRFYQASTSEVYGKVQEVP 137
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
 2214-2361 8.65e-04

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 43.80  E-value: 8.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  2214 GKEILQKLKER-VELIEGDLSLMNLgLDSKQLDHL----KKNVesIIHCGGEVRHYG---EREHFQKVNVQSTKYLLELA 2285
Cdd:pfam04321   11 GTELRRLLAERgIEVVALTRAELDL-TDPEAVARLlreiKPDV--VVNAAAYTAVDKaesEPDLAYAINALAPANLAEAC 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446581728  2286 KNTNVRFHYISTLSVV-GQAERDPKEfeffesdFDRGQNLdNLYLESKFQGEKMVREAMEkgvRATIYRVGNLVGNS 2361
Cdd:pfam04321   88 AAVGAPLIHISTDYVFdGTKPRPYEE-------DDETNPL-NVYGRTKLAGEQAVRAAGP---RHLILRTSWVYGEY 153
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
 2163-2346 1.13e-03

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 43.53  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLPsttiyclvreNEDQVIGAKLKerMEFYFGKEilqklkERVELIEGDLSlmnlglDSK 2242
Cdd:cd05238     2 KVLITGASGFVGQRLAERLLSDV----------PNERLILIDVV--SPKAPSGA------PRVTQIAGDLA------VPA 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2243 QLDHLKKNVESIIHCGGEVRHYGEREHFQK---VNVQSTKYLLELAKNTN--VRFHYISTLSVVGQAERDPKEFEFfesd 2317
Cdd:cd05238    58 LIEALANGRPDVVFHLAAIVSGGAEADFDLgyrVNVDGTRNLLEALRKNGpkPRFVFTSSLAVYGLPLPNPVTDHT---- 133

                         170       180       190
                  ....*....|....*....|....*....|.
gi 446581728 2318 fdrgqNLD--NLYLESKFQGEKMVREAMEKG 2346
Cdd:cd05238   134 -----ALDpaSSYGAQKAMCELLLNDYSRRG 159
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
 2163-2356 1.40e-03

NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs; NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187561 [Multi-domain]  Cd Length: 242  Bit Score: 43.03  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2163 TVFltGATGYLGAHILERLLQLPSTTIYCLVReNEdqvigaklkermefyfGKEILQKLKER-VELIEGDLSlmnlglDS 2241
Cdd:cd05251     2 LVF--GATGKQGGSVVRALLKDPGFKVRALTR-DP----------------SSPAAKALAAPgVEVVQGDLD------DP 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 2242 KQLDHLKKNVESIIHCGGEVRHYGEREHFQKVNVqstkylLELAKNTNVRfHYIstLSVVGQAERDPKEFEFFesdfdrg 2321
Cdd:cd05251    57 ESLEAALKGVYGVFLVTDFWEAGGEDEIAQGKNV------VDAAKRAGVQ-HFV--FSSVPDVEKLTLAVPHF------- 120

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 446581728 2322 qnldnlylESKFQGEKMVREAmekGVRATIYRVGN 2356
Cdd:cd05251   121 --------DSKAEVEEYIRAS---GLPATILRPAF 144
prpE PRK10524
propionyl-CoA synthetase; Provisional
 1540-1608 1.79e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 43.78  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446581728 1540 YMQVDR-------QPERIAIATATES---LTYRQLNMSSNQVAQHLLEKGIKRGDKVAIFLDRSMNSIVSMLGILKAGA 1608
Cdd:PRK10524   56 HNAVDRhlakrpeQLALIAVSTETDEertYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGA 134
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 1855-2026 2.71e-03

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 42.67  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1855 GIPISNTKVHILNSYMQYCPVGCMGELYIESLGLAQGYWKQKEKTKQAFISnpfsednskRLYRTGDLVRWLPNGNIEFM 1934
Cdd:cd17636   166 GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG---------GWHHTNDLGRREPDGSLSFV 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728 1935 GRKDKQVKIRGHRIELGEIEDAMLQLEGISQAVVTQTEGGMLLQAYYKTV---DGIGIEKNKLAIHLSNVLPEYMVPKYY 2011
Cdd:cd17636   237 GPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVvlkPGASVTEAELIEHCRARIASYKKPKSV 316

                         170
                  ....*....|....*
gi 446581728 2012 SHVLEIPITANGKID 2026
Cdd:cd17636   317 EFADALPRTAGGADD 331
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 850-964 3.16e-03

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 42.64  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581728  850 YCTGDLVRLLANGNLEFIGRKDNQVKIRGYRIELDEIEGTLFKHPEVRDAVVFTYQND----KIVCFYLSKDNTELKQE- 924
Cdd:cd05943   486 WAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKdgdeRVILFVKLREGVELDDEl 565

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446581728  925 --ALKTFLSESLPDFMMPNYIFHLESFPVSPSGkldrKKLEL 964
Cdd:cd05943   566 rkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSG----KKVEV 603
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
 2163-2196 4.51e-03

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 41.52  E-value: 4.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 446581728 2163 TVFLTGATGYLGAHILERLLQLPSTTIYCLVREN 2196
Cdd:cd05259     1 KIAIAGATGTLGGPIVSALLASPGFTVTVLTRPS 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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