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Conserved domains on  [gi|15598523|ref|NP_252017|]
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non-ribosomal peptide synthetase [Pseudomonas aeruginosa PAO1]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 1002729)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products; may contain C-terminal alpha/beta hydrolase domain

EC:  6.2.1.-
Gene Ontology:  GO:0019184|GO:0016874
PubMed:  11342140|15582399|14529378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
 4-2072 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1043.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     4 FARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEA 83
Cdd:PRK12467   47 FERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    84 RHVDLRA--DRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGEL 160
Cdd:PRK12467  127 PLDDLANeqGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTlHHIISDGWSMRVLVEELVQLYSAYS 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   161 GEPQAQMPTAsllaQLETDDY-----SGSEQYRGDR--AYFAEALEGLEPAL---FTRRRPAGLR-RTARHRLTLERTLL 229
Cdd:PRK12467  207 QGREPSLPAL----PIQYADYaiwqrSWLEAGERERqlAYWQEQLGGEHTVLelpTDRPRPAVPSyRGARLRVDLPQALS 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   230 DAI----RDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLR 305
Cdd:PRK12467  283 AGLkalaQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVK 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   306 EATRTLLRHQKMPLGDLLR--------GASPLF------DTTLSYMRWPAAQAIPNASVETVaQTHAHDpdalAIWVSEF 371
Cdd:PRK12467  363 RTALGAQAHQDLPFEQLVEalqperslSHSPLFqvmfnhQNTATGGRDREGAQLPGLTVEEL-SWARHT----AQFDLAL 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   372 DGHSDAQ---VDFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLp 448
Cdd:PRK12467  438 DTYESAQglwAAFTYATDLFEAT-TIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVH- 515

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   449 TLFAEQVARTPQRTALLeADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINP 528
Cdd:PRK12467  516 QLIEAQARQHPERPALV-FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   529 DHPLERVRLLLEDCGARVVLVDERAATLGESLGETRVLHLER----LPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGV 604
Cdd:PRK12467  595 EYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEpadlLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGV 674

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   605 MVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFV 684
Cdd:PRK12467  675 AISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIV 754

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   685 PSMLTPFLdlldgDPTARAAASSLRLVFCSGEALAPLQVARFRRLfGDAVRLVNLYGPTEATVDVSDHECASDN--PTRV 762
Cdd:PRK12467  755 PSHLQALL-----QASRVALPRPQRALVCGGEALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYELSDEErdFGNV 828

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   763 PIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA-GGRLYRTGDLARWLADGNLEY 841
Cdd:PRK12467  829 PIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEY 908

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   842 LGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAvRGTHLVGYYVAAAELDPGQ-------LRAGLSATLPDF 914
Cdd:PRK12467  909 LGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVPAAVADGAEhqatrdeLKAQLRQVLPDY 987

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   915 MLPAFFVRIDSLPLSANGKLDRRQLPAP---PEQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRI 991
Cdd:PRK12467  988 MVPAHLLLLDSLPLTPNGKLDRKALPKPdasAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQV 1067

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   992 RAAAQRR-GLGFELADLMRNPTVAGLAERLVrplaerSYQPFELVSEVDKPRLEGLEDAFPTSRlslgLLFHSRQRPDSS 1070
Cdd:PRK12467 1068 ISRVRQRlGIQVPLRTLFEHQTLAGFAQAVA------AQQQGAQPALPDVDRDQPLPLSYAQER----QWFLWQLEPGSA 1137

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1071 VYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGAsEPLQLVHTQArsePLILDLRgNPEAGTVLDEHIR--- 1147
Cdd:PRK12467 1138 AYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDG-RTRQVIHPVG---SLTLEEP-LLLAADKDEAQLKvyv 1212

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1148 QRRFHR-YSLQQpGLFLFAAFVR--EDGLDLVFSFHHAILDGWSVANLIVALVAAYR----GEPLPGPAPAL-----ACH 1215
Cdd:PRK12467 1213 EAEARQpFDLEQ-GPLLRVGLLRlaADEHVLVLTLHHIVSDGWSMQVLVDELVALYAaysqGQSLQLPALPIqyadyAVW 1291

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1216 VREELAALASPAAVGYWTGLLeGARMTRLDGFGAHEPQAAQG--PASHREALPDGLLERLKATAAQRGLPLKSLLLAAHC 1293
Cdd:PRK12467 1292 QRQWMDAGERARQLAYWKAQL-GGEQPVLELPTDRPRPAVQShrGARLAFELPPALAEGLRALARREGVTLFMLLLASFQ 1370

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1294 LTLHLFSRSDSVVTGA-ISN-GRPElpdADRMVGLFLNTVPVRSEIAGCSWIEvadALFRQER----DGHAHRRYPLSAI 1367
Cdd:PRK12467 1371 TLLHRYSGQDDIRVGVpIANrNRAE---TEGLIGFFVNTQVLRAEVDGQASFQ---QLLQQVKqaalEAQAHQDLPFEQL 1444

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1368 QQIVGDELSSAFNyvnlhvlePLWQ---------------LRDFRV----WEE--TNFALLVNvIATPSDGMYLRIDSDG 1426
Cdd:PRK12467 1445 VEALQPERSLSHS--------PLFQvmfnhqrddhqaqaqLPGLSVeslsWESqtAQFDLTLD-TYESSEGLQASLTYAT 1515

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1427 RGISRSQAALIGATFVELLWRLADHPDE-AADFAFLAP--RR------DAASQPEPLVDVV-SLFERQVEALPGSAALAF 1496
Cdd:PRK12467 1516 DLFEASTIERLAGHWLNLLQGLVADPERrLGELDLLDEaeRRqilegwNATHTGYPLARLVhQLIEDQAAATPEAVALVF 1595

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1497 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRV 1576
Cdd:PRK12467 1596 GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELL 1675

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1577 VAHPEHAH---VAAAERVLPVEELVADIEPETFAAPQL----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVAS 1649
Cdd:PRK12467 1676 LTQSHLQArlpLPDGLRSLVLDQEDDWLEGYSDSNPAVnlapQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQ 1755

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1650 GVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPG 1729
Cdd:PRK12467 1756 LSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE-HPL 1834

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1730 ALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPV 1808
Cdd:PRK12467 1835 SLRRVVCGGEALEV-EALRPWLERLPDTGLFNLYGPTETAvDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPV 1913

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1809 PVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 1887
Cdd:PRK12467 1914 PIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1888 lAIMRQaerQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL--------AELKQALRSELPEHMVPAHFAWVDGFALT 1959
Cdd:PRK12467 1994 -ARLRE---QGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLT 2069

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1960 PSGKRDDAALRALP---LEHGtnieYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRfMLLIEKRYGVD 2036
Cdd:PRK12467 2070 PNGKLDRKALPAPDaseLQQA----YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQ-VVSRARQAGIR 2144

                        2170      2180      2190      2200
                  ....*....|....*....|....*....|....*....|....
gi 15598523  2037 LPMAALIETPTVEGLAERLRE--------RSAVRAFDPLVPIRA 2072
Cdd:PRK12467 2145 FTPKDLFQHQTVQSLAAVAQEgdgtvsidQGPVTGDLPLLPIQQ 2188
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 2077-2341 5.16e-28

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00975:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 223  Bit Score: 114.02  E-value: 5.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2077 PPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAY 2156
Cdd:pfam00975    1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2157 EMARQLRALDPQaVAQLIVLDsitvdrnhaGSASdealllffywELVWFERSDKeveplpegASLEQKLDHIveRAIEAG 2236
Cdd:pfam00975   81 EVARRLERQGEA-VRSLFLSD---------ASAP----------HTVRYEASRA--------PDDDEVVAEF--TDEGGT 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2237 VLPAGTPRATVQRLYELFRASWQALIGYRPEVSDQDMTLLRADGPLPLALKPMHDAagthygdpknGWQHWTSGRLDVID 2316
Cdd:pfam00975  131 PEELLEDEELLSMLLPALRADYRALESYSCPPLDAQSATLFYGSDDPLHDADDLAE----------WVRDHTPGEFDVHV 200

                          250       260
                   ....*....|....*....|....*
gi 15598523   2317 VPGDHLVLMKEPyvETVAAEIAALL 2341
Cdd:pfam00975  201 FDGDHFYLIEHL--EAVLEIIEAKL 223
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 4-2072 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1043.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     4 FARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEA 83
Cdd:PRK12467   47 FERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    84 RHVDLRA--DRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGEL 160
Cdd:PRK12467  127 PLDDLANeqGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTlHHIISDGWSMRVLVEELVQLYSAYS 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   161 GEPQAQMPTAsllaQLETDDY-----SGSEQYRGDR--AYFAEALEGLEPAL---FTRRRPAGLR-RTARHRLTLERTLL 229
Cdd:PRK12467  207 QGREPSLPAL----PIQYADYaiwqrSWLEAGERERqlAYWQEQLGGEHTVLelpTDRPRPAVPSyRGARLRVDLPQALS 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   230 DAI----RDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLR 305
Cdd:PRK12467  283 AGLkalaQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVK 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   306 EATRTLLRHQKMPLGDLLR--------GASPLF------DTTLSYMRWPAAQAIPNASVETVaQTHAHDpdalAIWVSEF 371
Cdd:PRK12467  363 RTALGAQAHQDLPFEQLVEalqperslSHSPLFqvmfnhQNTATGGRDREGAQLPGLTVEEL-SWARHT----AQFDLAL 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   372 DGHSDAQ---VDFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLp 448
Cdd:PRK12467  438 DTYESAQglwAAFTYATDLFEAT-TIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVH- 515

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   449 TLFAEQVARTPQRTALLeADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINP 528
Cdd:PRK12467  516 QLIEAQARQHPERPALV-FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   529 DHPLERVRLLLEDCGARVVLVDERAATLGESLGETRVLHLER----LPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGV 604
Cdd:PRK12467  595 EYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEpadlLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGV 674

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   605 MVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFV 684
Cdd:PRK12467  675 AISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIV 754

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   685 PSMLTPFLdlldgDPTARAAASSLRLVFCSGEALAPLQVARFRRLfGDAVRLVNLYGPTEATVDVSDHECASDN--PTRV 762
Cdd:PRK12467  755 PSHLQALL-----QASRVALPRPQRALVCGGEALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYELSDEErdFGNV 828

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   763 PIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA-GGRLYRTGDLARWLADGNLEY 841
Cdd:PRK12467  829 PIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEY 908

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   842 LGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAvRGTHLVGYYVAAAELDPGQ-------LRAGLSATLPDF 914
Cdd:PRK12467  909 LGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVPAAVADGAEhqatrdeLKAQLRQVLPDY 987

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   915 MLPAFFVRIDSLPLSANGKLDRRQLPAP---PEQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRI 991
Cdd:PRK12467  988 MVPAHLLLLDSLPLTPNGKLDRKALPKPdasAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQV 1067

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   992 RAAAQRR-GLGFELADLMRNPTVAGLAERLVrplaerSYQPFELVSEVDKPRLEGLEDAFPTSRlslgLLFHSRQRPDSS 1070
Cdd:PRK12467 1068 ISRVRQRlGIQVPLRTLFEHQTLAGFAQAVA------AQQQGAQPALPDVDRDQPLPLSYAQER----QWFLWQLEPGSA 1137

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1071 VYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGAsEPLQLVHTQArsePLILDLRgNPEAGTVLDEHIR--- 1147
Cdd:PRK12467 1138 AYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDG-RTRQVIHPVG---SLTLEEP-LLLAADKDEAQLKvyv 1212

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1148 QRRFHR-YSLQQpGLFLFAAFVR--EDGLDLVFSFHHAILDGWSVANLIVALVAAYR----GEPLPGPAPAL-----ACH 1215
Cdd:PRK12467 1213 EAEARQpFDLEQ-GPLLRVGLLRlaADEHVLVLTLHHIVSDGWSMQVLVDELVALYAaysqGQSLQLPALPIqyadyAVW 1291

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1216 VREELAALASPAAVGYWTGLLeGARMTRLDGFGAHEPQAAQG--PASHREALPDGLLERLKATAAQRGLPLKSLLLAAHC 1293
Cdd:PRK12467 1292 QRQWMDAGERARQLAYWKAQL-GGEQPVLELPTDRPRPAVQShrGARLAFELPPALAEGLRALARREGVTLFMLLLASFQ 1370

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1294 LTLHLFSRSDSVVTGA-ISN-GRPElpdADRMVGLFLNTVPVRSEIAGCSWIEvadALFRQER----DGHAHRRYPLSAI 1367
Cdd:PRK12467 1371 TLLHRYSGQDDIRVGVpIANrNRAE---TEGLIGFFVNTQVLRAEVDGQASFQ---QLLQQVKqaalEAQAHQDLPFEQL 1444

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1368 QQIVGDELSSAFNyvnlhvlePLWQ---------------LRDFRV----WEE--TNFALLVNvIATPSDGMYLRIDSDG 1426
Cdd:PRK12467 1445 VEALQPERSLSHS--------PLFQvmfnhqrddhqaqaqLPGLSVeslsWESqtAQFDLTLD-TYESSEGLQASLTYAT 1515

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1427 RGISRSQAALIGATFVELLWRLADHPDE-AADFAFLAP--RR------DAASQPEPLVDVV-SLFERQVEALPGSAALAF 1496
Cdd:PRK12467 1516 DLFEASTIERLAGHWLNLLQGLVADPERrLGELDLLDEaeRRqilegwNATHTGYPLARLVhQLIEDQAAATPEAVALVF 1595

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1497 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRV 1576
Cdd:PRK12467 1596 GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELL 1675

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1577 VAHPEHAH---VAAAERVLPVEELVADIEPETFAAPQL----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVAS 1649
Cdd:PRK12467 1676 LTQSHLQArlpLPDGLRSLVLDQEDDWLEGYSDSNPAVnlapQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQ 1755

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1650 GVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPG 1729
Cdd:PRK12467 1756 LSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE-HPL 1834

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1730 ALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPV 1808
Cdd:PRK12467 1835 SLRRVVCGGEALEV-EALRPWLERLPDTGLFNLYGPTETAvDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPV 1913

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1809 PVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 1887
Cdd:PRK12467 1914 PIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1888 lAIMRQaerQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL--------AELKQALRSELPEHMVPAHFAWVDGFALT 1959
Cdd:PRK12467 1994 -ARLRE---QGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLT 2069

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1960 PSGKRDDAALRALP---LEHGtnieYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRfMLLIEKRYGVD 2036
Cdd:PRK12467 2070 PNGKLDRKALPAPDaseLQQA----YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQ-VVSRARQAGIR 2144

                        2170      2180      2190      2200
                  ....*....|....*....|....*....|....*....|....
gi 15598523  2037 LPMAALIETPTVEGLAERLRE--------RSAVRAFDPLVPIRA 2072
Cdd:PRK12467 2145 FTPKDLFQHQTVQSLAAVAQEgdgtvsidQGPVTGDLPLLPIQQ 2188
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-1309 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: 817.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    1 MVRFARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAE 80
Cdd:COG1020   12 AAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   81 FEARHVDLRAD---RDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRTHHIVSDAW----GLQLFLSRVR 153
Cdd:COG1020   92 APLPVVVLLVDleaLAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLsdglLLAELLRLYL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  154 AGYLGELGEPQAQMPTASLLAQLETDDYSGSEQYRgDRAYFAEALEGLEPAL---FTRRRPAGLR-RTARHRLTLERTLL 229
Cdd:COG1020  172 AAYAGAPLPLPPLPIQYADYALWQREWLQGEELAR-QLAYWRQQLAGLPPLLelpTDRPRPAVQSyRGARVSFRLPAELT 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  230 DAIRDRGE----SPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLR 305
Cdd:COG1020  251 AALRALARrhgvTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVR 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  306 EATRTLLRHQKMPLGDLLR--------GASPLFDTTLSYMRWPA-AQAIPNASVETVAQTHAHDPDALAIWVSEFDGHsd 376
Cdd:COG1020  331 ETLLAAYAHQDLPFERLVEelqperdlSRNPLFQVMFVLQNAPAdELELPGLTLEPLELDSGTAKFDLTLTVVETGDG-- 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  377 AQVDFEYACDVFDADFpMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVA 456
Cdd:COG1020  409 LRLTLEYNTDLFDAAT-IERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAA 487

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  457 RTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVR 536
Cdd:COG1020  488 RTPDAVAV-VFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLA 566

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  537 LLLEDCGARVVLVDER-AATLGESLGETRVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRL 615
Cdd:COG1020  567 YMLEDAGARLVLTQSAlAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLL 646

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  616 NWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDll 695
Cdd:COG1020  647 AWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLD-- 724

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  696 dgdpTARAAASSLRLVFCSGEALAPLQVARFRRLFGDaVRLVNLYGPTEATVDVSDHECASDNPT--RVPIGRPIDNLRL 773
Cdd:COG1020  725 ----AAPEALPSLRLVLVGGEALPPELVRRWRARLPG-ARLVNLYGPTETTVDSTYYEVTPPDADggSVPIGRPIANTRV 799

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  774 YVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPF-VAGGRLYRTGDLARWLADGNLEYLGRADDQVKIR 852
Cdd:COG1020  800 YVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIR 879

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  853 GNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAE--LDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSA 930
Cdd:COG1020  880 GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGaaAAAALLRLALALLLPPYMVPAAVVLLLPLPLTG 959

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  931 NGKLDRRQLPAPPEQVAA--VAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQRRGLGFELADLM 1008
Cdd:COG1020  960 NGKLDRLALPAPAAAAAAaaAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1009 RNPTVAGLAERLVRPLAERSYQPfelvsevdkPRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAA 1088
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAP---------LAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1089 FRHALDRVVAAYPALRSSFDLsgASEPLQLVHTQARSEPLILDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAFV 1168
Cdd:COG1020 1111 LLLLLALLLALLAALRARRAV--RQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLL 1188

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1169 REDGLDLVFSFHHAILDGWSVANLIVALVAAYRGEPLPGPAPALACHVREELAALASPAAVGYWTGLLEGARMTRLDGFG 1248
Cdd:COG1020 1189 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLA 1268

                       1290      1300      1310      1320      1330      1340
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523 1249 AHEPQAAQGPASHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGA 1309
Cdd:COG1020 1269 LALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1481-1970 0e+00

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: 654.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1481 FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 1560
Cdd:cd17651    1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1561 AQRLALILETAQPFRVVAHPEHAHVAAAERVLPV----EELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRM 1636
Cdd:cd17651   81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTlldqPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1637 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQR 1716
Cdd:cd17651  161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1717 LAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAHYPDLPPIGRPLDGV 1796
Cdd:cd17651  241 LAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1797 EVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKV 1876
Cdd:cd17651  321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKI 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1877 RGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPEA-VDLAELKQALRSELPEHMVPAHFAWVDG 1955
Cdd:cd17651  401 RGFRIELGEIEAALA----RHPGVREAVVLAREDRPGEKRLVAYVVGDPEApVDAAELRAALATHLPEYMVPSAFVLLDA 476

                        490
                 ....*....|....*
gi 15598523 1956 FALTPSGKRDDAALR 1970
Cdd:cd17651  477 LPLTPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 473-876 3.26e-155

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: 486.77  E-value: 3.26e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    473 SYAELDAKVQAVADALRAA-GVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDE 551
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    552 RAATLGESLGETRVLHLERL-----PQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGE 626
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLElaaldDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    627 RDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRD-AVTVIHFVPSMLTPFLDLLDGDPtaraaa 705
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEhPVTVLNLTPSLLALLAAALPPAL------ 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    706 SSLRLVFCSGEALAPLQVARFRRLFGDAvRLVNLYGPTEATVDVSDHECASDNPTR---VPIGRPIDNLRLYVLDRALRP 782
Cdd:TIGR01733  235 ASLRLVILGGEALTPALVDRWRARGPGA-RLINLYGPTETTVWSTATLVDPDDAPRespVPIGRPLANTRLYVLDDDLRP 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    783 QPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFV--AGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDE 860
Cdd:TIGR01733  314 VPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393

                          410
                   ....*....|....*.
gi 15598523    861 VRDRLAALPGVRDAAV 876
Cdd:TIGR01733  394 IEAALLRHPGVREAVV 409
AMP-binding pfam00501
AMP-binding enzyme;
451-852 1.72e-112

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 365.10  E-value: 1.72e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    451 FAEQVARTPQRTALLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDH 530
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    531 PLERVRLLLEDCGARVVLVDERA------ATLGESLGETRVLHLERLPQSTGDL-------------PAANVAPGDLAYV 591
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellEALGKLEVVKLVLVLDRDPVLKEEPlpeeakpadvpppPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    592 IYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYP----IGERDVLLQKTPVTFDVSV-WELFWWSFTGARLSLLPPGAEKDP 666
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    667 REMLRSIQRDAVTVIHFVPSMltpFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAVrlVNLYGPTEAT 746
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTL---LNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGAL--VNGYGLTETT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    747 VDVSDHECASDNPTRVP-IGRPIDNLRLYVLDRA-LRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDpfvaggRL 824
Cdd:pfam00501  316 GVVTTPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------GW 389

                          410       420
                   ....*....|....*....|....*...
gi 15598523    825 YRTGDLARWLADGNLEYLGRADDQVKIR 852
Cdd:pfam00501  390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 2077-2341 5.16e-28

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 114.02  E-value: 5.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2077 PPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAY 2156
Cdd:pfam00975    1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2157 EMARQLRALDPQaVAQLIVLDsitvdrnhaGSASdealllffywELVWFERSDKeveplpegASLEQKLDHIveRAIEAG 2236
Cdd:pfam00975   81 EVARRLERQGEA-VRSLFLSD---------ASAP----------HTVRYEASRA--------PDDDEVVAEF--TDEGGT 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2237 VLPAGTPRATVQRLYELFRASWQALIGYRPEVSDQDMTLLRADGPLPLALKPMHDAagthygdpknGWQHWTSGRLDVID 2316
Cdd:pfam00975  131 PEELLEDEELLSMLLPALRADYRALESYSCPPLDAQSATLFYGSDDPLHDADDLAE----------WVRDHTPGEFDVHV 200

                          250       260
                   ....*....|....*....|....*
gi 15598523   2317 VPGDHLVLMKEPyvETVAAEIAALL 2341
Cdd:pfam00975  201 FDGDHFYLIEHL--EAVLEIIEAKL 223
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 2071-2345 3.04e-11

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 65.64  E-value: 3.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2071 RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGST--PLAVLEDIAASYLAAIRRvQPEGPYYLGGW 2148
Cdd:COG3208    1 PRPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGepPLTSLEELADDLAEELAP-LLDRPFALFGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2149 SFGGFVAYEMARQLRALDPQAVAQLIVldS------ITVDRNHAGSASDEALLlffyWELVWFERSDKEVEPLPEGASLe 2222
Cdd:COG3208   80 SMGALLAFELARRLERRGRPLPAHLFV--SgrraphLPRRRRPLHDLSDAELL----AELRRLGGTPEEVLADPELLEL- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2223 qkldhiveraieagVLPAgtpratvqrlyelFRASWQALIGYRPevsdqdmtllRADGPLPLalkPMHDAAGTHygDPK- 2301
Cdd:COG3208  153 --------------FLPI-------------LRADFRLLETYRY----------TPGPPLDC---PITALGGDD--DPLv 190

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15598523 2302 -----NGWQHWTSGRLDVIDVPGDHLVLMKEPyvETVAAEIAALLEPST 2345
Cdd:COG3208  191 speelAAWREHTTGPFRLRVFPGGHFFLRDHP--AELLALIRAALAALA 237
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1991-2058 5.12e-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: 49.56  E-value: 5.12e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523    1991 RTLAGLLGeLLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRER 2058
Cdd:smart00823   19 EQVAAVLG-HAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 2071-2173 3.88e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 41.85  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  2071 RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQgSTPLAV---LEDIAASYLAAIRRVQPEgPYYLGG 2147
Cdd:PRK14875  126 LGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGA-SSKAVGagsLDELAAAVLAFLDALGIE-RAHLVG 203

                          90       100
                  ....*....|....*....|....*.
gi 15598523  2148 WSFGGFVAYEMARQlralDPQAVAQL 2173
Cdd:PRK14875  204 HSMGGAVALRLAAR----APQRVASL 225
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 4-2072 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1043.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     4 FARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEA 83
Cdd:PRK12467   47 FERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    84 RHVDLRA--DRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGEL 160
Cdd:PRK12467  127 PLDDLANeqGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTlHHIISDGWSMRVLVEELVQLYSAYS 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   161 GEPQAQMPTAsllaQLETDDY-----SGSEQYRGDR--AYFAEALEGLEPAL---FTRRRPAGLR-RTARHRLTLERTLL 229
Cdd:PRK12467  207 QGREPSLPAL----PIQYADYaiwqrSWLEAGERERqlAYWQEQLGGEHTVLelpTDRPRPAVPSyRGARLRVDLPQALS 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   230 DAI----RDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLR 305
Cdd:PRK12467  283 AGLkalaQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVK 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   306 EATRTLLRHQKMPLGDLLR--------GASPLF------DTTLSYMRWPAAQAIPNASVETVaQTHAHDpdalAIWVSEF 371
Cdd:PRK12467  363 RTALGAQAHQDLPFEQLVEalqperslSHSPLFqvmfnhQNTATGGRDREGAQLPGLTVEEL-SWARHT----AQFDLAL 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   372 DGHSDAQ---VDFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLp 448
Cdd:PRK12467  438 DTYESAQglwAAFTYATDLFEAT-TIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVH- 515

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   449 TLFAEQVARTPQRTALLeADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINP 528
Cdd:PRK12467  516 QLIEAQARQHPERPALV-FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   529 DHPLERVRLLLEDCGARVVLVDERAATLGESLGETRVLHLER----LPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGV 604
Cdd:PRK12467  595 EYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEpadlLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGV 674

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   605 MVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFV 684
Cdd:PRK12467  675 AISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIV 754

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   685 PSMLTPFLdlldgDPTARAAASSLRLVFCSGEALAPLQVARFRRLfGDAVRLVNLYGPTEATVDVSDHECASDN--PTRV 762
Cdd:PRK12467  755 PSHLQALL-----QASRVALPRPQRALVCGGEALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYELSDEErdFGNV 828

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   763 PIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA-GGRLYRTGDLARWLADGNLEY 841
Cdd:PRK12467  829 PIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEY 908

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   842 LGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAvRGTHLVGYYVAAAELDPGQ-------LRAGLSATLPDF 914
Cdd:PRK12467  909 LGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVPAAVADGAEhqatrdeLKAQLRQVLPDY 987

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   915 MLPAFFVRIDSLPLSANGKLDRRQLPAP---PEQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRI 991
Cdd:PRK12467  988 MVPAHLLLLDSLPLTPNGKLDRKALPKPdasAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQV 1067

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   992 RAAAQRR-GLGFELADLMRNPTVAGLAERLVrplaerSYQPFELVSEVDKPRLEGLEDAFPTSRlslgLLFHSRQRPDSS 1070
Cdd:PRK12467 1068 ISRVRQRlGIQVPLRTLFEHQTLAGFAQAVA------AQQQGAQPALPDVDRDQPLPLSYAQER----QWFLWQLEPGSA 1137

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1071 VYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGAsEPLQLVHTQArsePLILDLRgNPEAGTVLDEHIR--- 1147
Cdd:PRK12467 1138 AYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDG-RTRQVIHPVG---SLTLEEP-LLLAADKDEAQLKvyv 1212

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1148 QRRFHR-YSLQQpGLFLFAAFVR--EDGLDLVFSFHHAILDGWSVANLIVALVAAYR----GEPLPGPAPAL-----ACH 1215
Cdd:PRK12467 1213 EAEARQpFDLEQ-GPLLRVGLLRlaADEHVLVLTLHHIVSDGWSMQVLVDELVALYAaysqGQSLQLPALPIqyadyAVW 1291

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1216 VREELAALASPAAVGYWTGLLeGARMTRLDGFGAHEPQAAQG--PASHREALPDGLLERLKATAAQRGLPLKSLLLAAHC 1293
Cdd:PRK12467 1292 QRQWMDAGERARQLAYWKAQL-GGEQPVLELPTDRPRPAVQShrGARLAFELPPALAEGLRALARREGVTLFMLLLASFQ 1370

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1294 LTLHLFSRSDSVVTGA-ISN-GRPElpdADRMVGLFLNTVPVRSEIAGCSWIEvadALFRQER----DGHAHRRYPLSAI 1367
Cdd:PRK12467 1371 TLLHRYSGQDDIRVGVpIANrNRAE---TEGLIGFFVNTQVLRAEVDGQASFQ---QLLQQVKqaalEAQAHQDLPFEQL 1444

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1368 QQIVGDELSSAFNyvnlhvlePLWQ---------------LRDFRV----WEE--TNFALLVNvIATPSDGMYLRIDSDG 1426
Cdd:PRK12467 1445 VEALQPERSLSHS--------PLFQvmfnhqrddhqaqaqLPGLSVeslsWESqtAQFDLTLD-TYESSEGLQASLTYAT 1515

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1427 RGISRSQAALIGATFVELLWRLADHPDE-AADFAFLAP--RR------DAASQPEPLVDVV-SLFERQVEALPGSAALAF 1496
Cdd:PRK12467 1516 DLFEASTIERLAGHWLNLLQGLVADPERrLGELDLLDEaeRRqilegwNATHTGYPLARLVhQLIEDQAAATPEAVALVF 1595

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1497 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRV 1576
Cdd:PRK12467 1596 GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELL 1675

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1577 VAHPEHAH---VAAAERVLPVEELVADIEPETFAAPQL----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVAS 1649
Cdd:PRK12467 1676 LTQSHLQArlpLPDGLRSLVLDQEDDWLEGYSDSNPAVnlapQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQ 1755

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1650 GVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPG 1729
Cdd:PRK12467 1756 LSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE-HPL 1834

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1730 ALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPV 1808
Cdd:PRK12467 1835 SLRRVVCGGEALEV-EALRPWLERLPDTGLFNLYGPTETAvDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPV 1913

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1809 PVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 1887
Cdd:PRK12467 1914 PIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1888 lAIMRQaerQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL--------AELKQALRSELPEHMVPAHFAWVDGFALT 1959
Cdd:PRK12467 1994 -ARLRE---QGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLT 2069

                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1960 PSGKRDDAALRALP---LEHGtnieYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRfMLLIEKRYGVD 2036
Cdd:PRK12467 2070 PNGKLDRKALPAPDaseLQQA----YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQ-VVSRARQAGIR 2144

                        2170      2180      2190      2200
                  ....*....|....*....|....*....|....*....|....
gi 15598523  2037 LPMAALIETPTVEGLAERLRE--------RSAVRAFDPLVPIRA 2072
Cdd:PRK12467 2145 FTPKDLFQHQTVQSLAAVAQEgdgtvsidQGPVTGDLPLLPIQQ 2188
PRK12316 PRK12316
peptide synthase; Provisional
 41-2071 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 971.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    41 VDTQALE----RALLQAARDT-EAFRLRLGETDG--TPYQWLDTDAEFEARHVDLRADRDPEAAVRSWLRDAFRHAYPLD 113
Cdd:PRK12316 1585 VDVQGLDpdrfRAAWQATVDRhEILRSGFLWQDGleQPLQVIHKQVELPFAELDWRGREDLGQALDALAQAERQKGFDLT 1664

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   114 GRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGELGePQAQMPTASLLAQLETDDYSGSEqyrgdrA 192
Cdd:PRK12316 1665 RAPLLRLVLVRTGEGRHHLIYTnHHILMDGWSNAQLLGEVLQRYAGQPV-AAPGGRYRDYIAWLQRQDAAASE------A 1737

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   193 YFAEALEGL-EPALFTR--RRPAGLRRTARHRltlerTLLDAIRDRGESPF---------LFLSAAVALYLARIHQNDDV 260
Cdd:PRK12316 1738 FWKEQLAALeEPTRLAQaaRTEDGQVGYGDHQ-----QLLDPAQTRALAEFaraqkvtlnTLVQAAWLLLLQRYTGQETV 1812

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   261 VLGVPVLNR-ADRAA-KQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTLLRHQKMPLGDLLR----GASPLFDTTL 334
Cdd:PRK12316 1813 AFGATVAGRpAELPGiEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRwagqGGEALFDSLL 1892

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   335 SYMRWPAAQAIPNASV------ETVAQTHAHDPDALAIWVSEfdghsDAQVDFEYACDVFDADfPMDAAARHIETFLRAL 408
Cdd:PRK12316 1893 VFENYPVAEALKQGAPaglvfgRVSNHEQTNYPLTLAVTLGE-----TLSLQYSYDRGHFDAA-AIERLDRHLLHLLEQM 1966

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   409 VEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVARTPQRTALLeADGGTLSYAELDAKVQAVADAL 488
Cdd:PRK12316 1967 AEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVV-FGDQHLSYAELDSRANRLAHRL 2045

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   489 RAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDEraaTLGESL---GETRV 565
Cdd:PRK12316 2046 RARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR---HLLERLplpAGVAR 2122

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   566 LHLER---LPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSV 642
Cdd:PRK12316 2123 LPLDRdaeWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAH 2202

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   643 WELFWWSFTGARLsLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLL--DGDPTAraaassLRLVFCSGEALAp 720
Cdd:PRK12316 2203 EQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAerDGRPPA------VRVYCFGGEAVP- 2274

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   721 lqVARFRRLFG--DAVRLVNLYGPTEATVDVSDHECASDNP---TRVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGG 795
Cdd:PRK12316 2275 --AASLRLAWEalRPVYLFNGYGPTEAVVTPLLWKCRPQDPcgaAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGG 2352

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   796 VGVARGYLNRPELNAERFLVDPFVA-GGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDA 874
Cdd:PRK12316 2353 EGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREA 2432

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   875 AVVARDSAvRGTHLVGYYVA--AAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPAPP---EQVAAV 949
Cdd:PRK12316 2433 VVVAQDGA-SGKQLVAYVVPddAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDvsqLRQAYV 2511

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   950 APRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLR-IRAAAQRRGLGFELADLMRNPTVAGLAERLVRPLAERS 1028
Cdd:PRK12316 2512 APQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQvVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRA 2591

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1029 yqpfelVSEVDKPRLEGLEDAFPTSRLSlgllFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFD 1108
Cdd:PRK12316 2592 ------PVLQKVTRVQPLPLSHAQQRQW----FLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFV 2661

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1109 LSGaSEPLQLVHTQARSEPLILDlrgnpeAGTVLDEHIRQR---RFHRYSLQQPGLFLFAAFVREDGLD--LVFSFHHAI 1183
Cdd:PRK12316 2662 EVG-EQTRQVILPNMSLRIVLED------CAGVADAAIRQRvaeEIQRPFDLARGPLLRVRLLALDGQEhvLVITQHHIV 2734

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1184 LDGWSVANLIVALVAAYRGE---------PLPGPAPALACHVREELAALASPAAVGYWTGLLEGAR-MTRLDGFGAHEPQ 1253
Cdd:PRK12316 2735 SDGWSMQVMVDELVQAYAGArrgeqptlpPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQpVLELPLDRPRPAL 2814

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1254 AAQGPASHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRpELPDADRMVGLFLNTVPV 1333
Cdd:PRK12316 2815 QSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR-NRAETERLIGFFVNTQVL 2893

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1334 RSEI-AGCSWIEVADALFRQERDGHAHRRYPL----SAIQQIVGDELSSAFNYVNLH--------VLEPLWQLRDFRVWE 1400
Cdd:PRK12316 2894 RAQVdAQLAFRDLLGQVKEQALGAQAHQDLPFeqlvEALQPERSLSHSPLFQVMYNHqsgeraaaQLPGLHIESFAWDGA 2973

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1401 ETNFALLVNVIATPsDGMYLRIDSDGRGISRSQAALIGATFVELLWRLADHPDEAADFAFL-----------APRRDAAS 1469
Cdd:PRK12316 2974 ATQFDLALDTWESA-EGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMldaeergqlleAWNATAAE 3052

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1470 QPEPLvDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG 1549
Cdd:PRK12316 3053 YPLER-GVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAG 3131

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1550 LVCVPLDVSYPAQRLALILET--AQPFRVVAHPEHAHVAAAERVL--PVEELVADIEPETFAAPQldELAMLLFTSGSTG 1625
Cdd:PRK12316 3132 GAYVPLDPEYPEERLAYMLEDsgAQLLLSQSHLRLPLAQGVQVLDldRGDENYAEANPAIRTMPE--NLAYVIYTSGSTG 3209

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1626 RPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQ 1705
Cdd:PRK12316 3210 KPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVD 3289

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1706 rvLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCaampGLLLENQYGPTETHQVTYHSLSGDPahYPD 1785
Cdd:PRK12316 3290 --VLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFA----GLPLYNLYGPTEATITVTHWQCVEE--GKD 3361

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1786 LPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIV 1865
Cdd:PRK12316 3362 AVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIE 3441

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1866 WLGRADTQVKVRGFRIEPAEVElAIMRQaerQPGLRGAAVVARERQGndafLAAFLLGEPEAVDLAE-LKQALRSELPEH 1944
Cdd:PRK12316 3442 YIGRVDHQVKIRGFRIELGEIE-ARLLE---HPWVREAVVLAVDGRQ----LVAYVVPEDEAGDLREaLKAHLKASLPEY 3513

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1945 MVPAHFAWVDGFALTPSGKRDDAALRAlPLEHGTNIEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMR 2024
Cdd:PRK12316 3514 MVPAHLLFLERMPLTPNGKLDRKALPR-PDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQ 3592

                        2090      2100      2110      2120      2130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15598523  2025 FMLLIeKRYGVDLPMAALIETPTVEGLAERLR-------ERSAVRAFDPLVPIR 2071
Cdd:PRK12316 3593 VVSRA-RQAGIRFTPKDLFQHQTIQGLARVARvgggvavDQGPVSGETLLLPIQ 3645
PRK05691 PRK05691
peptide synthase; Validated
 7-2020 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 944.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     7 LPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEARHV 86
Cdd:PRK05691  676 LPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRI 755

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    87 DLRADRDPEAAVRSWLR--DAFRHAYPLDGRSLVDLALLH-SDQALYVYVRTHHIVSDAWGLQLFL---SRVRAGYLGel 160
Cdd:PRK05691  756 DLSDLPEAEREARAAQIreEEARQPFDLEKGPLLRVTLVRlDDEEHQLLVTLHHIVADGWSLNILLdefSRLYAAACQ-- 833

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   161 GEPQAQMPTASLLAQLET--DDYSGSEQYRGDRAYFAEALEGLEPAL-FTRRRPAGLRR---TARHRLTLERTLLDAIR- 233
Cdd:PRK05691  834 GQTAELAPLPLGYADYGAwqRQWLAQGEAARQLAYWKAQLGDEQPVLeLATDHPRSARQahsAARYSLRVDASLSEALRg 913

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   234 ---DRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRT 310
Cdd:PRK05691  914 laqAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLG 993

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   311 LLRHQKMPLGDLLR-----GASPLFDTTLSYMR--WPAAQAIPNASVETVAQtHAHDPDALAIWVSEFDGHSDAQVDFEY 383
Cdd:PRK05691  994 AQAHQDLPFEQLVEalpqaREQGLFQVMFNHQQrdLSALRRLPGLLAEELPW-HSREAKFDLQLHSEEDRNGRLTLSFDY 1072

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   384 ACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATdqAFPEQATLPTLFAEQVARTPQRTA 463
Cdd:PRK05691 1073 AAELFDAA-TIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAP--CAPAQAWLPELLNEQARQTPERIA 1149

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   464 lLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCG 543
Cdd:PRK05691 1150 -LVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   544 ARVVLVDERA-ATLGESLGETRV----LHLERLPQSTgdlPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWM 618
Cdd:PRK05691 1229 VELLLTQSHLlERLPQAEGVSAIaldsLHLDSWPSQA---PGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1305

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   619 QRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDlldgD 698
Cdd:PRK05691 1306 QATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFID----E 1381

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   699 PTArAAASSLRLVFCSGEALAPLQVARFRRLFgDAVRLVNLYGPTEATVDVSDHECASDNPTRVPIGRPIDNLRLYVLDR 778
Cdd:PRK05691 1382 PLA-AACTSLRRLFSGGEALPAELRNRVLQRL-PQVQLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDA 1459

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   779 ALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFV-AGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVE 857
Cdd:PRK05691 1460 ELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVE 1539

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   858 PDEVRDRLAALPGVRDAAVVARDSAVrGTHLVGYYVAAAELD--PGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLD 935
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQAAVLVREGAA-GAQLVGYYTGEAGQEaeAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLD 1618

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   936 RRQLPAPPEQVAA-VAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRA-AAQRRGLGFELADLMRNPTV 1013
Cdd:PRK05691 1619 RRALPEPVWQQREhVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSrTRQACDVELPLRALFEASEL 1698

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1014 AGLAE--RLVRPLAERSYQPfeLVSEVDKprleglEDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRH 1091
Cdd:PRK05691 1699 GAFAEqvARIQAAGERNSQG--AIARVDR------SQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEA 1770

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1092 ALDRVVAAYPALRSSFDlSGASEPLQLVHTQArseplilDLRGNPEAGTVLDEHIRQRRFHRYS---LQQP-----GLFL 1163
Cdd:PRK05691 1771 ALQALILRHETLRTTFP-SVDGVPVQQVAEDS-------GLRMDWQDFSALPADARQQRLQQLAdseAHQPfdlerGPLL 1842

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1164 FAAFVREDGLD--LVFSFHHAILDGWSV---ANLIVALVAAY---RGEPL-PGPAPALACHV--REELAALASPAAVGYW 1232
Cdd:PRK05691 1843 RACLVKAAEREhyFVLTLHHIVTEGWAMdifARELGALYEAFlddRESPLePLPVQYLDYSVwqRQWLESGERQRQLDYW 1922

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1233 TGLLegARMTRLDGFGAHEP----QAAQGPAsHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTG 1308
Cdd:PRK05691 1923 KAQL--GNEHPLLELPADRPrppvQSHRGEL-YRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIG 1999

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1309 AISNGRPElPDADRMVGLFLNTVPVRSEIAGCSwieVADALFRQER----DGHAHRRYPLSAIQQIVGDELSSAFNyvnl 1384
Cdd:PRK05691 2000 APVANRIR-PESEGLIGAFLNTQVLRCQLDGQM---SVSELLEQVRqtviEGQSHQDLPFDHLVEALQPPRSAAYN---- 2071

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1385 hvlePL---------WQLRDFRVWEETNFALLVN-VIATPSDgMYLRI-DSDGR-----GISRS-----QAALIGATFVE 1443
Cdd:PRK05691 2072 ----PLfqvmcnvqrWEFQQSRQLAGMTVEYLVNdARATKFD-LNLEVtDLDGRlgcclTYSRDlfdepRIARMAEHWQN 2146

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1444 LLWRLADHP----------DEAADFAFLAPRRDAASQPEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDhvARcv 1513
Cdd:PRK05691 2147 LLEALLGDPqqrlaelpllAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELD--AR-- 2222

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1514 ATRLVRAGARRGDA----IGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAqpfRVVAHPEHAHVAAAE 1589
Cdd:PRK05691 2223 ANRLARALRERGVGpqvrVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDS---GIGLLLSDRALFEAL 2299

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1590 RVLPV--------EELVA-----DIEPETFAAPQldELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRT 1656
Cdd:PRK05691 2300 GELPAgvarwcleDDAAAlaaysDAPLPFLSLPQ--HQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCE 2377

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1657 LQFAPLSFDMAFQEIFSTLCGGGELQLisnrermdpsallhvleRRQVQRVLLPFVALQRlAEASNALGVRPG------- 1729
Cdd:PRK05691 2378 LHFYSINFDAASERLLVPLLCGARVVL-----------------RAQGQWGAEEICQLIR-EQQVSILGFTPSygsqlaq 2439

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1730 ---------ALRVVVSSGEQLrITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDpahypDLP------PIGRPLD 1794
Cdd:PRK05691 2440 wlagqgeqlPVRMCITGGEAL-TGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPE-----QLEegaasvPIGRVVG 2513

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1795 GVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRP-GARLYRTGDLGRILGNGEIVWLGRADTQ 1873
Cdd:PRK05691 2514 ARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQ 2593

                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1874 VKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAfLAAFLLGEPEAVDLAE-------LKQALRSELPEHMV 1946
Cdd:PRK05691 2594 VKIRGFRIELGEIESRLL----EHPAVREAVVLALDTPSGKQ-LAGYLVSAVAGQDDEAqaalreaLKAHLKQQLPDYMV 2668

                        2090      2100      2110      2120      2130      2140      2150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523  1947 PAHFAWVDGFALTPSGKRDDAALRALPLEHGTNiEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSL 2020
Cdd:PRK05691 2669 PAHLILLDSLPLTANGKLDRRALPAPDPELNRQ-AYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSI 2741
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-1309 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: 817.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    1 MVRFARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAE 80
Cdd:COG1020   12 AAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   81 FEARHVDLRAD---RDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRTHHIVSDAW----GLQLFLSRVR 153
Cdd:COG1020   92 APLPVVVLLVDleaLAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLsdglLLAELLRLYL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  154 AGYLGELGEPQAQMPTASLLAQLETDDYSGSEQYRgDRAYFAEALEGLEPAL---FTRRRPAGLR-RTARHRLTLERTLL 229
Cdd:COG1020  172 AAYAGAPLPLPPLPIQYADYALWQREWLQGEELAR-QLAYWRQQLAGLPPLLelpTDRPRPAVQSyRGARVSFRLPAELT 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  230 DAIRDRGE----SPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLR 305
Cdd:COG1020  251 AALRALARrhgvTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVR 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  306 EATRTLLRHQKMPLGDLLR--------GASPLFDTTLSYMRWPA-AQAIPNASVETVAQTHAHDPDALAIWVSEFDGHsd 376
Cdd:COG1020  331 ETLLAAYAHQDLPFERLVEelqperdlSRNPLFQVMFVLQNAPAdELELPGLTLEPLELDSGTAKFDLTLTVVETGDG-- 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  377 AQVDFEYACDVFDADFpMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVA 456
Cdd:COG1020  409 LRLTLEYNTDLFDAAT-IERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAA 487

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  457 RTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVR 536
Cdd:COG1020  488 RTPDAVAV-VFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLA 566

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  537 LLLEDCGARVVLVDER-AATLGESLGETRVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRL 615
Cdd:COG1020  567 YMLEDAGARLVLTQSAlAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLL 646

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  616 NWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDll 695
Cdd:COG1020  647 AWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLD-- 724

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  696 dgdpTARAAASSLRLVFCSGEALAPLQVARFRRLFGDaVRLVNLYGPTEATVDVSDHECASDNPT--RVPIGRPIDNLRL 773
Cdd:COG1020  725 ----AAPEALPSLRLVLVGGEALPPELVRRWRARLPG-ARLVNLYGPTETTVDSTYYEVTPPDADggSVPIGRPIANTRV 799

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  774 YVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPF-VAGGRLYRTGDLARWLADGNLEYLGRADDQVKIR 852
Cdd:COG1020  800 YVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIR 879

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  853 GNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAE--LDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSA 930
Cdd:COG1020  880 GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGaaAAAALLRLALALLLPPYMVPAAVVLLLPLPLTG 959

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  931 NGKLDRRQLPAPPEQVAA--VAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQRRGLGFELADLM 1008
Cdd:COG1020  960 NGKLDRLALPAPAAAAAAaaAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1009 RNPTVAGLAERLVRPLAERSYQPfelvsevdkPRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAA 1088
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAP---------LAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1089 FRHALDRVVAAYPALRSSFDLsgASEPLQLVHTQARSEPLILDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAFV 1168
Cdd:COG1020 1111 LLLLLALLLALLAALRARRAV--RQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLL 1188

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1169 REDGLDLVFSFHHAILDGWSVANLIVALVAAYRGEPLPGPAPALACHVREELAALASPAAVGYWTGLLEGARMTRLDGFG 1248
Cdd:COG1020 1189 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLA 1268

                       1290      1300      1310      1320      1330      1340
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523 1249 AHEPQAAQGPASHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGA 1309
Cdd:COG1020 1269 LALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
5-1035 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 751.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     5 ARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEF-EA 83
Cdd:PRK10252    6 QHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFpLP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    84 RHVDLRADRDPEAAVRSWLRDAFRHAYPLD-GRSLVDLALLH-SDQALYVYVRTHHIVSDAWGLQLFLSRVRAGYLGEL- 160
Cdd:PRK10252   86 EIIDLRTQPDPHAAAQALMQADLQQDLRVDsGKPLVFHQLIQlGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLr 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   161 GEPQAQMPTASLLAQLETDD-YSGSEQYRGDRAYFAEALEGL-EPALFTRRRPAGLRRTAR-HRLTLERTLLDAIRDRGE 237
Cdd:PRK10252  166 GEPTPASPFTPFADVVEEYQrYRASEAWQRDAAFWAEQRRQLpPPASLSPAPLPGRSASADiLRLKLEFTDGAFRQLAAQ 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   238 SPFL----FLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTLLR 313
Cdd:PRK10252  246 ASGVqrpdLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRR 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   314 HQKMPLGDLLR------GASPLFDTTLSYMRWPAAQAIPNasVETVAQTHAHDP-DALAIWVSEfDGHSDAQVDFEYACD 386
Cdd:PRK10252  326 HQRYDAEQIVRdsgraaGDEPLFGPVLNIKVFDYQLDFPG--VQAQTHTLATGPvNDLELALFP-DEHGGLSIEILANPQ 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   387 VFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELiHTRNATDQAFPEQaTLPTLFAEQVARTPQRTALLe 466
Cdd:PRK10252  403 RYDEA-TLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQL-AQVNATAVEIPET-TLSALVAQQAAKTPDAPALA- 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   467 ADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARV 546
Cdd:PRK10252  479 DARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSL 558

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   547 VL-VDERAATLGESLGETrVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIG 625
Cdd:PRK10252  559 LItTADQLPRFADVPDLT-SLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLT 637

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   626 ERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDpTARAAA 705
Cdd:PRK10252  638 ADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPE-GARQSC 716

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   706 SSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVSDH-----ECASDNPTRVPIGRPIDNLRLYVLDRAL 780
Cdd:PRK10252  717 ASLRQVFCSGEALPADLCREWQQLTG--APLHNLYGPTEAAVDVSWYpafgeELAAVRGSSVPIGYPVWNTGLRILDARM 794

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   781 RPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDE 860
Cdd:PRK10252  795 RPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGE 874

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   861 VRDRLAALPGVRDAAVVAR------DSAVRGTHLVGYYVAA--AELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANG 932
Cdd:PRK10252  875 IDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQsgLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANG 954

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   933 KLDRRQLPAPP--EQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIrAAAQRRGLGFE--LADLM 1008
Cdd:PRK10252  955 KLDRKALPLPElkAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKL-AAQLSRQFARQvtPGQVM 1033

                        1050      1060
                  ....*....|....*....|....*..
gi 15598523  1009 RNPTVAGLAERLVRPLAERSYQPFELV 1035
Cdd:PRK10252 1034 VASTVAKLATLLDAEEDESRRLGFGTI 1060
PRK12467 PRK12467
peptide synthase; Provisional
 3-1334 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 691.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     3 RFARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFE 82
Cdd:PRK12467 1113 RDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLT 1192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    83 ARHVDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYlgelg 161
Cdd:PRK12467 1193 LEEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTlHHIVSDGWSMQVLVDELVALY----- 1267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   162 EPQAQMPTASLLA-QLETDDYS--------GSEQYRgDRAYFAEALEGLEPAL---FTRRRPA-GLRRTARHRLTLERTL 228
Cdd:PRK12467 1268 AAYSQGQSLQLPAlPIQYADYAvwqrqwmdAGERAR-QLAYWKAQLGGEQPVLelpTDRPRPAvQSHRGARLAFELPPAL 1346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   229 LDAIRDR----GESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQL 304
Cdd:PRK12467 1347 AEGLRALarreGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQV 1426

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   305 REATRTLLRHQKMPLGDLLR--------GASPLFDTTLSYMR--WPAAQAIPNASVETVAQTHAHDPDALAIwvSEFDGH 374
Cdd:PRK12467 1427 KQAALEAQAHQDLPFEQLVEalqperslSHSPLFQVMFNHQRddHQAQAQLPGLSVESLSWESQTAQFDLTL--DTYESS 1504

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   375 SDAQVDFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQ 454
Cdd:PRK12467 1505 EGLQASLTYATDLFEAS-TIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQ 1583

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   455 VARTPQRTALLEAdGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLER 534
Cdd:PRK12467 1584 AAATPEAVALVFG-EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER 1662

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   535 VRLLLEDCGARVVLVDERAATLGESLGETRVLHLER----LPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRS 610
Cdd:PRK12467 1663 LAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQeddwLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGA 1742

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   611 VVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTP 690
Cdd:PRK12467 1743 LVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQ 1822

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   691 FLDLldgdPTARAAASSLRLVFCSGEALAP-LQVARFRRLfgDAVRLVNLYGPTEATVDVSDHECASDNPT---RVPIGR 766
Cdd:PRK12467 1823 LLQM----DEQVEHPLSLRRVVCGGEALEVeALRPWLERL--PDTGLFNLYGPTETAVDVTHWTCRRKDLEgrdSVPIGQ 1896

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   767 PIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPF-VAGGRLYRTGDLARWLADGNLEYLGRA 845
Cdd:PRK12467 1897 PIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRI 1976

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   846 DDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAvRGTHLVGYYVAAAELDP----------GQLRAGLSATLPDFM 915
Cdd:PRK12467 1977 DHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVPTDPGLVdddeaqvalrAILKNHLKASLPEYM 2055

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   916 LPAFFVRIDSLPLSANGKLDRRQLPAPPE---QVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIR 992
Cdd:PRK12467 2056 VPAHLVFLARMPLTPNGKLDRKALPAPDAselQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVV 2135

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   993 AAAQRRGLGFELADLMRNPTVAGLAERLVRPLAERSyqpfelvseVDKPRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVY 1072
Cdd:PRK12467 2136 SRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVS---------IDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVL 2206

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1073 HDVFHyrfdlAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARSEPLI----------LDLRGNpEAGTVL 1142
Cdd:PRK12467 2207 LEPRE-----ALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEQERRPLLwqvvvadkeeLEALCE-QAQRSL 2280

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1143 DehirqrrfhrysLQQ-PGLFLFAAFVREDGLDLVFSFHHAILDGWSVANLIVALVAAYR----GEPLPGPAPALACHV- 1216
Cdd:PRK12467 2281 D------------LEEgPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRqlqgGQPVKLPAKTSAFKAw 2348

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1217 REELAALASPAA----VGYWTGLLEGARmtrlDGFGAHEPQAAQG---PASHREALPDGLLERL--KATAAQRgLPLKSL 1287
Cdd:PRK12467 2349 AERLQTYAASAAladeLGYWQAQLQGAS----TELPCDHPQGGLQrrhAASVTTHLDSEWTRRLlqEAPAAYR-TQVNDL 2423

                        1370      1380      1390      1400      1410
                  ....*....|....*....|....*....|....*....|....*....|
gi 15598523  1288 LLAAHCLTLHLFSRSDSVVTGAISNGRPEL-PDAD--RMVGLFLNTVPVR 1334
Cdd:PRK12467 2424 LLTALARVIARWTGQASTLIQLEGHGREDLfDEIDltRTVGWFTSLYPVK 2473
PRK12316 PRK12316
peptide synthase; Provisional
 6-1334 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 667.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     6 RLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEARH 85
Cdd:PRK12316   49 RDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    86 VDLRADRDPEAAVRswLRDAFRHA----YPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGEL 160
Cdd:PRK12316  129 EDCSGLPEAEQEAR--LRDEAQREslqpFDLCEGPLLRVRLLRLGEEEHVLLLTlHHIVSDGWSMNVLIEEFSRFYSAYA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   161 GEPQAQMPTASLlaqlETDDYS--------GSEQYRgDRAYFAEALEGLEPAL---FTRRRPAGLR-RTARHRLTLERTL 228
Cdd:PRK12316  207 TGAEPGLPALPI----QYADYAlwqrswleAGEQER-QLEYWRAQLGEEHPVLelpTDHPRPAVPSyRGSRYEFSIDPAL 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   229 LDAIRD----RGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQL 304
Cdd:PRK12316  282 AEALRGtarrQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGV 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   305 REATRTLLRHQKMPLGDLLRG--------ASPLFDTTLSYMRWPAAQA----IPNASVETVAQTHAHDPDALAIWVSEFD 372
Cdd:PRK12316  362 KDTVLGAQAHQDLPFERLVEAlkverslsHSPLFQVMYNHQPLVADIEaldtVAGLEFGQLEWKSRTTQFDLTLDTYEKG 441

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   373 GHSDAQvdFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFA 452
Cdd:PRK12316  442 GRLHAA--LTYATDLFEAR-TVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFE 518

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   453 EQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPL 532
Cdd:PRK12316  519 EQVERTPEAPALAFGEE-TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPA 597

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   533 ERVRLLLEDCGARVVLVDERAATLGESLGETRVLHLER----LPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEH 608
Cdd:PRK12316  598 ERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRpaawLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRH 677

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   609 RSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSML 688
Cdd:PRK12316  678 RALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSML 757

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   689 TPFLDllDGDPtarAAASSLRLVFCSGEAL-APLQVARFRRLfgDAVRLVNLYGPTEATVDVSDHECASDNPTRVPIGRP 767
Cdd:PRK12316  758 QAFLQ--DEDV---ASCTSLRRIVCSGEALpADAQEQVFAKL--PQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRP 830

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   768 IDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADD 847
Cdd:PRK12316  831 IANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDH 910

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   848 QVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDsavrGTHLVGYYVAAAELD--PGQLRAGLSATLPDFMLPAFFVRIDS 925
Cdd:PRK12316  911 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGdwREALKAHLAASLPEYMVPAQWLALER 986

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   926 LPLSANGKLDRRQLPAPPEQVAA---VAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQRRGLGF 1002
Cdd:PRK12316  987 LPLTPNGKLDRKALPAPEASVAQqgyVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQL 1066

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1003 ELADLMRNPTVAGLAerlvrpLAERsyqpFELVSEVDKPRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVyhdVFHYRFDL 1082
Cdd:PRK12316 1067 SPRDLFQHQTIRSLA------LVAK----AGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSL---LLQARQPL 1133

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1083 awDEAAFRHALDRVVAAYPALRSSFDlsGASEPLQLVHTQARSEPLIL--DLRGNPEAGTVLDEhiRQRRFhrySLQQ-P 1159
Cdd:PRK12316 1134 --DPDRLGRALERLVAHHDALRLRFR--EEDGGWQQAYAAPQAGEVLWqrQAASEEELLALCEE--AQRSL---DLEQgP 1204

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1160 GLFLFAAFVREDGLDLVFSFHHAILDGWSVANLIVALVAAYRGEPLPGPA-----PALACHVREELAALAspAAVGYWTG 1234
Cdd:PRK12316 1205 LLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPArtssyQAWARRLHEHAGARA--EELDYWQA 1282

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1235 LLEGARmtrlDGFGAHEPQAAQGPASHREA---LPDGLLERL--KATAAQRgLPLKSLLLAAHCLTLHLFSRSDSVVTGA 1309
Cdd:PRK12316 1283 QLEDAP----HELPCENPDGALENRHERKLelrLDAERTRQLlqEAPAAYR-TQVNDLLLTALARVTCRWSGQASVLVQL 1357

                        1370      1380
                  ....*....|....*....|....*...
gi 15598523  1310 ISNGRPELPDA---DRMVGLFLNTVPVR 1334
Cdd:PRK12316 1358 EGHGREDLFEDidlSRTVGWFTSLFPVR 1385
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1481-1970 0e+00

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: 654.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1481 FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 1560
Cdd:cd17651    1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1561 AQRLALILETAQPFRVVAHPEHAHVAAAERVLPV----EELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRM 1636
Cdd:cd17651   81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTlldqPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1637 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQR 1716
Cdd:cd17651  161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1717 LAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAHYPDLPPIGRPLDGV 1796
Cdd:cd17651  241 LAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1797 EVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKV 1876
Cdd:cd17651  321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKI 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1877 RGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPEA-VDLAELKQALRSELPEHMVPAHFAWVDG 1955
Cdd:cd17651  401 RGFRIELGEIEAALA----RHPGVREAVVLAREDRPGEKRLVAYVVGDPEApVDAAELRAALATHLPEYMVPSAFVLLDA 476

                        490
                 ....*....|....*
gi 15598523 1956 FALTPSGKRDDAALR 1970
Cdd:cd17651  477 LPLTPNGKLDRRALP 491
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 459-939 0e+00

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: 619.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:cd05930    1 PDAVAV-VDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  539 LEDCGARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWM 618
Cdd:cd05930   80 LEDSGAKLVLTD----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  619 QRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDgd 698
Cdd:cd05930  126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE-- 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  699 ptaRAAASSLRLVFCSGEALAPLQVARFRRLFGDaVRLVNLYGPTEATVDVSDHECASDN--PTRVPIGRPIDNLRLYVL 776
Cdd:cd05930  204 ---LAALPSLRLVLVGGEALPPDLVRRWRELLPG-ARLVNLYGPTEATVDATYYRVPPDDeeDGRVPIGRPIPNTRVYVL 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  777 DRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRV 856
Cdd:cd05930  280 DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  857 EPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAA--ELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKL 934
Cdd:cd05930  360 ELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439


                 ....*
gi 15598523  935 DRRQL 939
Cdd:cd05930  440 DRKAL 444
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 448-939 0e+00

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: 611.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  448 PTLFAEQVARTPQRTALLeADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPIN 527
Cdd:cd17646    1 HALVAEQAARTPDAPAVV-DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  528 PDHPLERVRLLLEDCGARVVLVDERAATLGESLGETRVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVE 607
Cdd:cd17646   80 PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  608 HRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSM 687
Cdd:cd17646  160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSM 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  688 LTPFLDLLdgdptARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVSDHEC-ASDNPTRVPIGR 766
Cdd:cd17646  240 LRVFLAEP-----AAGSCASLRRVFCSGEALPPELAARFLALPG--AELHNLYGPTEAAIDVTHWPVrGPAETPSVPIGR 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  767 PIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRAD 846
Cdd:cd17646  313 PVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSD 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  847 DQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAA---ELDPGQLRAGLSATLPDFMLPAFFVRI 923
Cdd:cd17646  393 DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaaGPDTAALRAHLAERLPEYMVPAAFVVL 472

                        490
                 ....*....|....*.
gi 15598523  924 DSLPLSANGKLDRRQL 939
Cdd:cd17646  473 DALPLTANGKLDRAAL 488
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1041-2296 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: 592.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1041 PRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVH 1120
Cdd:COG1020   12 AAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1121 TQARSEPLILDLRGNPEA---GTVLDEHIRQRRFHRYSLQQPGLFLFAAFVREDGLDLVFSFHHAILDGWSVANLIVALV 1197
Cdd:COG1020   92 APLPVVVLLVDLEALAEAaaeAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1198 AAYRGEPLPGPAPAL-----ACHVREELAALASPAAVGYWTGLLEGARmTRLDGFGAHEPQAAQGP--ASHREALPDGLL 1270
Cdd:COG1020  172 AAYAGAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLP-PLLELPTDRPRPAVQSYrgARVSFRLPAELT 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1271 ERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIAGC-SWIEVADAL 1349
Cdd:COG1020  251 AALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR-PELEGLVGFFVNTLPLRVDLSGDpSFAELLARV 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1350 FRQERDGHAHRRYPLSAIQQIVGDELS--------SAFNYVNLHVLE---PLWQLRDFRVWEET-NFALLVNVIATPsDG 1417
Cdd:COG1020  330 RETLLAAYAHQDLPFERLVEELQPERDlsrnplfqVMFVLQNAPADElelPGLTLEPLELDSGTaKFDLTLTVVETG-DG 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1418 MYLRIDSDGRGISRSQAALIGATFVELLWRLADHPDE---------AADFAFLAPRRDAASQPEPL-VDVVSLFERQVEA 1487
Cdd:COG1020  409 LRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQplgdlplltAAERQQLLAEWNATAAPYPAdATLHELFEAQAAR 488

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1488 LPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI 1567
Cdd:COG1020  489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1568 LETAQPFRVVAHPEHAHVAAAE--RVLPVEELVADIEPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHRMWANYTQW 1643
Cdd:COG1020  569 LEDAGARLVLTQSALAARLPELgvPVLALDALALAAEPATNPPVPVtpDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAW 648

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1644 QLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNA 1723
Cdd:COG1020  649 MQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE 728

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1724 lgvRPGALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHyPDLPPIGRPLDGVEVQVLD 1802
Cdd:COG1020  729 ---ALPSLRLVLVGGEALP-PELVRRWRARLPGARLVNLYGPTETTvDSTYYEVTPPDAD-GGSVPIGRPIANTRVYVLD 803

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1803 AALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRI 1881
Cdd:COG1020  804 AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRI 883

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1882 EPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTP 1960
Cdd:COG1020  884 ELGEIEAALL----QHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAAlLRLALALLLPPYMVPAAVVLLLPLPLTG 959

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1961 SGKRDDAALRALPLEHGTniEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMA 2040
Cdd:COG1020  960 NGKLDRLALPAPAAAAAA--AAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLL 1037

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2041 ALIETPTVEGLAERLRERSAVRAfDPLVPIRAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPL 2120
Cdd:COG1020 1038 LLFLAAAAAAAAAAAAAAAAAAA-APLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLA 1116

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2121 AVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALDPQAVAQLIVLDSITVDRNHAGSASDEALLLFFYW 2200
Cdd:COG1020 1117 LLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLL 1196

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2201 ELVWFERSDKEVEPLPEGASLEQKLDHIVERAIEAGVLPAGTPRATVQRLYELFRASWQALIGYRPEVSDQDMTLLRADG 2280
Cdd:COG1020 1197 LLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLAL 1276

                       1290
                 ....*....|....*.
gi 15598523 2281 PLPLALKPMHDAAGTH 2296
Cdd:COG1020 1277 ALLLPALARARAARTA 1292
PRK12316 PRK12316
peptide synthase; Provisional
 3-1334 2.93e-180

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 618.51  E-value: 2.93e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     3 RFARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFE 82
Cdd:PRK12316 2599 RVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLR 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    83 ARHVDlrADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGELG 161
Cdd:PRK12316 2679 IVLED--CAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITqHHIVSDGWSMQVMVDELVQAYAGARR 2756

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   162 EPQAQMPTASLLAQ---LETDDYSGSEQYRGDRAYFAEALEGLEPAL---FTRRRPA-----GLRRTARHRLTLERTLLD 230
Cdd:PRK12316 2757 GEQPTLPPLPLQYAdyaAWQRAWMDSGEGARQLDYWRERLGGEQPVLelpLDRPRPAlqshrGARLDVALDVALSRELLA 2836

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   231 AIRDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRT 310
Cdd:PRK12316 2837 LARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALG 2916

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   311 LLRHQKMPLGDLLR--------GASPLFDTTLSYMRWPAAQA-IPNASVETVA--QTHAHDPDALAIWVSEfdghSDAQV 379
Cdd:PRK12316 2917 AQAHQDLPFEQLVEalqperslSHSPLFQVMYNHQSGERAAAqLPGLHIESFAwdGAATQFDLALDTWESA----EGLGA 2992

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   380 DFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVARTP 459
Cdd:PRK12316 2993 SLTYATDLFDAR-TVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTP 3071

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   460 QRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLL 539
Cdd:PRK12316 3072 DAVALAFGEQ-RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML 3150

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   540 EDCGARVVLVDERAaTLGESLGeTRVLHLERLPQSTGDL-PAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWM 618
Cdd:PRK12316 3151 EDSGAQLLLSQSHL-RLPLAQG-VQVLDLDRGDENYAEAnPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWM 3228

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   619 QRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDlldgD 698
Cdd:PRK12316 3229 QQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE----E 3304

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   699 PTARAAaSSLRLVFCSGEALAPLQVARFRRlfgdAVRLVNLYGPTEATVDVSDHECASDNPTRVPIGRPIDNLRLYVLDR 778
Cdd:PRK12316 3305 EDAHRC-TSLKRIVCGGEALPADLQQQVFA----GLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDG 3379

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   779 ALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEP 858
Cdd:PRK12316 3380 SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIEL 3459

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   859 DEVRDRLAALPGVRDAAVVardsAVRGTHLVGYYVAAAELD--PGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDR 936
Cdd:PRK12316 3460 GEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGdlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   937 RQLPAPP---EQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQRRGLGFELADLMRNPTV 1013
Cdd:PRK12316 3536 KALPRPDaalLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTI 3615

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1014 AGLAeRLVRplaersyqpFELVSEVDKPRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVYhdvfhYRFDLAWDEAAFRHAL 1093
Cdd:PRK12316 3616 QGLA-RVAR---------VGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLL-----LKPREALDAAALEAAL 3680

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1094 DRVVAAYPALRSSFDLSGASEPLQLVHTQARSEPLI-LDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAfvreDG 1172
Cdd:PRK12316 3681 QALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWrAELDDAEELERLGEEAQRSLDLADGPLLRALLATLAD----GS 3756

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1173 LDLVFSFHHAILDGWSVANLIVALVAAY----RGEP--LPG---PAPALACHVREELAALASPAAVGYWTGLLEGARmTR 1243
Cdd:PRK12316 3757 QRLLLVIHHLVVDGVSWRILLEDLQQAYqqllQGEAprLPAktsSFKAWAERLQEHARGEALKAELAYWQEQLQGVS-SE 3835

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1244 LDGFGAHEPQAAQGPASHREALPDGLLERL--KATAAQRgLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPEL---P 1318
Cdd:PRK12316 3836 LPCDHPQGALQNRHAASVQTRLDRELTRRLlqQAPAAYR-TQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLfadI 3914

                        1370
                  ....*....|....*.
gi 15598523  1319 DADRMVGLFLNTVPVR 1334
Cdd:PRK12316 3915 DLSRTVGWFTSLFPVR 3930
PRK12316 PRK12316
peptide synthase; Provisional
 8-1020 7.25e-177

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 607.72  E-value: 7.25e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     8 PLSPYQRDIWvaaaqFPELDQYTIFSYDRFTgEVDTQALE----RALLQAARDTEAFrLRLG----ETDGTPYQWLDTDA 79
Cdd:PRK12316 4104 PLSPMQQGML-----FHSLYEQEAGDYINQM-RVDVQGLDverfRAAWQAALDRHDV-LRSGfvwqGELGRPLQVVHKQV 4176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    80 EFEARHVDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLG 158
Cdd:PRK12316 4177 SLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTnHHILMDGWSNSQLLGEVLERYSG 4256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   159 ELGEPQAqMPTASLLAQLETDDYSGSEQYRGDRAYFAEALEGLEPALftrRRPAGLRRT--ARHRLTLERTLLDAIRD-- 234
Cdd:PRK12316 4257 RPPAQPG-GRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAI---ARADLRSANgyGEHVRELDATATARLREfa 4332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   235 RGESPFL--FLSAAVALYLARIHQNDDVVLGVPVLNR-ADR-AAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRT 310
Cdd:PRK12316 4333 RTQRVTLntLVQAAWLLLLQRYTGQDTVAFGATVAGRpAELpGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLA 4412

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   311 LLRHQKMPLGDLLR----GASPLFDTTLSYMRWPAAQAIPNAS--------VETVAQTHAhdPDALAIWVSEfdghsDAQ 378
Cdd:PRK12316 4413 LREHEHTPLYEIQRwagqGGEALFDSLLVFENYPVSEALQQGApgglrfgeVTNHEQTNY--PLTLAVGLGE-----TLS 4485

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   379 VDFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVART 458
Cdd:PRK12316 4486 LQFSYDRGHFDAA-TIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMT 4564

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   459 PQRTALLeADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:PRK12316 4565 PDAVAVV-FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYM 4643

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   539 LEDCGARVVLVDERAATLGESLGETRVLHLERLPQSTG---DLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRL 615
Cdd:PRK12316 4644 MEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGfpaHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHL 4723

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   616 NWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEkDPREMLRSIQRDAVTVIHFVPSMLTPFLDll 695
Cdd:PRK12316 4724 HATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAE-- 4800

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   696 dgDPTARAAASSLRLVFCSGEALAPlqvARFRRLFGDA--VRLVNLYGPTEATVDVSDHECASDNP---TRVPIGRPIDN 770
Cdd:PRK12316 4801 --HAERDGEPPSLRVYCFGGEAVAQ---ASYDLAWRALkpVYLFNGYGPTETTVTVLLWKARDGDAcgaAYMPIGTPLGN 4875

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   771 LRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA-GGRLYRTGDLARWLADGNLEYLGRADDQV 849
Cdd:PRK12316 4876 RSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGApGGRLYRTGDLARYRADGVIDYLGRVDHQV 4955

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   850 KIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVrGTHLVGYYVAA----AELDP------GQLRAGLSATLPDFMLPAF 919
Cdd:PRK12316 4956 KIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQdpalADADEaqaelrDELKAALRERLPEYMVPAH 5034

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   920 FVRIDSLPLSANGKLDRRQLPAPPE---QVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQ 996
Cdd:PRK12316 5035 LVFLARMPLTPNGKLDRKALPQPDAsllQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQ 5114

                        1050      1060
                  ....*....|....*....|....*
gi 15598523   997 RR-GLGFELADLMRNPTVAGLAERL 1020
Cdd:PRK12316 5115 LElGLELPLRELFQTPTLAAFVELA 5139
PRK12467 PRK12467
peptide synthase; Provisional
 71-1020 2.54e-172

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 593.29  E-value: 2.54e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    71 PYQWLDTDAEFEARHVDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFL 149
Cdd:PRK12467 2712 PLQVVYKQARLPFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTnHHILMDGWSGSQLL 2791

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   150 SRVRAGYLGE-LGEPQAQMptASLLAQLETDDYSGSEqyrgdrAYFAEALEGL-EPALFTRRRPA----GLRRTARHRLT 223
Cdd:PRK12467 2792 GEVLQRYFGQpPPAREGRY--RDYIAWLQAQDAEASE------AFWKEQLAALeEPTRLARALYPapaeAVAGHGAHYLH 2863

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   224 LE----RTLLDAIRDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRAD--RAAKQVVGHFANTLPLRIRTAPEQTV 297
Cdd:PRK12467 2864 LDatqtRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAqlRGAEQQLGLFINTLPVIASPRAEQTV 2943

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   298 DEFLAQLREATRTLLRHQKMPLGDLLR----GASPLFDTTLSYMRWPAAQAIPNASVETV------AQTHAHDPDALAIW 367
Cdd:PRK12467 2944 SDWLQQVQAQNLALREFEHTPLADIQRwagqGGEALFDSILVFENYPISEALKQGAPSGLrfgavsSREQTNYPLTLAVG 3023

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   368 VSEfdghsDAQVDFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATL 447
Cdd:PRK12467 3024 LGD-----TLELEFSYDRQHFDAA-AIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLV 3097

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   448 PTLFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPIN 527
Cdd:PRK12467 3098 HQLIEAQVARTPEAPALVFGDQ-QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLD 3176

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   528 PDHPLERVRLLLEDCGARVVLVDERAatlgeslgetrvlhLERLPQSTGDL----------------PAANVAPGDLAYV 591
Cdd:PRK12467 3177 PEYPRERLAYMIEDSGVKLLLTQAHL--------------LEQLPAPAGDTaltldrldlngysennPSTRVMGENLAYV 3242

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   592 IYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLsLLPPGAEKDPREMLR 671
Cdd:PRK12467 3243 IYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCL-VVRDNDLWDPEELWQ 3321

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   672 SIQRDAVTVIHFVPSMLTPFLDllDGDPtarAAASSLRLVFCSGEALAPLQVARFRRLFgDAVRLVNLYGPTEATVDVSD 751
Cdd:PRK12467 3322 AIHAHRISIACFPPAYLQQFAE--DAGG---ADCASLDIYVFGGEAVPPAAFEQVKRKL-KPRGLTNGYGPTEAVVTVTL 3395

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   752 HECASD---NPTRVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPF-VAGGRLYRT 827
Cdd:PRK12467 3396 WKCGGDavcEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsGSGGRLYRT 3475

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   828 GDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAvRGTHLVGYYVAAAELDP--GQLRA 905
Cdd:PRK12467 3476 GDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPADPQGDwrETLRD 3554

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   906 GLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPAPPEQV--AAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGG 983
Cdd:PRK12467 3555 HLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGsrEYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGG 3634

                         970       980       990      1000
                  ....*....|....*....|....*....|....*....|.
gi 15598523   984 DSILML----RIRAAAqrrGLGFELADLMRNPTVAGLAERL 1020
Cdd:PRK12467 3635 DSLLALqvlsRIRQSL---GLKLSLRDLMSAPTIAELAGYS 3672
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 450-939 1.02e-163

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: 513.67  E-value: 1.02e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  450 LFAEQVARTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD 529
Cdd:cd12117    2 LFEEQAARTPDAVAV-VYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  530 HPLERVRLLLEDCGARVVLVDERAATLGeSLGETRVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHR 609
Cdd:cd12117   81 LPAERLAFMLADAGAKVLLTDRSLAGRA-GGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  610 SVVnRL----NWMQrrypIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVP 685
Cdd:cd12117  160 GVV-RLvkntNYVT----LGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  686 SMltpFLDLLDGDPtarAAASSLRLVFCSGEALAPLQVARFRRLFGDaVRLVNLYGPTEATVDVSDHECA--SDNPTRVP 763
Cdd:cd12117  235 AL---FNQLADEDP---ECFAGLRELLTGGEVVSPPHVRRVLAACPG-LRLVNGYGPTENTTFTTSHVVTelDEVAGSIP 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  764 IGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLG 843
Cdd:cd12117  308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  844 RADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRI 923
Cdd:cd12117  388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVL 467

                        490
                 ....*....|....*.
gi 15598523  924 DSLPLSANGKLDRRQL 939
Cdd:cd12117  468 DELPLTANGKVDRRAL 483
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 450-942 4.80e-162

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: 509.18  E-value: 4.80e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  450 LFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD 529
Cdd:cd17655    2 LFEEQAEKTPDHTAVVFEDQ-TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  530 HPLERVRLLLEDCGARVVLVDERAATLGESLGEtrVLHLERlpQSTGDLPAANVAP----GDLAYVIYTSGSTGMPKGVM 605
Cdd:cd17655   81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGL--IDLLDE--DTIYHEESENLEPvsksDDLAYVIYTSGSTGKPKGVM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  606 VEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVP 685
Cdd:cd17655  157 IEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  686 SmltpFLDLLDgdPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAVRLVNLYGPTEATVDVSDHEC--ASDNPTRVP 763
Cdd:cd17655  237 A----HLKLLD--AADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYepETDQQVSVP 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  764 IGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLG 843
Cdd:cd17655  311 IGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLG 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  844 RADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRI 923
Cdd:cd17655  391 RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKL 470

                        490
                 ....*....|....*....
gi 15598523  924 DSLPLSANGKLDRRQLPAP 942
Cdd:cd17655  471 DEIPLTPNGKVDRKALPEP 489
PRK12467 PRK12467
peptide synthase; Provisional
 1043-2258 6.02e-160

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 554.77  E-value: 6.02e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1043 LEGLEDAFPTSRLSLGLLFHSRQRPDSSVYhdVFHYRFDL-AWDEAAFRHALDRVVAAYPALRSSFDLSGA-SEPLQLVH 1120
Cdd:PRK12467 2640 VGDIEDIYPLSPMQQGMLFHTLYEGGAGDY--INQMRVDVeGLDVERFRTAWQAVIDRHEILRSGFLWDGElEEPLQVVY 2717

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1121 TQARSEPLILDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLfLFAAFVR--EDGLDLVFSFHHAILDGWSVANLIVALVA 1198
Cdd:PRK12467 2718 KQARLPFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPL-LRLTLVRtgEDRHHLIYTNHHILMDGWSGSQLLGEVLQ 2796

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1199 AYRGEPLPGPApalaCHVREELAAL-ASPAAV--GYWTG-LLEGARMTRL-DGFGAHEPQAAQGPASHREALPDGLLERL 1273
Cdd:PRK12467 2797 RYFGQPPPARE----GRYRDYIAWLqAQDAEAseAFWKEqLAALEEPTRLaRALYPAPAEAVAGHGAHYLHLDATQTRQL 2872

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1274 KATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPV----RSEIAGCSWIEVADA 1348
Cdd:PRK12467 2873 IEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPaQLRGAEQQLGLFINTLPViaspRAEQTVSDWLQQVQA 2952

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1349 LFRQERDghaHRRYPLSAIQQIVGDELSSAFNYV----NLHVLEPLWQ-----LRDFRV--WEETNFALLVNVIAtpSDG 1417
Cdd:PRK12467 2953 QNLALRE---FEHTPLADIQRWAGQGGEALFDSIlvfeNYPISEALKQgapsgLRFGAVssREQTNYPLTLAVGL--GDT 3027

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1418 MYLRIDSDGRGISRSQAALIGATFVELLWRLADHPDE---------AADFAFLAPRRDAASQPEPL-VDVVSLFERQVEA 1487
Cdd:PRK12467 3028 LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAArlgelptlaAHERRQVLHAWNATAAAYPSeRLVHQLIEAQVAR 3107

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1488 LPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI 1567
Cdd:PRK12467 3108 TPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYM 3187

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1568 LETAQPFRVVAHP---EHAHVAAAERVLPVEELVADIEPETFAAPQLD--ELAMLLFTSGSTGRPKGVELSHRMWANYTQ 1642
Cdd:PRK12467 3188 IEDSGVKLLLTQAhllEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMgeNLAYVIYTSGSTGKPKGVGVRHGALANHLC 3267

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1643 WQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERmDPSALLHVLERRQVQRVLLPFVALQRLAEASn 1722
Cdd:PRK12467 3268 WIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDA- 3345

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1723 alGVRPGA-LRVVVSSGEQLRITEDVRAFcAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRPLDGVEVQV 1800
Cdd:PRK12467 3346 --GGADCAsLDIYVFGGEAVPPAAFEQVK-RKLKPRGLTNGYGPTEAVvTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYV 3422

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1801 LDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWR-PGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGF 1879
Cdd:PRK12467 3423 LDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGF 3502

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1880 RIEPAEVElAIMRQaerQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALT 1959
Cdd:PRK12467 3503 RIELGEIE-ARLLQ---HPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLG 3578

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1960 PSGKRDDaalRALPLEHGTNI-EYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLP 2038
Cdd:PRK12467 3579 PNGKVDR---KALPDPDAKGSrEYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLS 3655

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  2039 MAALIETPTVEGLAERLRERSAvrAFDPLVPI-RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGS 2117
Cdd:PRK12467 3656 LRDLMSAPTIAELAGYSPLGDV--PVNLLLDLnRLETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLTCRHLLDDG 3733

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  2118 TPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRAlDPQAVAQLIVLDSITVDRNHAGSASDEALLLF 2197
Cdd:PRK12467 3734 WQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLER-EGESEAFLGLFDNTLPLPDEFVPQAEFLELLR 3812

                        1210      1220      1230      1240      1250      1260
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598523  2198 FYWELVwfERSDKEVEPLPEGA-SLEQKLDHIVERAIEAGVLPAGTPRATVQRLYELFRASW 2258
Cdd:PRK12467 3813 QLGELI--GRANRLLRGLEEGGvGPDVLVGIAIQRCFDIAPLELYTPLLDAGELAHIFDVAM 3872
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 473-876 3.26e-155

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: 486.77  E-value: 3.26e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    473 SYAELDAKVQAVADALRAA-GVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDE 551
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    552 RAATLGESLGETRVLHLERL-----PQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGE 626
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLElaaldDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    627 RDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRD-AVTVIHFVPSMLTPFLDLLDGDPtaraaa 705
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEhPVTVLNLTPSLLALLAAALPPAL------ 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    706 SSLRLVFCSGEALAPLQVARFRRLFGDAvRLVNLYGPTEATVDVSDHECASDNPTR---VPIGRPIDNLRLYVLDRALRP 782
Cdd:TIGR01733  235 ASLRLVILGGEALTPALVDRWRARGPGA-RLINLYGPTETTVWSTATLVDPDDAPRespVPIGRPLANTRLYVLDDDLRP 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    783 QPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFV--AGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDE 860
Cdd:TIGR01733  314 VPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393

                          410
                   ....*....|....*.
gi 15598523    861 VRDRLAALPGVRDAAV 876
Cdd:TIGR01733  394 IEAALLRHPGVREAVV 409
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 451-940 3.57e-155

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: 489.93  E-value: 3.57e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  451 FAEQVARTPQRTALLeADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDH 530
Cdd:cd17651    1 FERQAARTPDAPALV-AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  531 PLERVRLLLEDCGARVVLVDERAAtlGESLGETRVLHLERLPQSTGDLPAANVA---PGDLAYVIYTSGSTGMPKGVMVE 607
Cdd:cd17651   80 PAERLAFMLADAGPVLVLTHPALA--GELAVELVAVTLLDQPGAAAGADAEPDPaldADDLAYVIYTSGSTGRPKGVVMP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  608 HRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIhFVPsm 687
Cdd:cd17651  158 HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRV-FLP-- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  688 lTPFLDLLDGDPTARAAAS-SLRLVFCSGEALAPlqVARFRRLFGD--AVRLVNLYGPTEATVdVSDHECASDN---PTR 761
Cdd:cd17651  235 -TVALRALAEHGRPLGVRLaALRYLLTGGEQLVL--TEDLREFCAGlpGLRLHNHYGPTETHV-VTALSLPGDPaawPAP 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  762 VPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEY 841
Cdd:cd17651  311 PPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEF 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  842 LGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAE--LDPGQLRAGLSATLPDFMLPAF 919
Cdd:cd17651  391 LGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEapVDAAELRAALATHLPEYMVPSA 470

                        490       500
                 ....*....|....*....|.
gi 15598523  920 FVRIDSLPLSANGKLDRRQLP 940
Cdd:cd17651  471 FVLLDALPLTPNGKLDRRALP 491
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 6-415 1.77e-153

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: 482.25  E-value: 1.77e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    6 RLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEARH 85
Cdd:cd19533    1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   86 VDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLH-SDQALYVYVRTHHIVSDAWGLQLFLSRVRAGYLGELGEPQ 164
Cdd:cd19533   81 IDLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTlGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  165 AQMPTA--SLLAQLETDDYSGSEQYRGDRAYFAEALEGL-EPALFTRR----RPAGLRRTARHRLTLERTLLDAIRDRGE 237
Cdd:cd19533  161 APPAPFgsFLDLVEEEQAYRQSERFERDRAFWTEQFEDLpEPVSLARRapgrSLAFLRRTAELPPELTRTLLEAAEAHGA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  238 SPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTLLRHQKM 317
Cdd:cd19533  241 SWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRY 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  318 PLGDLLRGAS------PLFDTTLSYMRWPAAQAIPNasVETVAQTHAHDP-DALAIWVSEFDGHSDAQVDFEYACDVFDa 390
Cdd:cd19533  321 RYEDLRRDLGltgelhPLFGPTVNYMPFDYGLDFGG--VVGLTHNLSSGPtNDLSIFVYDRDDESGLRIDFDANPALYS- 397

                        410       420
                 ....*....|....*....|....*
gi 15598523  391 dfpMDAAARHIETFLRALVEGGERR 415
Cdd:cd19533  398 ---GEDLARHQERLLRLLEEAAADP 419
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1489-1969 1.07e-150

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: 475.48  E-value: 1.07e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:cd05930    1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1569 ETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVA 1648
Cdd:cd05930   81 EDSGAKLVLTDPDD-------------------------------LAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1649 SGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEAsnALGVRP 1728
Cdd:cd05930  130 PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE--LELAAL 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1729 GALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYpDLPPIGRPLDGVEVQVLDAALRP 1807
Cdd:cd05930  208 PSLRLVLVGGEALP-PDLVRRWRELLPGARLVNLYGPTEATvDATYYRVPPDDEED-GRVPIGRPIPNTRVYVLDENLRP 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1808 VPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 1887
Cdd:cd05930  286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1888 LAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFL-LGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDD 1966
Cdd:cd05930  366 AALL----AHPGVREAAVVAREDGDGEKRLVAYVvPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441


                 ...
gi 15598523 1967 AAL 1969
Cdd:cd05930  442 KAL 444
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1046-2343 3.20e-149

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 500.73  E-value: 3.20e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1046 LEDAFPTSRLSLGLLFHSRQRPDSSVYhDVFHY-RFDLAWDEAAFRHALDRVVAAYPALRSSFdLSGASEPLQLVHTQAR 1124
Cdd:PRK10252    4 MSQHLPLVAAQPGIWMAEKLSPLPSAW-SVAHYvELTGELDAPLLARAVVAGLAEADTLRMRF-TEDNGEVWQWVDPALT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1125 -SEPLILDLRGNPeagtvlDEHIRQRRFHRYSLQQP-------GLFLFAAFVREDGLDLVF-SFHHAILDGWS---VANL 1192
Cdd:PRK10252   82 fPLPEIIDLRTQP------DPHAAAQALMQADLQQDlrvdsgkPLVFHQLIQLGDNRWYWYqRYHHLLVDGFSfpaITRR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1193 IVALVAAY-RGEPLPG-PAPALACHVREELAALASPA---AVGYW----TGLLEGARMTrldgfGAHEPQAAQGPASHRE 1263
Cdd:PRK10252  156 IAAIYCAWlRGEPTPAsPFTPFADVVEEYQRYRASEAwqrDAAFWaeqrRQLPPPASLS-----PAPLPGRSASADILRL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1264 AL--PDGLLERLKATAAQRGLPlkSLLLAAHCLTLHLFSRSDSVVTGAISNGRPELPdADRMVGLFLNTVPVRSEIAGCS 1341
Cdd:PRK10252  231 KLefTDGAFRQLAAQASGVQRP--DLALALVALWLGRLCGRMDYAAGFIFMRRLGSA-ALTATGPVLNVLPLRVHIAAQE 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1342 WI-EVADALFRQERDGHAHRRYPLSAIQQ---IVGDELSSAFNYVNLHVLEPLWQLRDFRVWEETNFALLVNVIA----- 1412
Cdd:PRK10252  308 TLpELATRLAAQLKKMRRHQRYDAEQIVRdsgRAAGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLElalfp 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1413 TPSDGMYLRIDSDGRGISRSQAALIGATFVELLWRLADHPD---------EAADFAFLApRRDAASQPEPLVDVVSLFER 1483
Cdd:PRK10252  388 DEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPAllcgdvdilLPGEYAQLA-QVNATAVEIPETTLSALVAQ 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1484 QVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQR 1563
Cdd:PRK10252  467 QAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1564 LALILETAQPFRVVAHPEHAHVAAAERVL-----PVEELVADIEPETFAAPQldELAMLLFTSGSTGRPKGVELSHRMWA 1638
Cdd:PRK10252  547 LKMMLEDARPSLLITTADQLPRFADVPDLtslcyNAPLAPQGAAPLQLSQPH--HTAYIIFTSGSTGRPKGVMVGQTAIV 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1639 NYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQ------VQRVLLPFV 1712
Cdd:PRK10252  625 NRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGvttthfVPSMLAAFV 704

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1713 AlqrlAEASNALGVRPGALRVVVSSGEQLRiTEDVRAFCAAMpGLLLENQYGPTETH-QVTYHSLSG-DPAHYPDLP-PI 1789
Cdd:PRK10252  705 A----SLTPEGARQSCASLRQVFCSGEALP-ADLCREWQQLT-GAPLHNLYGPTEAAvDVSWYPAFGeELAAVRGSSvPI 778

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1790 GRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGR 1869
Cdd:PRK10252  779 GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGR 858

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1870 ADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR-----ERQGNDAF-LAAFLLGEP-EAVDLAELKQALRSELP 1942
Cdd:PRK10252  859 SDDQLKIRGQRIELGEIDRAMQ----ALPDVEQAVTHACvinqaAATGGDARqLVGYLVSQSgLPLDTSALQAQLRERLP 934

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1943 EHMVPAHFAWVDGFALTPSGKRDDaalRALPL-EHGTNIEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLS 2021
Cdd:PRK10252  935 PHMVPVVLLQLDQLPLSANGKLDR---KALPLpELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLL 1011

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  2022 AMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRA---FDPLVPIRAgGSRPPLFLVHPLGGHVLCYLPLVRA 2098
Cdd:PRK10252 1012 AMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRrlgFGTILPLRE-GDGPTLFCFHPASGFAWQFSVLSRY 1090

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  2099 LPPDQPVYALQAAGTGqGSTPL-AVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALDpQAVAQLIVLD 2177
Cdd:PRK10252 1091 LDPQWSIYGIQSPRPD-GPMQTaTSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARG-EEVAFLGLLD 1168

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  2178 SITVDRNHagsasdealllffywelvWFERSDKEVEP--LPEGASleqkldhivERAIEAGVLPAGTPRATVQRLYELFR 2255
Cdd:PRK10252 1169 TWPPETQN------------------WREKEANGLDPevLAEIDR---------EREAFLAAQQGSLSTELFTTIEGNYA 1221

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  2256 ASWQALIGYRPEVSDQDMTLLRADGPLPLALkpmhdaagthygDPKNGWQHWTSGrLDVIDVPGDHLVLMKEPYVETVAA 2335
Cdd:PRK10252 1222 DAVRLLTTAHSVPFDGKATLFVAERTLQEGM------------SPEQAWSPWIAE-LDVYRQDCAHVDIISPEAFEKIGP 1288


                  ....*...
gi 15598523  2336 EIAALLEP 2343
Cdd:PRK10252 1289 ILRATLNE 1296
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 459-939 4.71e-149

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: 471.02  E-value: 4.71e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:cd17643    1 PEAVAV-VDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  539 LEDCGARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWM 618
Cdd:cd17643   80 LADSGPSLLLTD----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  619 QRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGD 698
Cdd:cd17643  126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRD 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  699 PTARAAassLRLVFCSGEALAPLQVARFRRLFGD-AVRLVNLYGPTEATVDVSDHEC-ASDNP--TRVPIGRPIDNLRLY 774
Cdd:cd17643  206 GRDPLA---LRYVIFGGEALEAAMLRPWAGRFGLdRPQLVNMYGITETTVHVTFRPLdAADLPaaAASPIGRPLPGLRVY 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  775 VLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGG-RLYRTGDLARWLADGNLEYLGRADDQVKIRG 853
Cdd:cd17643  283 VLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGsRMYRTGDLARRLPDGELEYLGRADEQVKIRG 362

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  854 NRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVA--AAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSAN 931
Cdd:cd17643  363 FRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAddGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVN 442


                 ....*...
gi 15598523  932 GKLDRRQL 939
Cdd:cd17643  443 GKLDRAAL 450
PRK05691 PRK05691
peptide synthase; Validated
 3-1334 9.77e-148

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 516.26  E-value: 9.77e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     3 RFARLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFE 82
Cdd:PRK05691 1725 RSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLR 1804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    83 ARHVDLRA-DRDPEAAVRSWLRDAFRHAyPLD---GRSLVDLALLHSDQALYVYVRTHHIVSDAWGLQLF---LSRVRAG 155
Cdd:PRK05691 1805 MDWQDFSAlPADARQQRLQQLADSEAHQ-PFDlerGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFareLGALYEA 1883

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   156 YLGELGEPQAQMPTASLlaqletdDYS--------GSEQYRgDRAYFAEALEGLEPAL---FTRRRPA-GLRRTARHRLT 223
Cdd:PRK05691 1884 FLDDRESPLEPLPVQYL-------DYSvwqrqwleSGERQR-QLDYWKAQLGNEHPLLelpADRPRPPvQSHRGELYRFD 1955

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   224 LERTLLDAIR----DRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDE 299
Cdd:PRK05691 1956 LSPELAARVRafnaQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSE 2035

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   300 FLAQLREATRTLLRHQKMPLGDLL------RGAS--PLFDTTLSYMRWPAAQA--IPNASVETVAQTHAHDPDALAIWVS 369
Cdd:PRK05691 2036 LLEQVRQTVIEGQSHQDLPFDHLVealqppRSAAynPLFQVMCNVQRWEFQQSrqLAGMTVEYLVNDARATKFDLNLEVT 2115

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   370 EFDGHSDAQvdFEYACDVFDAdfPMDAA-ARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLP 448
Cdd:PRK05691 2116 DLDGRLGCC--LTYSRDLFDE--PRIARmAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLH 2191

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   449 TLFAEQVARTPQRTALLEAdGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINP 528
Cdd:PRK05691 2192 GLFAAQAARTPQAPALTFA-GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   529 DHPLERVRLLLEDCGARVVLVDERA-ATLGESLGETRVLHLERLPQSTGDLPAANVA----PGDLAYVIYTSGSTGMPKG 603
Cdd:PRK05691 2271 EYPLERLHYMIEDSGIGLLLSDRALfEALGELPAGVARWCLEDDAAALAAYSDAPLPflslPQHQAYLIYTSGSTGKPKG 2350

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   604 VMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGaEKDPREMLRSIQRDAVTVIHF 683
Cdd:PRK05691 2351 VVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQG-QWGAEEICQLIREQQVSILGF 2429

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   684 VPSMLTPFLDLLDGdptaRAAASSLRLVFCSGEALAPLQVARFRRLFGDAVrLVNLYGPTEATV--------DVSDHECA 755
Cdd:PRK05691 2430 TPSYGSQLAQWLAG----QGEQLPVRMCITGGEALTGEHLQRIRQAFAPQL-FFNAYGPTETVVmplaclapEQLEEGAA 2504

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   756 SdnptrVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA-GGRLYRTGDLARWL 834
Cdd:PRK05691 2505 S-----VPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLR 2579

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   835 ADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAvRGTHLVGYYVAA-AELDPGQ-------LRAG 906
Cdd:PRK05691 2580 ADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP-SGKQLAGYLVSAvAGQDDEAqaalreaLKAH 2658

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   907 LSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPAP-PEQV--AAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGG 983
Cdd:PRK05691 2659 LKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPdPELNrqAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGG 2738

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   984 DSILMLRIRAAAQRRGLGFELADLMRNPTVAGLAErlvrpLAERSyqpfELVSEvDKPRLEGLEDAFPTSRLSLGLLFHS 1063
Cdd:PRK05691 2739 DSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAA-----VATHS----EAAQA-EQGPLQGASGLTPIQHWFFDSPVPQ 2808

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1064 RQRPDSSVYHDVFHyrfdlAWDEAAFRHALDRVVAAYPALRSSFdlSGASEPLQLVHTQARSEPLILDLRGNPEAGTVLD 1143
Cdd:PRK05691 2809 PQHWNQALLLEPRQ-----ALDPALLEQALQALVEHHDALRLRF--SQADGRWQAEYRAVTAQELLWQVTVADFAECAAL 2881

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1144 EHIRQRRFhrySLQQpGLFLFAAFVR--EDGLDLVFSFHHAILDGWSVANLIVALVAAYR----GEPLPGPAPALAchVR 1217
Cdd:PRK05691 2882 FADAQRSL---DLQQ-GPLLRALLVDgpQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRqlsaGAEPALPAKTSA--FR 2955

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1218 EELAALASPAA-------VGYWTGLLEGARMTrldgFGAHEPQAAQgpashREALPDGLLERLKATAAQRGLP------- 1283
Cdd:PRK05691 2956 DWAARLQAYAGseslreeLGWWQAQLGGPRAE----LPCDRPQGGN-----LNRHAQTVSVRLDAERTRQLLQqapaayr 3026

                        1370      1380      1390      1400      1410
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  1284 --LKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPEL---PDADRMVGLFLNTVPVR 1334
Cdd:PRK05691 3027 tqVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALfddIDLTRSVGWFTSAYPLR 3082
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 459-939 1.08e-146

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: 465.23  E-value: 1.08e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:cd12116    1 PDATAV-RDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  539 LEDCGARVVLVDERAATLGeSLGETRVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWM 618
Cdd:cd12116   80 LEDAEPALVLTDDALPDRL-PAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  619 QRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPfldLLDGD 698
Cdd:cd12116  159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRM---LLDAG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  699 PTARAaasSLRLVfCSGEALAPlQVArfRRLFGDAVRLVNLYGPTEATVDVSDHE-CASDNPtrVPIGRPIDNLRLYVLD 777
Cdd:cd12116  236 WQGRA---GLTAL-CGGEALPP-DLA--ARLLSRVGSLWNLYGPTETTIWSTAARvTAAAGP--IPIGRPLANTQVYVLD 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  778 RALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFV-AGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRV 856
Cdd:cd12116  307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  857 EPDEVRDRLAALPGVRDAAVVARDsAVRGTHLVGYYVAAAE--LDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKL 934
Cdd:cd12116  387 ELGEIEAALAAHPGVAQAAVVVRE-DGGDRRLVAYVVLKAGaaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465


                 ....*
gi 15598523  935 DRRQL 939
Cdd:cd12116  466 DRKAL 470
PRK05691 PRK05691
peptide synthase; Validated
 440-2083 1.15e-141

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 497.00  E-value: 1.15e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   440 AFPEQATLPTLFAEQVARTPQRTAL--LEADGG---TLSYAELDAKVQAVADALRAAGVRTDeRVALLVARGPHLLPAIL 514
Cdd:PRK05691    4 AFELPLTLVQALQRRAAQTPDRLALrfLADDPGegvVLSYRDLDLRARTIAAALQARASFGD-RAVLLFPSGPDYVAAFF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   515 GVQRAGGAYVPINP-----DHPLERVRLLLEDCGARVVLVDeraATLGESLGETRVLHLERLPQ--STGDLPAA------ 581
Cdd:PRK05691   83 GCLYAGVIAVPAYPpesarRHHQERLLSIIADAEPRLLLTV---ADLRDSLLQMEELAAANAPEllCVDTLDPAlaeawq 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   582 --NVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRlNWMQRR---YPIGERDVLLQKTPVTFDVS-VWELFWWSFTGARL 655
Cdd:PRK05691  160 epALQPDDIAFLQYTSGSTALPKGVQVSHGNLVAN-EQLIRHgfgIDLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPC 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   656 SLLPPGA-EKDPREMLRSIQRDAVTVihfvpSMLTPFLDLLDGDPTARAAASSL-----RLVFCSGEALAPLQVARFRRL 729
Cdd:PRK05691  239 VLMSPAYfLERPLRWLEAISEYGGTI-----SGGPDFAYRLCSERVSESALERLdlsrwRVAYSGSEPIRQDSLERFAEK 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   730 FG----DAVRLVNLYGPTEATVDVS--------------------DHECASDNPTRVPIGRPIDNLRLYVLD-RALRPQP 784
Cdd:PRK05691  314 FAacgfDPDSFFASYGLAEATLFVSggrrgqgipaleldaealarNRAEPGTGSVLMSCGRSQPGHAVLIVDpQSLEVLG 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   785 LGAVGELYIGGVGVARGYLNRPELNAERFLVdpfVAGGRLYRTGDLArWLADGNLEYLGRADDQVKIRGNRVEPDEVRDR 864
Cdd:PRK05691  394 DNRVGEIWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKT 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   865 L-AALPGVRDAAVVARDSAVRGTHLVGyyvAAAELDPGQLRAGLSATLPDFM----------LPAFFVRID--SLPLSAN 931
Cdd:PRK05691  470 VeREVEVVRKGRVAAFAVNHQGEEGIG---IAAEISRSVQKILPPQALIKSIrqavaeacqeAPSVVLLLNpgALPKTSS 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   932 GKLDRR---------------QLPA--PPEQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAA 994
Cdd:PRK05691  547 GKLQRSacrlrladgsldsyaLFPAlqAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVAR 626

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   995 -AQRRGLGFELADLMRNPTVAGLAERLVRPLAERSyqpfelVSEVDKPRLEGlEDAFPTSRLSLGLLFHSRQRPDSSVYH 1073
Cdd:PRK05691  627 lRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGG------AAQAAIARLPR-GQALPQSLAQNRLWLLWQLDPQSAAYN 699

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1074 --DVFHYRFDLawDEAAFRHALDRVVAAYPALRSSFDlSGASEPLQLVHTQARSEPLILDLRGNPE------AGTVLDEH 1145
Cdd:PRK05691  700 ipGGLHLRGEL--DEAALRASFQRLVERHESLRTRFY-ERDGVALQRIDAQGEFALQRIDLSDLPEaerearAAQIREEE 776

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1146 IRQRrfhrYSLQQpGLFLFAAFVREDGLD--LVFSFHHAILDGWSVANLIVAL----VAAYRGEPLPGPAPAL-----AC 1214
Cdd:PRK05691  777 ARQP----FDLEK-GPLLRVTLVRLDDEEhqLLVTLHHIVADGWSLNILLDEFsrlyAAACQGQTAELAPLPLgyadyGA 851

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1215 HVREELAALASPAAVGYWTGLLEGARMTrLDgFGAHEPQAAQ---GPASHREALPDGLLERLKATAAQRGLPLKSLLLAA 1291
Cdd:PRK05691  852 WQRQWLAQGEAARQLAYWKAQLGDEQPV-LE-LATDHPRSARqahSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAA 929

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1292 HCLTLHLFSRSDSVVTGAISNGRPELpDADRMVGLFLNTVPVRSEIAG-CSWIEVADALFRQERDGHAHRRYPLSAIQQI 1370
Cdd:PRK05691  930 FQALLHRYSGQGDIRIGVPNANRPRL-ETQGLVGFFINTQVLRAQLDGrLPFTALLAQVRQATLGAQAHQDLPFEQLVEA 1008

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1371 VGDE----------------LSSAFNYVNLHVLEPLWQLRdfrvweETNFALLVNVIATPSDGMYLRIDSDGRGISRSQA 1434
Cdd:PRK05691 1009 LPQAreqglfqvmfnhqqrdLSALRRLPGLLAEELPWHSR------EAKFDLQLHSEEDRNGRLTLSFDYAAELFDAATI 1082

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1435 ALIGATFVELLWRLADHPDEA-ADFAFL-APRR------DAASQPEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDL 1506
Cdd:PRK05691 1083 ERLAEHFLALLEQVCEDPQRAlGDVQLLdAAERaqlaqwGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAEL 1162

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1507 DHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAH---PEHA 1583
Cdd:PRK05691 1163 HAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQshlLERL 1242

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1584 HVAAAERVLPVEELVADIEPETfaAPQL----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQF 1659
Cdd:PRK05691 1243 PQAEGVSAIALDSLHLDSWPSQ--APGLhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQK 1320

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1660 APLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVqrVLLPFVA--LQRLAEASNALGVRpgALRVVVSS 1737
Cdd:PRK05691 1321 APISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGV--TTLHFVPplLQLFIDEPLAAACT--SLRRLFSG 1396

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1738 GEQLRiTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAhypDLPPIGRPLDGVEVQVLDAALRPVPVGVTGEL 1816
Cdd:PRK05691 1397 GEALP-AELRNRVLQRLPQVQLHNRYGPTETAiNVTHWQCQAEDG---ERSPIGRPLGNVLCRVLDAELNLLPPGVAGEL 1472

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1817 YFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqae 1895
Cdd:PRK05691 1473 CIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLL---- 1548

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1896 RQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDaalRALPLE 1975
Cdd:PRK05691 1549 AQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR---RALPEP 1625

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1976 HGTNIEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERL 2055
Cdd:PRK05691 1626 VWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQV 1705

                        1770      1780
                  ....*....|....*....|....*...
gi 15598523  2056 RERSAVRAFDPLVPIRAGGSRPPLFLVH 2083
Cdd:PRK05691 1706 ARIQAAGERNSQGAIARVDRSQPVPLSY 1733
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 459-940 9.42e-140

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: 444.50  E-value: 9.42e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALLeADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:cd17649    1 PDAVALV-FGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  539 LEDCGARVVLVDEraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWM 618
Cdd:cd17649   80 LEDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  619 QRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGD 698
Cdd:cd17649  127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRT 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  699 PTARAAasSLRLVFCSGEALAPlqvARFRRLFGDAVRLVNLYGPTEATVDVSDHECASDN---PTRVPIGRPIDNLRLYV 775
Cdd:cd17649  207 GDGRPP--SLRLYIFGGEALSP---ELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAaraGASMPIGRPLGGRSAYI 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  776 LDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA-GGRLYRTGDLARWLADGNLEYLGRADDQVKIRGN 854
Cdd:cd17649  282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  855 RVEPDEVRDRLAALPGVRDAAVVARDSAVrGTHLVGYYVAAA----ELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSA 930
Cdd:cd17649  362 RIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAaaaqPELRAQLRTALRASLPDYMVPAHLVFLARLPLTP 440

                        490
                 ....*....|
gi 15598523  931 NGKLDRRQLP 940
Cdd:cd17649  441 NGKLDRKALP 450
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 447-939 1.06e-138

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: 441.37  E-value: 1.06e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  447 LPTLFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPI 526
Cdd:cd12115    1 LHDLVEAQAARTPDAIALVCGDE-SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  527 NPDHPLERVRLLLEDCGARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMV 606
Cdd:cd12115   80 DPAYPPERLRFILEDAQARLVLTD----------------------------------PDDLAYVIYTSGSTGRPKGVAI 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  607 EHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLppgaeKDPREMLRSIQRDAVTVIHFVPS 686
Cdd:cd12115  126 EHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTVPS 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  687 MLTPFLDLldgdptaRAAASSLRLVFCSGEALAPLQVARFRRLfGDAVRLVNLYGPTEATVDVSDHECASDNPTRVPIGR 766
Cdd:cd12115  201 AAAELLRH-------DALPASVRVVNLAGEPLPRDLVQRLYAR-LQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGR 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  767 PIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRAD 846
Cdd:cd12115  273 PLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRAD 352

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  847 DQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVA--AAELDPGQLRAGLSATLPDFMLPAFFVRID 924
Cdd:cd12115  353 NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAepGAAGLVEDLRRHLGTRLPAYMVPSRFVRLD 432

                        490
                 ....*....|....*
gi 15598523  925 SLPLSANGKLDRRQL 939
Cdd:cd12115  433 ALPLTPNGKIDRSAL 447
PRK12316 PRK12316
peptide synthase; Provisional
 1038-2065 5.19e-136

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 479.07  E-value: 5.19e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1038 VDKPRLEGL-------EDAFPTSRLSLGLLFHSRQRPDSSVYhdVFHYRFDL-AWDEAAFRHALDRVVAAYPALRSSFDL 1109
Cdd:PRK12316 4084 LDQARLDALplplgeiEDIYPLSPMQQGMLFHSLYEQEAGDY--INQMRVDVqGLDVERFRAAWQAALDRHDVLRSGFVW 4161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1110 SGASE-PLQLVHTQARSEPLILDLRGNPEAGTVLDEHIRQRRFHRYSLQQ-PGLFLFAAFVREDGLDLVFSFHHAILDGW 1187
Cdd:PRK12316 4162 QGELGrPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRaPLLRLVLVRTAEGRHHLIYTNHHILMDGW 4241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1188 SVANLIVALVAAYRGEPLPGPAPalacHVREELAALA---SPAAVGYW-TGLLEGARMTRL-DGFGAHEPQAAQGPASHR 1262
Cdd:PRK12316 4242 SNSQLLGEVLERYSGRPPAQPGG----RYRDYIAWLQrqdAAASEAFWrEQLAALDEPTRLaQAIARADLRSANGYGEHV 4317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1263 EALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPVRSEIAG-C 1340
Cdd:PRK12316 4318 RELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPaELPGIEGQIGLFINTLPVIATPRAqQ 4397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1341 SWIEVADALFRQERDGHAHRRYPLSAIQQIVGDELSSAF----NYVNLHVLEPLWQ-----LRDFRV--WEETNFALLVN 1409
Cdd:PRK12316 4398 SVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFdsllVFENYPVSEALQQgapggLRFGEVtnHEQTNYPLTLA 4477

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1410 ViaTPSDGMYLRIDSDGRGISRSQAALIGATFVELLWRLADHP------------DEAADFAFLAPRRDAASQPEPLVDv 1477
Cdd:PRK12316 4478 V--GLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPqrrlgelqllekAEQQRIVALWNRTDAGYPATRCVH- 4554

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1478 vSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDV 1557
Cdd:PRK12316 4555 -QLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDP 4633

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1558 SYPAQRLALILETAqpfRVVAHPEHAHVAAAervLPVEELVA--DIEPE------TFAAPQL----DELAMLLFTSGSTG 1625
Cdd:PRK12316 4634 EYPRERLAYMMEDS---GAALLLTQSHLLQR---LPIPDGLAslALDRDedwegfPAHDPAVrlhpDNLAYVIYTSGSTG 4707

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1626 RPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQ 1705
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV-VIRDDSLWDPERLYAEIHEHRVT 4786

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1706 RVLLPFVALQRLAEASNALGvRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLeNQYGPTETHQVTYH--SLSGDPAHy 1783
Cdd:PRK12316 4787 VLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLF-NGYGPTETTVTVLLwkARDGDACG- 4863

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1784 PDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNG 1862
Cdd:PRK12316 4864 AAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADG 4943

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1863 EIVWLGRADTQVKVRGFRIEPAEVElAIMRQaerQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL--------AELK 1934
Cdd:PRK12316 4944 VIDYLGRVDHQVKIRGFRIELGEIE-ARLRE---HPAVREAVVIAQEGAVGKQLVGYVVPQDPALADAdeaqaelrDELK 5019

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1935 QALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRALPLEHGTNIeYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFD 2014
Cdd:PRK12316 5020 AALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQA-YVAPRSELEQQVAAIWAEVLQLERVGLDDNFFE 5098

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15598523  2015 LGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRAFD 2065
Cdd:PRK12316 5099 LGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEK 5149
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 459-940 5.90e-134

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: 427.44  E-value: 5.90e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:cd17652    1 PDAPAV-VFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  539 LEDCGARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWM 618
Cdd:cd17652   80 LADARPALLLTT----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  619 QRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLtpflDLLDGD 698
Cdd:cd17652  126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAAL----AALPPD 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  699 ptaraAASSLRLVFCSGEALAPLQVARFrrlfGDAVRLVNLYGPTEATVDVSDHECASDNPTrVPIGRPIDNLRLYVLDR 778
Cdd:cd17652  202 -----DLPDLRTLVVAGEACPAELVDRW----APGRRMINAYGPTETTVCATMAGPLPGGGV-PPIGRPVPGTRVYVLDA 271

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  779 ALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA-GGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVE 857
Cdd:cd17652  272 RLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIE 351

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  858 PDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAE--LDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLD 935
Cdd:cd17652  352 LGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLD 431


                 ....*
gi 15598523  936 RRQLP 940
Cdd:cd17652  432 RRALP 436
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 450-940 2.19e-133

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: 426.85  E-value: 2.19e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  450 LFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD 529
Cdd:cd17644    5 LFEEQVERTPDAVAVVFEDQ-QLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  530 HPLERVRLLLEDCGARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHR 609
Cdd:cd17644   84 YPQERLTYILEDAQISVLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMIEHQ 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  610 SVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLT 689
Cdd:cd17644  130 SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWH 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  690 pfLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAVRLVNLYGPTEATVDVSDHECASD---NPTRVPIGR 766
Cdd:cd17644  210 --LLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLterNITSVPIGR 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  767 PIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA--GGRLYRTGDLARWLADGNLEYLGR 844
Cdd:cd17644  288 PIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEYLGR 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  845 ADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAE--LDPGQLRAGLSATLPDFMLPAFFVR 922
Cdd:cd17644  368 IDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEesPSTVELRQFLKAKLPDYMIPSAFVV 447

                        490
                 ....*....|....*...
gi 15598523  923 IDSLPLSANGKLDRRQLP 940
Cdd:cd17644  448 LEELPLTPNGKIDRRALP 465
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 450-940 3.98e-131

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: 419.65  E-value: 3.98e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  450 LFAEQVARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD 529
Cdd:cd17645    3 LFEEQVERTPDHVAVVD-RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  530 HPLERVRLLLEDCGARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHR 609
Cdd:cd17645   82 YPGERIAYMLADSSAKILLTN----------------------------------PDDLAYVIYTSGSTGLPKGVMIEHH 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  610 SVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTvIHFVPSMLT 689
Cdd:cd17645  128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPTGAA 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  690 PFLDLLDGdptaraaaSSLRLVFCSGEALaplqvarfRRLFGDAVRLVNLYGPTEATVDVSDHECasDNP-TRVPIGRPI 768
Cdd:cd17645  207 EQFMQLDN--------QSLRVLLTGGDKL--------KKIERKGYKLVNNYGPTENTVVATSFEI--DKPyANIPIGKPI 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  769 DNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQ 848
Cdd:cd17645  269 DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  849 VKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPL 928
Cdd:cd17645  349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPL 428

                        490
                 ....*....|..
gi 15598523  929 SANGKLDRRQLP 940
Cdd:cd17645  429 TANGKVDRKALP 440
PRK12316 PRK12316
peptide synthase; Provisional
 1046-2083 5.44e-131

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 462.89  E-value: 5.44e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1046 LEDAFPTSRLSLGLLFHSRQRPDSSVYhdVFHYRFDL-AWDEAAFRHALDRVVAAYPALRSSF-DLSGASEPLQLVHTQA 1123
Cdd:PRK12316 1553 IADIYPLSPMQQGMLFHSLYEQEAGDY--INQLRVDVqGLDPDRFRAAWQATVDRHEILRSGFlWQDGLEQPLQVIHKQV 1630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1124 RSEPLILDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAaFVR--EDGLDLVFSFHHAILDGWSVANLIVALVAAYR 1201
Cdd:PRK12316 1631 ELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLV-LVRtgEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYA 1709

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1202 GEPLPGP---------------APALACHVREELAALASPaavgywTGLLEGARMtrldgfgahePQAAQGPASHREALP 1266
Cdd:PRK12316 1710 GQPVAAPggryrdyiawlqrqdAAASEAFWKEQLAALEEP------TRLAQAART----------EDGQVGYGDHQQLLD 1773

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1267 DGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPV----RSEIAGCS 1341
Cdd:PRK12316 1774 PAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPaELPGIEQQIGLFINTLPViaapRPDQSVAD 1853

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1342 WIEVADALFRQERDghaHRRYPLSAIQQIVGDELSSAFN----YVNLHVLEPLWQ-----LRDFRV--WEETNFALLVNV 1410
Cdd:PRK12316 1854 WLQEVQALNLALRE---HEHTPLYDIQRWAGQGGEALFDsllvFENYPVAEALKQgapagLVFGRVsnHEQTNYPLTLAV 1930

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1411 iaTPSDGMYLRIDSDGRGISRSQAALIGATFVELLWRLADHPD---------EAADFAFLAPRRDAASQPEPL-VDVVSL 1480
Cdd:PRK12316 1931 --TLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQaalgelallDAGERQRILADWDRTPEAYPRgPGVHQR 2008

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1481 FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 1560
Cdd:PRK12316 2009 IAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYP 2088

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1561 AQRLALILETAQPFRVVAHP---EHAHVAAAERVLPVEElVADIE--PETFAAPQLDE--LAMLLFTSGSTGRPKGVELS 1633
Cdd:PRK12316 2089 AERLAYMLEDSGAALLLTQRhllERLPLPAGVARLPLDR-DAEWAdyPDTAPAVQLAGenLAYVIYTSGSTGLPKGVAVS 2167

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1634 HRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQRVLLPFVA 1713
Cdd:PRK12316 2168 HGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVY 2246

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1714 LQRLAEASNALGvRPGALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRP 1792
Cdd:PRK12316 2247 LQQLAEHAERDG-RPPAVRVYCFGGEAVP-AASLRLAWEALRPVYLFNGYGPTEAVvTPLLWKCRPQDPCGAAYVPIGRA 2324

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1793 LDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRAD 1871
Cdd:PRK12316 2325 LGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRID 2404

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1872 TQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARERQGNDAfLAAFLLGEPEAVDLA-ELKQALRSELPEHMVPAHF 1950
Cdd:PRK12316 2405 HQVKIRGFRIELGEIE----ARLQAHPAVREAVVVAQDGASGKQ-LVAYVVPDDAAEDLLaELRAWLAARLPAYMVPAHW 2479

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1951 AWVDGFALTPSGKRDDAALRAlPLEHGTNIEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIE 2030
Cdd:PRK12316 2480 VVLERLPLNPNGKLDRKALPK-PDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVR 2558

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15598523  2031 KRYGVDLPMAALIETPTVEGLAERLRERSAVRAFDPLVPIRAggsrPPLFLVH 2083
Cdd:PRK12316 2559 QDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRV----QPLPLSH 2607
PRK05691 PRK05691
peptide synthase; Validated
 120-1018 7.16e-131

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 462.33  E-value: 7.16e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   120 LALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYlGELGE-PQAQMPTASllaqlETDDYSGSEQYRG---DRAYF 194
Cdd:PRK05691 3374 LRLIRVDEARYWFMMSnHHILIDAWCRSLLMNDFFEIY-TALGEgREAQLPVPP-----RYRDYIGWLQRQDlaqARQWW 3447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   195 AEALEGLE-PALFTRRRPAgLRRTARHRLTLE----RTLLDA-----IRDRGESPFL----FLSAAVALYLARIHQNDDV 260
Cdd:PRK05691 3448 QDNLRGFErPTPIPSDRPF-LREHAGDSGGMVvgdcYTRLDAadgarLRELAQAHQLtvntFAQAAWALVLRRYSGDRDV 3526

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   261 VLGVPVLNRADR--AAKQVVGHFANTLPLRIR-TAPEQ--TVDEFLAQLREATRTLLRHQKMPLGDL-----LRGASPLF 330
Cdd:PRK05691 3527 LFGVTVAGRPVSmpQMQRTVGLFINSIALRVQlPAAGQrcSVRQWLQGLLDSNMELREYEYLPLVAIqecseLPKGQPLF 3606

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   331 DTTLSYMRWPA-------AQAIpNASVETvAQTHAHDP--------DALAIWVSeFDghsdaQVDFEYACdvfdadfpMD 395
Cdd:PRK05691 3607 DSLFVFENAPVevsvldrAQSL-NASSDS-GRTHTNFPltavcypgDDLGLHLS-YD-----QRYFDAPT--------VE 3670

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   396 AAARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVARTPQRTAL--LEAdggTLS 473
Cdd:PRK05691 3671 RLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAAscLDQ---QWS 3747

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   474 YAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDERA 553
Cdd:PRK05691 3748 YAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAAC 3827

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   554 ATLGESL-------GETRVLHLERLPQstGDLPAAN----VAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRY 622
Cdd:PRK05691 3828 REQARALldelgcaNRPRLLVWEEVQA--GEVASHNpgiySGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYL 3905

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   623 PIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLdlldgdPTAR 702
Cdd:PRK05691 3906 ALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGML------AEDR 3979

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   703 AAASSLRLVFCSGEALAPLQVARFRRLFGDaVRLVNLYGPTEATVDVSDH--ECASDNPTRVPIGRPIDNLRLYVLDRAL 780
Cdd:PRK05691 3980 QALDGLRWMLPTGEAMPPELARQWLQRYPQ-IGLVNAYGPAECSDDVAFFrvDLASTRGSYLPIGSPTDNNRLYLLDEAL 4058

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   781 RPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGG-RLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPD 859
Cdd:PRK05691 4059 ELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGeRLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELG 4138

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   860 EVRDRLAALPGVRDAAVVARDsAVRGTHLVGYYVAA-AELDPG----QLRAGLSATLPDFMLPAFFVRIDSLPLSANGKL 934
Cdd:PRK05691 4139 EIEARLHEQAEVREAAVAVQE-GVNGKHLVGYLVPHqTVLAQGalleRIKQRLRAELPDYMVPLHWLWLDRLPLNANGKL 4217

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   935 DRRQLPAPP----EQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQRR-GLGFELADLMR 1009
Cdd:PRK05691 4218 DRKALPALDigqlQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKAlQRNVPLRAMFE 4297


                  ....*....
gi 15598523  1010 NPTVAGLAE 1018
Cdd:PRK05691 4298 CSTVEELAE 4306
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 459-939 2.12e-129

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: 415.90  E-value: 2.12e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:cd12114    1 PDATAVICGDG-TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  539 LEDCGARVVLVDERAATLGESLGetRVLHLERLPQSTGDL-PAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNW 617
Cdd:cd12114   80 LADAGARLVLTDGPDAQLDVAVF--DVLILDLDALAAPAPpPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  618 MQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPfldLLDG 697
Cdd:cd12114  158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEM---LLDV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  698 DPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAvRLVNLYGPTEATVDVSDHECASDNPTRVPI--GRPIDNLRLYV 775
Cdd:cd12114  235 LEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDA-RLISLGGATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRV 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  776 LDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPfvAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNR 855
Cdd:cd12114  314 LDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYR 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  856 VEPDEVRDRLAALPGVRDAAVVARDSAvRGTHLVGYYVA---AAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANG 932
Cdd:cd12114  392 IELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPdndGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANG 470


                 ....*..
gi 15598523  933 KLDRRQL 939
Cdd:cd12114  471 KVDRAAL 477
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 472-939 1.77e-127

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: 409.16  E-value: 1.77e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDe 551
Cdd:cd17650   13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  552 raatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDV-L 630
Cdd:cd17650   92 ---------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVrL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  631 LQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDptaRAAASSLRL 710
Cdd:cd17650  139 LQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRN---GLDLSAMRL 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  711 VFCSGEALAPLQVARFRRLFGDAVRLVNLYGPTEATVDVS------DHECASDNptrVPIGRPIDNLRLYVLDRALRPQP 784
Cdd:cd17650  216 LIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTyyeegrDPLGDSAN---VPIGRPLPNTAMYVLDERLQPQP 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  785 LGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDR 864
Cdd:cd17650  293 VGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQ 372

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598523  865 LAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd17650  373 LARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 459-940 1.28e-124

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: 401.39  E-value: 1.28e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALLEADGgTLSYAELDAKVQAVADALRAAG-VRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRL 537
Cdd:cd17648    1 PDRVAVVYGDK-RLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  538 LLEDCGARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNW 617
Cdd:cd17648   80 ILEDTGARVVITN----------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  618 MQRRYPIGERD--VLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFlDLl 695
Cdd:cd17648  126 LSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY-DL- 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  696 dgdptarAAASSLRLVFCSGEALAPLQVARFRRLFGDavRLVNLYGPTEATVDVSDHECASDNPTRVPIGRPIDNLRLYV 775
Cdd:cd17648  204 -------ARLPHLKRVDAAGEEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYV 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  776 LDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVA--------GGRLYRTGDLARWLADGNLEYLGRADD 847
Cdd:cd17648  275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDF 354

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  848 QVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGT-----HLVGYYVAAAE-LDPGQLRAGLSATLPDFMLPAFFV 921
Cdd:cd17648  355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLV 434

                        490
                 ....*....|....*....
gi 15598523  922 RIDSLPLSANGKLDRRQLP 940
Cdd:cd17648  435 RLEGIPVTINGKLDVRALP 453
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 1480-1969 1.21e-123

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: 399.73  E-value: 1.21e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1480 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:cd17646    3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1560 PAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPET---FAAPQLDELAMLLFTSGSTGRPKGVELSHRM 1636
Cdd:cd17646   83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPAtppLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1637 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRV------LLP 1710
Cdd:cd17646  163 IVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTChfvpsmLRV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1711 FVALQRLAEAsnalgvrpGALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDpaHYPDLPPI 1789
Cdd:cd17646  243 FLAEPAAGSC--------ASLRRVFCSGEAL--PPELAARFLALPGAELHNLYGPTEAAiDVTHWPVRGP--AETPSVPI 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1790 GRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGR 1869
Cdd:cd17646  311 GRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGR 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1870 ADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEP--EAVDLAELKQALRSELPEHMVP 1947
Cdd:cd17646  391 SDDQVKIRGFRVEPGEIEAAL----AAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVP 466

                        490       500
                 ....*....|....*....|..
gi 15598523 1948 AHFAWVDGFALTPSGKRDDAAL 1969
Cdd:cd17646  467 AAFVVLDALPLTANGKLDRAAL 488
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 455-939 3.21e-123

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: 397.00  E-value: 3.21e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  455 VARTPQRTALLEAdGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLER 534
Cdd:cd05945    1 AAANPDRPAVVEG-GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  535 VRLLLEDCGARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNR 614
Cdd:cd05945   80 IREILDAAKPALLIAD----------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  615 LNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSmltpFLDL 694
Cdd:cd05945  126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPS----FAAM 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  695 LDGDPT-ARAAASSLRLVFCSGEALAPLQVARFRRLFGDAvRLVNLYGPTEATVDVSDHEC---ASDNPTRVPIGRPIDN 770
Cdd:cd05945  202 CLLSPTfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDA-RIYNTYGPTEATVAVTYIEVtpeVLDGYDRLPIGYAKPG 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  771 LRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPfvaGGRLYRTGDLARWLADGNLEYLGRADDQVK 850
Cdd:cd05945  281 AKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVK 357

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  851 IRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQ---LRAGLSATLPDFMLPAFFVRIDSLP 927
Cdd:cd05945  358 LNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLtkaIKAELAERLPPYMIPRRFVYLDELP 437

                        490
                 ....*....|..
gi 15598523  928 LSANGKLDRRQL 939
Cdd:cd05945  438 LNANGKIDRKAL 449
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1480-1969 6.64e-122

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: 394.65  E-value: 6.64e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1480 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:cd12117    2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1560 PAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR-- 1635
Cdd:cd12117   82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVspDDLAYVMYTSGSTGRPKGVAVTHRgv 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1636 ----MWANYtqwqlrvASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPF 1711
Cdd:cd12117  162 vrlvKNTNY-------VTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1712 VALQRLAEAsnalgvRPGA---LRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAHYPDLPP 1788
Cdd:cd12117  235 ALFNQLADE------DPECfagLRELLTGGEVVSP-PHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIP 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1789 IGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLG 1868
Cdd:cd12117  308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1869 RADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEpEAVDLAELKQALRSELPEHMVPA 1948
Cdd:cd12117  388 RIDDQVKIRGFRIELGEIEAAL----RAHPGVREAVVVVREDAGGDKRLVAYVVAE-GALDAAELRAFLRERLPAYMVPA 462

                        490       500
                 ....*....|....*....|.
gi 15598523 1949 HFAWVDGFALTPSGKRDDAAL 1969
Cdd:cd12117  463 AFVVLDELPLTANGKVDRRAL 483
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1502-1905 1.48e-118

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: 382.00  E-value: 1.48e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1502 TYRDLDHVARCVATRLV-RAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHP 1580
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1581 EHAHVAAA---ERVLPVEELVADIEPET-----FAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVP 1652
Cdd:TIGR01733   81 ALASRLAGlvlPVILLDPLELAALDDAPappppDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1653 GLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALL-HVLERRQVQRVLLPFVALQRLAEASNAlgvRPGAL 1731
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLaALIAEHPVTVLNLTPSLLALLAAALPP---ALASL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1732 RVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPV 1810
Cdd:TIGR01733  238 RLVILGGEALT-PALVDRWRARGPGARLINLYGPTETTvWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPV 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1811 GVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRP--GARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVEL 1888
Cdd:TIGR01733  317 GVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 396

                          410
                   ....*....|....*..
gi 15598523   1889 AIMrqaeRQPGLRGAAV 1905
Cdd:TIGR01733  397 ALL----RHPGVREAVV 409
PRK12316 PRK12316
peptide synthase; Provisional
 1067-2063 1.32e-116

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 416.67  E-value: 1.32e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1067 PDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDlSGASEPLQLVHTQARSEPLILDLRGNPEAGtvLDEHI 1146
Cdd:PRK12316   67 PQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFP-RGADDSLAQVPLDRPLEVEFEDCSGLPEAE--QEARL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1147 RQRrFHRYSLQ----QPGLFLFAAFVREDGLD--LVFSFHHAILDGWSVANLIVALVAAYRG---------EPLPGPAPA 1211
Cdd:PRK12316  144 RDE-AQRESLQpfdlCEGPLLRVRLLRLGEEEhvLLLTLHHIVSDGWSMNVLIEEFSRFYSAyatgaepglPALPIQYAD 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1212 LACHVREELAALASPAAVGYWTGLLeGARMTRLDGFGAHEPQAAQGP--ASHREALPDGLLERLKATAAQRGLPLKSLLL 1289
Cdd:PRK12316  223 YALWQRSWLEAGEQERQLEYWRAQL-GEEHPVLELPTDHPRPAVPSYrgSRYEFSIDPALAEALRGTARRQGLTLFMLLL 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1290 AAHCLTLHLFS-RSDSVVTGAISN-GRPELpdaDRMVGLFLNTVPVRSEIAG-CSWIEVADALFRQERDGHAHRRYPLSA 1366
Cdd:PRK12316  302 GAFNVLLHRYSgQTDIRVGVPIANrNRAEV---EGLIGFFVNTQVLRSVFDGrTRVATLLAGVKDTVLGAQAHQDLPFER 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1367 I----------------------QQIVGD-ELSSAFNYVNLHVLEplWQLRdfrvweETNFALLVNVIATPsDGMYLRID 1423
Cdd:PRK12316  379 LvealkverslshsplfqvmynhQPLVADiEALDTVAGLEFGQLE--WKSR------TTQFDLTLDTYEKG-GRLHAALT 449

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1424 SDGRGISRSQAALIGATFVELLWRLADHPD---------EAADFAFLAPRRDAASQPEPLV-DVVSLFERQVEALPGSAA 1493
Cdd:PRK12316  450 YATDLFEARTVERMARHWQNLLRGMVENPQarvdelpmlDAEERGQLVEGWNATAAEYPLQrGVHRLFEEQVERTPEAPA 529

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1494 LAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQp 1573
Cdd:PRK12316  530 LAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSG- 608

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1574 FRVVAHPEHAH----VAAAERVLPVEELVADIEPETFAAPQL----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQL 1645
Cdd:PRK12316  609 VQLLLSQSHLGrklpLAAGVQVLDLDRPAAWLEGYSEENPGTelnpENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQ 688

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1646 RVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALG 1725
Cdd:PRK12316  689 QAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS 768

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1726 VRPgaLRVVVSSGEQLRITEDVRAFcAAMPGLLLENQYGPTETHQVTYHSLSGDPAhyPDLPPIGRPLDGVEVQVLDAAL 1805
Cdd:PRK12316  769 CTS--LRRIVCSGEALPADAQEQVF-AKLPQAGLYNLYGPTEAAIDVTHWTCVEEG--GDSVPIGRPIANLACYILDANL 843

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1806 RPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAE 1885
Cdd:PRK12316  844 EPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 923

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1886 VELAIMrqaeRQPGLRGAAVVARERQGndafLAAFLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTPSGKR 1964
Cdd:PRK12316  924 IEARLL----EHPWVREAAVLAVDGKQ----LVGYVVLESEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1965 DDaalRALPLEHGTNI--EYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRfMLLIEKRYGVDLPMAAL 2042
Cdd:PRK12316  996 DR---KALPAPEASVAqqGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQ-VVSRARQAGIQLSPRDL 1071

                        1050      1060
                  ....*....|....*....|.
gi 15598523  2043 IETPTVEGLAERLRERSAVRA 2063
Cdd:PRK12316 1072 FQHQTIRSLALVAKAGQATAA 1092
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 458-940 5.99e-116

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: 377.58  E-value: 5.99e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  458 TPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRL 537
Cdd:cd17656    1 TPDAVAVVFENQ-KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  538 LLEDCGARVVLVDERAATLGESLGETRVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNW 617
Cdd:cd17656   80 IMLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  618 MQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIhFVPSMLTPFLDLLDG 697
Cdd:cd17656  160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSERE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  698 dpTARAAASSLRLVFCSGEALAPLQVarFRRLFGD-AVRLVNLYGPTEA------TVDVSDHEcasdnPTRVPIGRPIDN 770
Cdd:cd17656  239 --FINRFPTCVKHIITAGEQLVITNE--FKEMLHEhNVHLHNHYGPSEThvvttyTINPEAEI-----PELPPIGKPISN 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  771 LRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVK 850
Cdd:cd17656  310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  851 IRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSA 930
Cdd:cd17656  390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTP 469

                        490
                 ....*....|
gi 15598523  931 NGKLDRRQLP 940
Cdd:cd17656  470 NGKVDRKALP 479
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 1489-1969 7.55e-114

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: 371.42  E-value: 7.55e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:cd17656    2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1569 ETAQPFRVVAHPEHAHVAAAER--VLPVEELVADIEPETF-AAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQL 1645
Cdd:cd17656   82 LDSGVRVVLTQRHLKSKLSFNKstILLEDPSISQEDTSNIdYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1646 RVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALG 1725
Cdd:cd17656  162 EKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFIN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1726 VRPGALRVVVSSGEQLRITEDVRAFCAAMpGLLLENQYGPTETHQVTYHSLSGDPaHYPDLPPIGRPLDGVEVQVLDAAL 1805
Cdd:cd17656  242 RFPTCVKHIITAGEQLVITNEFKEMLHEH-NVHLHNHYGPSETHVVTTYTINPEA-EIPELPPIGKPISNTWIYILDQEQ 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1806 RPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAE 1885
Cdd:cd17656  320 QLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1886 VELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEpEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 1965
Cdd:cd17656  400 IEAQLL----NHPGVSEAVVLDKADDKGEKYLCAYFVME-QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474


                 ....
gi 15598523 1966 DAAL 1969
Cdd:cd17656  475 RKAL 478
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 447-950 2.74e-113

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: 368.75  E-value: 2.74e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  447 LPTLFAEQVARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPI 526
Cdd:COG0318    1 LADLLRRAAARHPDRPALVF-GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  527 NPDHPLERVRLLLEDCGARVVLVderaatlgeslgetrvlhlerlpqstgdlpaanvapgdlAYVIYTSGSTGMPKGVMV 606
Cdd:COG0318   80 NPRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVML 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  607 EHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSF-TGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVP 685
Cdd:COG0318  121 THRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLlAGATLVLLP---RFDPERVLELIERERVTVLFGVP 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  686 SMLTpflDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVSDHECASDNPTRVPIG 765
Cdd:COG0318  198 TMLA---RLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPGERRPGSVG 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  766 RPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlvdpfvAGGrLYRTGDLARWLADGNLEYLGRA 845
Cdd:COG0318  273 RPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF------RDG-WLRTGDLGRLDEDGYLYIVGRK 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  846 DDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDPGQLRAGLSATLPDFMLPAFFVRI 923
Cdd:COG0318  346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRRVEFV 425

                        490       500
                 ....*....|....*....|....*..
gi 15598523  924 DSLPLSANGKLDRRQLPAPPEQVAAVA 950
Cdd:COG0318  426 DELPRTASGKIDRRALRERYAAGALEA 452
AMP-binding pfam00501
AMP-binding enzyme;
451-852 1.72e-112

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 365.10  E-value: 1.72e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    451 FAEQVARTPQRTALLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDH 530
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    531 PLERVRLLLEDCGARVVLVDERA------ATLGESLGETRVLHLERLPQSTGDL-------------PAANVAPGDLAYV 591
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellEALGKLEVVKLVLVLDRDPVLKEEPlpeeakpadvpppPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    592 IYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYP----IGERDVLLQKTPVTFDVSV-WELFWWSFTGARLSLLPPGAEKDP 666
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    667 REMLRSIQRDAVTVIHFVPSMltpFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAVrlVNLYGPTEAT 746
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTL---LNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGAL--VNGYGLTETT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    747 VDVSDHECASDNPTRVP-IGRPIDNLRLYVLDRA-LRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDpfvaggRL 824
Cdd:pfam00501  316 GVVTTPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------GW 389

                          410       420
                   ....*....|....*....|....*...
gi 15598523    825 YRTGDLARWLADGNLEYLGRADDQVKIR 852
Cdd:pfam00501  390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 447-939 2.03e-112

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: 367.25  E-value: 2.03e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  447 LPTLFAEQVARTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPI 526
Cdd:cd05918    1 VHDLIEERARSQPDAPAV-CAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  527 NPDHPLERVRLLLEDCGARVVLVDEraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMV 606
Cdd:cd05918   80 DPSHPLQRLQEILQDTGAKVVLTSS---------------------------------PSDAAYVIFTSGSTGKPKGVVI 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  607 EHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFW-WSFtGARLSLLPpgaEKDPREML-RSIQRDAVTVIHFV 684
Cdd:cd05918  127 EHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTtLAA-GGCLCIPS---EEDRLNDLaGFINRLRVTWAFLT 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  685 PSmltpFLDLLDgdptaRAAASSLRLVFCSGEALAPLQVARFrrlfGDAVRLVNLYGPTEATVDVSDHECASDNPTRVpI 764
Cdd:cd05918  203 PS----VARLLD-----PEDVPSLRTLVLGGEALTQSDVDTW----ADRVRLINAYGPAECTIAATVSPVVPSTDPRN-I 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  765 GRPIDNlRLYVLDRA--LRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDP-------FVAGGRLYRTGDLARWLA 835
Cdd:cd05918  269 GRPLGA-TCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNP 347

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  836 DGNLEYLGRADDQVKIRGNRVEPDEVRDRL-AALPGVRD--AAVVARDSAVRGTHLVGYYVAA----------------- 895
Cdd:cd05918  348 DGSLEYVGRKDTQVKIRGQRVELGEIEHHLrQSLPGAKEvvVEVVKPKDGSSSPQLVAFVVLDgsssgsgdgdslfleps 427

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 15598523  896 --AELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05918  428 deFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 1489-1969 2.57e-112

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: 365.04  E-value: 2.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:cd17652    1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1569 ETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVA 1648
Cdd:cd17652   81 ADARPALLLTTPDN-------------------------------LAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1649 SGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNAlgvrp 1728
Cdd:cd17652  130 DVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLP----- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1729 gALRVVVSSGEQLRiTEDVRAFCaamPGLLLENQYGPTEThqvTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPV 1808
Cdd:cd17652  205 -DLRTLVVAGEACP-AELVDRWA---PGRRMINAYGPTET---TVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1809 PVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWR-PGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 1887
Cdd:cd17652  277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGaPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1888 LAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDD 1966
Cdd:cd17652  357 AAL----TEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPgAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432


                 ...
gi 15598523 1967 AAL 1969
Cdd:cd17652  433 RAL 435
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 1489-1970 4.74e-112

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: 365.15  E-value: 4.74e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:cd17649    1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1569 ETAQPFRVVAHpehahvaaaervlpveelvadiEPETfaapqldeLAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVA 1648
Cdd:cd17649   81 EDSGAGLLLTH----------------------HPRQ--------LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERY 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1649 SGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVR- 1727
Cdd:cd17649  131 GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGr 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1728 PGALRVVVSSGEQLRItEDVRAFCAAmpGLLLENQYGPTET--HQVTYHSLSGDPAHYPDLPpIGRPLDGVEVQVLDAAL 1805
Cdd:cd17649  211 PPSLRLYIFGGEALSP-ELLRRWLKA--PVRLFNAYGPTEAtvTPLVWKCEAGAARAGASMP-IGRPLGGRSAYILDADL 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1806 RPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPA 1884
Cdd:cd17649  287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1885 EVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPE--AVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 1962
Cdd:cd17649  367 EIEAALL----EHPGVREAAVVALDGAGGKQLVAYVVLRAAAaqPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNG 442


                 ....*...
gi 15598523 1963 KRDDAALR 1970
Cdd:cd17649  443 KLDRKALP 450
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1480-1973 3.53e-111

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: 363.96  E-value: 3.53e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1480 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:cd17655    2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1560 PAQRLALILETAQPFRVVAHPEHAH-VAAAERVLPVEELVADIEPETFAAP--QLDELAMLLFTSGSTGRPKGVELSHRM 1636
Cdd:cd17655   82 PEERIQYILEDSGADILLTQSHLQPpIAFIGLIDLLDEDTIYHEESENLEPvsKSDDLAYVIYTSGSTGKPKGVMIEHRG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1637 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQR 1716
Cdd:cd17655  162 VVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1717 LAEASNALGVRpgaLRVVVSSGEQL------RITEDVRAFCAampgllLENQYGPTETH-QVTYHSLSGDPAHYPDlPPI 1789
Cdd:cd17655  242 LDAADDSEGLS---LKHLIVGGEALstelakKIIELFGTNPT------ITNAYGPTETTvDASIYQYEPETDQQVS-VPI 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1790 GRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGR 1869
Cdd:cd17655  312 GKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGR 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1870 ADTQVKVRGFRIEPAEVElAIMRQAerqPGLRGAAVVARERQGNDAFLAAFLLGEPEAvDLAELKQALRSELPEHMVPAH 1949
Cdd:cd17655  392 IDHQVKIRGYRIELGEIE-ARLLQH---PDIKEAVVIARKDEQGQNYLCAYIVSEKEL-PVAQLREFLARELPDYMIPSY 466

                        490       500
                 ....*....|....*....|....
gi 15598523 1950 FAWVDGFALTPSGKRDdaaLRALP 1973
Cdd:cd17655  467 FIKLDEIPLTPNGKVD---RKALP 487
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1480-1969 1.30e-108

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: 355.09  E-value: 1.30e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1480 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:cd12115    4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1560 PAQRLALILETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHRMWAN 1639
Cdd:cd12115   84 PPERLRFILEDAQARLVLTDPDD-------------------------------LAYVIYTSGSTGRPKGVAIEHRNAAA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1640 YTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNrermdpsaLLHVLERRQVQRVLL----PFVALQ 1715
Cdd:cd12115  133 FLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADN--------VLALPDLPAAAEVTLintvPSAAAE 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1716 RLAeasnaLGVRPGALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTEThqVTYHSLSGDPAHYPDLPPIGRPLDG 1795
Cdd:cd12115  205 LLR-----HDALPASVRVVNLAGEPLP-RDLVQRLYARLQVERVVNLYGPSED--TTYSTVAPVPPGASGEVSIGRPLAN 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1796 VEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVK 1875
Cdd:cd12115  277 TQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVK 356

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1876 VRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVD 1954
Cdd:cd12115  357 VRGFRIELGEIEAAL----RSIPGVREAVVVAIGDAAGERRLVAYIVAEPgAAGLVEDLRRHLGTRLPAYMVPSRFVRLD 432

                        490
                 ....*....|....*
gi 15598523 1955 GFALTPSGKRDDAAL 1969
Cdd:cd12115  433 ALPLTPNGKIDRSAL 447
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 1489-1969 1.85e-107

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: 352.75  E-value: 1.85e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:cd12116    1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1569 ETAQPFRVVAHPEHAHVAAAErvLPVEELVADIEPETFAAPQ----LDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQ 1644
Cdd:cd12116   81 EDAEPALVLTDDALPDRLPAG--LPVLLLALAAAAAAPAAPRtpvsPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1645 LRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVqrvllpfvalqrlaeasNAL 1724
Cdd:cd12116  159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSI-----------------TVM 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1725 GVRPGALRVVVSSGEQLRitEDVRAFC---AAMPGLL---------LENQYGPTETH-QVTYHSLSGDPAHypdlPPIGR 1791
Cdd:cd12116  222 QATPATWRMLLDAGWQGR--AGLTALCggeALPPDLAarllsrvgsLWNLYGPTETTiWSTAARVTAAAGP----IPIGR 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1792 PLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWR-PGARLYRTGDLGRILGNGEIVWLGRA 1870
Cdd:cd12116  296 PLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRA 375

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1871 DTQVKVRGFRIEPAEVElAIMRqaeRQPGLRGAAVVARErQGNDAFLAAFL-LGEPEAVDLAELKQALRSELPEHMVPAH 1949
Cdd:cd12116  376 DGQVKIRGHRIELGEIE-AALA---AHPGVAQAAVVVRE-DGGDRRLVAYVvLKAGAAPDAAALRAHLRATLPAYMVPSA 450

                        490       500
                 ....*....|....*....|
gi 15598523 1950 FAWVDGFALTPSGKRDDAAL 1969
Cdd:cd12116  451 FVRLDALPLTANGKLDRKAL 470
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1480-1973 3.19e-106

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: 348.66  E-value: 3.19e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1480 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:cd17644    5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1560 PAQRLALILETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHRMWAN 1639
Cdd:cd17644   85 PQERLTYILEDAQISVLLTQPEN-------------------------------LAYVIYTSGSTGKPKGVMIEHQSLVN 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1640 YTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLA- 1718
Cdd:cd17644  134 LSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVl 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1719 EASNALGVRPGALRVVVSSGEqlRITEDVRAFCAAMPGLLLE--NQYGPTE-THQVTYHSLSGDPAHYPDLPPIGRPLDG 1795
Cdd:cd17644  214 ELLLSTIDLPSSLRLVIVGGE--AVQPELVRQWQKNVGNFIQliNVYGPTEaTIAATVCRLTQLTERNITSVPIGRPIAN 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1796 VEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWR--PGARLYRTGDLGRILGNGEIVWLGRADTQ 1873
Cdd:cd17644  292 TQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLGRIDNQ 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1874 VKVRGFRIEPAEVElAIMRQaerQPGLRGAAVVARERQGNDAFLAAFLLGE-PEAVDLAELKQALRSELPEHMVPAHFAW 1952
Cdd:cd17644  372 VKIRGFRIELGEIE-AVLSQ---HNDVKTAVVIVREDQPGNKRLVAYIVPHyEESPSTVELRQFLKAKLPDYMIPSAFVV 447

                        490       500
                 ....*....|....*....|.
gi 15598523 1953 VDGFALTPSGKRDDaalRALP 1973
Cdd:cd17644  448 LEELPLTPNGKIDR---RALP 465
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 450-939 1.66e-105

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: 345.45  E-value: 1.66e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  450 LFAEQVARTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD 529
Cdd:cd17653    2 AFERIAAAHPDAVAV-ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  530 HPLERVRLLLEDCGARVVLvderaatlgeslgetrvlhlerlpqstgdlpaANVAPGDLAYVIYTSGSTGMPKGVMVEHR 609
Cdd:cd17653   81 LPSARIQAILRTSGATLLL--------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMVPHR 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  610 SVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLlppgaeKDPREMLRSIQRdAVTVIHFVPSmlt 689
Cdd:cd17653  129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVAR-TVDALMSTPS--- 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  690 pFLDLLDGDPTaraaaSSLRLVFCSGEALAPLQVARFrrlfGDAVRLVNLYGPTEATVDVSDHECASDNPtrVPIGRPID 769
Cdd:cd17653  199 -ILSTLSPQDF-----PNLKTIFLGGEAVPPSLLDRW----SPGRRLYNAYGPTECTISSTMTELLPGQP--VTIGKPIP 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  770 NLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQV 849
Cdd:cd17653  267 NSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQV 346

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  850 KIRGNRVEPDEVRDRLAAL-PGVRDAAVVardsAVRGThLVGyYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPL 928
Cdd:cd17653  347 KVRGFRINLEEIEEVVLQSqPEVTQAAAI----VVNGR-LVA-FVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPL 420

                        490
                 ....*....|.
gi 15598523  929 SANGKLDRRQL 939
Cdd:cd17653  421 TANGKVDRKAL 431
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 1489-1969 5.77e-105

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: 344.68  E-value: 5.77e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:cd17643    1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1569 ETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHR-----MWAnyTQW 1643
Cdd:cd17643   81 ADSGPSLLLTDPDD-------------------------------LAYVIYTSGSTGRPKGVVVSHAnvlalFAA--TQR 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1644 QLRVAsgvPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQrVL--LPfVALQRLAEAS 1721
Cdd:cd17643  128 WFGFN---EDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVT-VLnqTP-SAFYQLVEAA 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1722 NALGVRPGALRVVVSSGEQLRITEdVRAFCAAM--PGLLLENQYGPTET--HqVTYHSLSGDPAHYPDLPPIGRPLDGVE 1797
Cdd:cd17643  203 DRDGRDPLALRYVIFGGEALEAAM-LRPWAGRFglDRPQLVNMYGITETtvH-VTFRPLDAADLPAAAASPIGRPLPGLR 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1798 VQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKV 1876
Cdd:cd17643  281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1877 RGFRIEPAEVELAIMrqaeRQPGLRGAAVVARE-RQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDG 1955
Cdd:cd17643  361 RGFRIELGEIEAALA----THPSVRDAAVIVREdEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDA 436

                        490
                 ....*....|....
gi 15598523 1956 FALTPSGKRDDAAL 1969
Cdd:cd17643  437 LPLTVNGKLDRAAL 450
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1477-1972 1.43e-98

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: 327.19  E-value: 1.43e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1477 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 1556
Cdd:cd05918    1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1557 VSYPAQRLALILETAQpfrvvahpehAHVAAAErvlpveelvadiepetfaapQLDELAMLLFTSGSTGRPKGVELSHRM 1636
Cdd:cd05918   81 PSHPLQRLQEILQDTG----------AKVVLTS--------------------SPSDAAYVIFTSGSTGKPKGVVIEHRA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1637 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDpsALLHVLERRQVQRVLL-PFVAlq 1715
Cdd:cd05918  131 LSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLtPSVA-- 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1716 RLaeasnalgVRPGA---LRVVVSSGEQLRiTEDVRAFCaamPGLLLENQYGPTEThqvTYHSLSGDPAHYPDLPPIGRP 1792
Cdd:cd05918  207 RL--------LDPEDvpsLRTLVLGGEALT-QSDVDTWA---DRVRLINAYGPAEC---TIAATVSPVVPSTDPRNIGRP 271

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1793 LDGVeVQVLDAA--LRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHP-WR------PGARLYRTGDLGRILGNGE 1863
Cdd:cd05918  272 LGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPaWLkqegsgRGRRLYRTGDLVRYNPDGS 350

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1864 IVWLGRADTQVKVRGFRIEPAEVELAImRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVD-------------- 1929
Cdd:cd05918  351 LEYVGRKDTQVKIRGQRVELGEIEHHL-RQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGsgdgdslflepsde 429

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 15598523 1930 ----LAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:cd05918  430 fralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
PRK05691 PRK05691
peptide synthase; Validated
 1046-2056 1.87e-98

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 357.17  E-value: 1.87e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1046 LEDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARS 1125
Cdd:PRK05691 3254 IEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRT 3333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1126 EPLILDLRGNPEAGT---VLDEHIRQRRFHRYSLQQPGLFLFAAFVREDGLDLVFSFHHAILDGWSVANLIVALVAAY-- 1200
Cdd:PRK05691 3334 PIDYLDWRGLPEDGQeqrLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYta 3413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1201 --RGEPLPGPAPAlacHVREELAALASPAavgywtglLEGAR---MTRLDGFGAHEPQAAQGPASHREALPDGLLE---- 1271
Cdd:PRK05691 3414 lgEGREAQLPVPP---RYRDYIGWLQRQD--------LAQARqwwQDNLRGFERPTPIPSDRPFLREHAGDSGGMVvgdc 3482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1272 ----------RLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPVRSEIAG- 1339
Cdd:PRK05691 3483 ytrldaadgaRLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvSMPQMQRTVGLFINSIALRVQLPAa 3562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1340 ---CSWIEVADALFRQERDGHAHRRYPLSAIQQIV----GDEL-SSAFNYVNLHV-LEPLWQLRDFRVWEE-----TNFA 1405
Cdd:PRK05691 3563 gqrCSVRQWLQGLLDSNMELREYEYLPLVAIQECSelpkGQPLfDSLFVFENAPVeVSVLDRAQSLNASSDsgrthTNFP 3642

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1406 LlvNVIATPSDGMYLRIDSDGRGISRSQAALIGATFVELLWRLADHPD-EAADFAFLAPRR-----DAASQPE---PL-V 1475
Cdd:PRK05691 3643 L--TAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHgDLSELPLLGEQErdfllDGCNRSErdyPLeQ 3720

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1476 DVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL 1555
Cdd:PRK05691 3721 SYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3800

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1556 DVSYPAQRLALILE-TAQPFRVV--AHPEHAHVAAAE-------RVLPVEEL----VADIEPETFAAPqlDELAMLLFTS 1621
Cdd:PRK05691 3801 DPGLPAQRLQRIIElSRTPVLVCsaACREQARALLDElgcanrpRLLVWEEVqageVASHNPGIYSGP--DNLAYVIYTS 3878

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1622 GSTGRPKGVELSHR-MWANytqwQLrvaSGVPGLR------TLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSA 1694
Cdd:PRK05691 3879 GSTGLPKGVMVEQRgMLNN----QL---SKVPYLAlseadvIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQG 3951

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1695 LL-HVLERRQVQRVLLPFVALQRLAEASNALGvrpgALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTEThqvty 1773
Cdd:PRK05691 3952 LLaHVQAQGITVLESVPSLIQGMLAEDRQALD----GLRWMLPTGEAMP-PELARQWLQRYPQIGLVNAYGPAEC----- 4021

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1774 hslSGDPAHYP-DLP-------PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPW-R 1844
Cdd:PRK05691 4022 ---SDDVAFFRvDLAstrgsylPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgA 4098

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1845 PGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQAErqpgLRGAAVVARERQgNDAFLAAFLLGE 1924
Cdd:PRK05691 4099 PGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAE----VREAAVAVQEGV-NGKHLVGYLVPH 4173

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1925 PEAVDLAEL----KQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRALPLEHGTNIEYLAPRDDYERTLAGLLGEL 2000
Cdd:PRK05691 4174 QTVLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADV 4253

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  2001 LDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLR 2056
Cdd:PRK05691 4254 LKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 1489-1969 7.66e-97

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: 322.30  E-value: 7.66e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:cd12114    1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1569 ETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAA--PQLDELAMLLFTSGSTGRPKGVELSHRMWANY-----T 1641
Cdd:cd12114   81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPvdVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTildinR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1642 QWQLRvasgvPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVqrVLLPFVA--LQRLAE 1719
Cdd:cd12114  161 RFAVG-----PDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGV--TLWNSVPalLEMLLD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1720 ASNALGVRPGALRVVVSSGEqlRITEDV-RAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLpPIGRPLDGVE 1797
Cdd:cd12114  234 VLEAAQALLPSLRLVLLSGD--WIPLDLpARLRALAPDARLISLGGATEASiWSIYHPIDEVPPDWRSI-PYGRPLANQR 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1798 VQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPwrPGARLYRTGDLGRILGNGEIVWLGRADTQVKVR 1877
Cdd:cd12114  311 YRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1878 GFRIEPAEVElaimRQAERQPGLRGAAVVAReRQGNDAFLAAFLLGEPEA--VDLAELKQALRSELPEHMVPAHFAWVDG 1955
Cdd:cd12114  389 GYRIELGEIE----AALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGtpIAPDALRAFLAQTLPAYMIPSRVIALEA 463

                        490
                 ....*....|....
gi 15598523 1956 FALTPSGKRDDAAL 1969
Cdd:cd12114  464 LPLTANGKVDRAAL 477
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1485-1969 7.53e-95

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: 315.34  E-value: 7.53e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1485 VEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRL 1564
Cdd:cd05945    1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1565 ALILETAQPFRVVAHPehahvaaaervlpveelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQ 1644
Cdd:cd05945   81 REILDAAKPALLIADG-------------------------------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1645 LRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVL-LP-FVALQRLAEASN 1722
Cdd:cd05945  130 LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVsTPsFAAMCLLSPTFT 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1723 ALGVrpGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTE-THQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVL 1801
Cdd:cd05945  210 PESL--PSLRHFLFCGEVLPH-KTARALQQRFPDARIYNTYGPTEaTVAVTYIEVTPEVLDGYDRLPIGYAKPGAKLVIL 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1802 DAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpwrPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRI 1881
Cdd:cd05945  287 DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1882 EPAEVElaimRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEP--EAVDLAELKQALRSELPEHMVPAHFAWVDGFALT 1959
Cdd:cd05945  364 ELEEIE----AALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLN 439

                        490
                 ....*....|
gi 15598523 1960 PSGKRDDAAL 1969
Cdd:cd05945  440 ANGKIDRKAL 449
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 1489-1969 7.59e-94

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: 312.48  E-value: 7.59e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:cd17650    1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1569 ETAqpfrvvahpehahvaAAERVLpveelvadIEPEtfaapqldELAMLLFTSGSTGRPKGVELSHRMWAN-YTQWQLRV 1647
Cdd:cd17650   81 EDS---------------GAKLLL--------TQPE--------DLAYVIYTSGTTGKPKGVMVEHRNVAHaAHAWRREY 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1648 ASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQ-RVLLPFVALQRLAEASNAlGV 1726
Cdd:cd17650  130 ELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITlMESTPALIRPVMAYVYRN-GL 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1727 RPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTE-THQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAAL 1805
Cdd:cd17650  209 DLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEaTIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERL 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1806 RPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAE 1885
Cdd:cd17650  289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGE 368

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1886 VELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEpEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 1965
Cdd:cd17650  369 IESQLA----RHPAIDEAVVAVREDKGGEARLCAYVVAA-ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443


                 ....
gi 15598523 1966 DAAL 1969
Cdd:cd17650  444 RRAL 447
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1479-1970 2.28e-93

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: 310.40  E-value: 2.28e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1479 SLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVS 1558
Cdd:cd17653    1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1559 YPAQRLALILETAQPFRVVAhpehahvaaaervlpveelvadiepetfaAPQLDELAMLLFTSGSTGRPKGVELSHRMWA 1638
Cdd:cd17653   81 LPSARIQAILRTSGATLLLT-----------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1639 NYTQW-QLRVASGvPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLisnRERMDPSAllHVLERRQVQRVLLPFVALQRL 1717
Cdd:cd17653  132 NYVSQpPARLDVG-PGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL---ADPSDPFA--HVARTVDALMSTPSILSTLSP 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1718 AEASNalgvrpgaLRVVVSSGEqlritedvrafcAAMPGLL--------LENQYGPTE-THQVTYHSLsgdpahYPDLP- 1787
Cdd:cd17653  206 QDFPN--------LKTIFLGGE------------AVPPSLLdrwspgrrLYNAYGPTEcTISSTMTEL------LPGQPv 259

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1788 PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWL 1867
Cdd:cd17653  260 TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFL 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1868 GRADTQVKVRGFRIEPAEVELAIMRQaerQPGLRGAAVVarerQGNDaFLAAFLLgePEAVDLAELKQALRSELPEHMVP 1947
Cdd:cd17653  340 GREDNQVKVRGFRINLEEIEEVVLQS---QPEVTQAAAI----VVNG-RLVAFVT--PETVDVDGLRSELAKHLPSYAVP 409

                        490       500
                 ....*....|....*....|...
gi 15598523 1948 AHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd17653  410 DRIIALDSFPLTANGKVDRKALR 432
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1477-1976 2.50e-92

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: 308.28  E-value: 2.50e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1477 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 1556
Cdd:COG0318    1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1557 VSYPAQRLALILETAQPfRVVahpehahVAAAervlpveelvadiepetfaapqldelamLLFTSGSTGRPKGVELSHRM 1636
Cdd:COG0318   81 PRLTAEELAYILEDSGA-RAL-------VTAL----------------------------ILYTSGTTGRPKGVMLTHRN 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1637 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAF-QEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQ 1715
Cdd:COG0318  125 LLANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGVPTMLA 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1716 RLAEASNALGVRPGALRVVVSSGEQLRiTEDVRAFCAAMpGLLLENQYGPTETHQVTyhSLSGDPAHYPDLPPIGRPLDG 1795
Cdd:COG0318  202 RLLRHPEFARYDLSSLRLVVSGGAPLP-PELLERFEERF-GVRIVEGYGLTETSPVV--TVNPEDPGERRPGSVGRPLPG 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1796 VEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEhPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVK 1875
Cdd:COG0318  278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-GW------LRTGDLGRLDEDGYLYIVGRKKDMII 350

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1876 VRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGnDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWV 1953
Cdd:COG0318  351 SGGENVYPAEVEEVLA----AHPGVAEAAVVGVpdEKWG-ERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFV 425

                        490       500
                 ....*....|....*....|...
gi 15598523 1954 DGFALTPSGKRDDAALRALPLEH 1976
Cdd:COG0318  426 DELPRTASGKIDRRALRERYAAG 448
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1480-1969 1.75e-91

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: 305.25  E-value: 1.75e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1480 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:cd17645    3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1560 PAQRLALILETAQPFRVVAHPehahvaaaervlpveelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHRMWAN 1639
Cdd:cd17645   83 PGERIAYMLADSSAKILLTNP-------------------------------DDLAYVIYTSGSTGLPKGVMIEHHNLVN 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1640 YTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAE 1719
Cdd:cd17645  132 LCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQ 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1720 ASNAlgvrpgALRVVVSSGEQLRITEDvrafcaamPGLLLENQYGPTEtHQVTYHSLSGDPAHYPdlPPIGRPLDGVEVQ 1799
Cdd:cd17645  212 LDNQ------SLRVLLTGGDKLKKIER--------KGYKLVNNYGPTE-NTVVATSFEIDKPYAN--IPIGKPIDNTRVY 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1800 VLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGF 1879
Cdd:cd17645  275 ILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGY 354

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1880 RIEPAEVELAIMRQAERQPglrgAAVVARERQGNDAFLAAFLLGePEAVDLAELKQALRSELPEHMVPAHFAWVDGFALT 1959
Cdd:cd17645  355 RIEPGEIEPFLMNHPLIEL----AAVLAKEDADGRKYLVAYVTA-PEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLT 429

                        490
                 ....*....|
gi 15598523 1960 PSGKRDDAAL 1969
Cdd:cd17645  430 ANGKVDRKAL 439
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 1489-1973 1.20e-85

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: 288.91  E-value: 1.20e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDA-IGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI 1567
Cdd:cd17648    1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1568 LETAQPFRVVAHPEhahvaaaervlpveelvadiepetfaapqldELAMLLFTSGSTGRPKGVELSHRMWANytqwqLRV 1647
Cdd:cd17648   81 LEDTGARVVITNST-------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVN-----LRT 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1648 A-SGVPGLRT------LQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAea 1720
Cdd:cd17648  125 SlSERYFGRDngdeavLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYD-- 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1721 snaLGVRPgALRVVVSSGEQLriTEDV-RAFCAAMPGLLLeNQYGPTEThQVTYHSlSGDPAHYPDLPPIGRPLDGVEVQ 1799
Cdd:cd17648  203 ---LARLP-HLKRVDAAGEEF--TAPVfEKLRSRFAGLII-NAYGPTET-TVTNHK-RFFPGDQRFDKSLGRPVRNTKCY 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1800 VLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRP--------GARLYRTGDLGRILGNGEIVWLGRAD 1871
Cdd:cd17648  274 VLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRND 353

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1872 TQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGN-----DAFLAAFLLGEPEAVDLAELKQALRSELPEHMV 1946
Cdd:cd17648  354 FQVKIRGQRIEPGEVEAALA----SYPGVRECAVVAKEDASQaqsriQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMV 429

                        490       500
                 ....*....|....*....|....*..
gi 15598523 1947 PAHFAWVDGFALTPSGKRDdaaLRALP 1973
Cdd:cd17648  430 PARLVRLEGIPVTINGKLD---VRALP 453
AMP-binding pfam00501
AMP-binding enzyme;
1481-1877 4.64e-85

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 285.75  E-value: 4.64e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1481 FERQVEALPGSAALA-FEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1560 PAQRLALILETAQP--------FRVVAHPEHAHV--------------AAAERVLPVEELVADIEPETFAAPQLDELAML 1617
Cdd:pfam00501   81 PAEELAYILEDSGAkvlitddaLKLEELLEALGKlevvklvlvldrdpVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1618 LFTSGSTGRPKGVELSHR--MWANYTQWQLRVASGV--PGLRTLQFAPLSFDMAFQ-EIFSTLCGGGELQLISNRERMDP 1692
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRnlVANVLSIKRVRPRGFGlgPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1693 SALLHVLERRQVQrvLLPFV--ALQRLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLeNQYGPTETHQ 1770
Cdd:pfam00501  241 AALLELIERYKVT--VLYGVptLLNMLLEAGAPKRALLSSLRLVLSGGAPLPP-ELARRFRELFGGALV-NGYGLTETTG 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1771 VTYHSLSGDPaHYPDLPPIGRPLDGVEVQVLDAA-LRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarl 1849
Cdd:pfam00501  317 VVTTPLPLDE-DLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW------ 389

                          410       420
                   ....*....|....*....|....*...
gi 15598523   1850 YRTGDLGRILGNGEIVWLGRADTQVKVR 1877
Cdd:pfam00501  390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
453-939 2.03e-76

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 264.06  E-value: 2.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   453 EQVART-PQRTALLEAdGGTLSYAELDAKVQAVADALraAGVRTDERVALLVARG--PHLLPAILGVQRAGGAYVPINPD 529
Cdd:PRK04813    9 EEFAQTqPDFPAYDYL-GEKLTYGQLKEDSDALAAFI--DSLKLPDKSPIIVFGHmsPEMLATFLGAVKAGHAYIPVDVS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   530 HPLERVRLLLEDCGARVVLVderAATLGESLGETRVLHLERLPQSTGDLPAAN----VAPGDLAYVIYTSGSTGMPKGVM 605
Cdd:PRK04813   86 SPAERIEMIIEVAKPSLIIA---TEELPLEILGIPVITLDELKDIFATGNPYDfdhaVKGDDNYYIIFTSGTTGKPKGVQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   606 VEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVP 685
Cdd:PRK04813  163 ISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   686 SmltpFLD--LLDGDPTARAAASSLRLVFCsGEALaPLQVAR-FRRLFGDAvRLVNLYGPTEATVDVS----DHECASDN 758
Cdd:PRK04813  243 S----FADmcLLDPSFNEEHLPNLTHFLFC-GEEL-PHKTAKkLLERFPSA-TIYNTYGPTEATVAVTsieiTDEMLDQY 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   759 PtRVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLvdpFVAGGRLYRTGDLARwLADGN 838
Cdd:PRK04813  316 K-RLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAGY-LEDGL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   839 LEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAA-----ELDPG-QLRAGLSATLP 912
Cdd:PRK04813  391 LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEedferEFELTkAIKKELKERLM 470

                         490       500
                  ....*....|....*....|....*..
gi 15598523   913 DFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK04813  471 EYMIPRKFIYRDSLPLTPNGKIDRKAL 497
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 587-935 7.92e-75

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: 253.36  E-value: 7.92e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  587 DLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGaekDP 666
Cdd:cd04433    1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  667 REMLRSIQRDAVTVIHFVPSMLTpflDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEAT 746
Cdd:cd04433   78 EAALELIEREKVTILLGVPTLLA---RLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTETG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  747 VDVSdhECASDNPTRVP--IGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlvdpfvaGGRL 824
Cdd:cd04433  153 GTVA--TGPPDDDARKPgsVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGW 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  825 YRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDPGQ 902
Cdd:cd04433  224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRpgADLDAEE 303

                        330       340       350
                 ....*....|....*....|....*....|...
gi 15598523  903 LRAGLSATLPDFMLPAFFVRIDSLPLSANGKLD 935
Cdd:cd04433  304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 456-939 4.25e-73

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: 254.30  E-value: 4.25e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    456 ARTPQRTALLEAdGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERV 535
Cdd:TIGR01734   11 ETYPQTIAYRYQ-GQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    536 RLLLEDCGARVVLvdeRAATLGESLGETRVLHLERLPQS-TGDLP---AANVAPGDLAYVIYTSGSTGMPKGVMVEHRSV 611
Cdd:TIGR01734   90 EMIIEAAGPELVI---HTAELSIDAVGTQIITLSALEQAeTSGGPvsfDHAVKGDDNYYIIYTSGSTGNPKGVQISHDNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    612 VNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSmltpF 691
Cdd:TIGR01734  167 VSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPS----F 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    692 LD--LLDGDPTARAAASSLRLVFCsGEALAPLQVARFRRLFGDAvRLVNLYGPTEATVDVSD----HECASDNPtRVPIG 765
Cdd:TIGR01734  243 VDmcLLDPNFNQENYPHLTHFLFC-GEELPVKTAKALLERFPKA-TIYNTYGPTEATVAVTSvkitQEILDQYP-RLPIG 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    766 RPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLvdpFVAGGRLYRTGDLARwLADGNLEYLGRA 845
Cdd:TIGR01734  320 FAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLFYQGRL 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    846 DDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVAR---DSAVrgTHLVGYYVA-----AAELDPGQ-LRAGLSATLPDFML 916
Cdd:TIGR01734  396 DFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKynkDHKV--EYLIAAIVPetedfEKEFQLTKaIKKELKKSLPAYMI 473

                          490       500
                   ....*....|....*....|...
gi 15598523    917 PAFFVRIDSLPLSANGKLDRRQL 939
Cdd:TIGR01734  474 PRKFIYRDQLPLTANGKIDRKAL 496
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 447-939 4.49e-69

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: 241.31  E-value: 4.49e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  447 LPTLFAEQVARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPI 526
Cdd:cd05936    1 LADLLEEAARRFPDKTALIF-MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  527 NPDHPLERVRLLLEDCGARVVLVDERAATLGESlgetrvlhlerlPQSTGDLPAanVAPGDLAYVIYTSGSTGMPKGVMV 606
Cdd:cd05936   80 NPLYTPRELEHILNDSGAKALIVAVSFTDLLAA------------GAPLGERVA--LTPEDVAVLQYTSGTTGVPKGAML 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  607 EHRSVVNRLNWMQRRYP--IGERDVLLQKTPV--TFDVSV-WELFWwsFTGARLSLLPpgaEKDPREMLRSIQRDAVTVI 681
Cdd:cd05936  146 THRNLVANALQIKAWLEdlLEGDDVVLAALPLfhVFGLTVaLLLPL--ALGATIVLIP---RFRPIGVLKEIRKHRVTIF 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  682 HFVPSMLTPFLDLLDGdptARAAASSLRLVFCSGEALaPLQVA-RFRRLFGdaVRLVNLYGPTEATVDVsdHECASDNPT 760
Cdd:cd05936  221 PGVPTMYIALLNAPEF---KKRDFSSLRLCISGGAPL-PVEVAeRFEELTG--VPIVEGYGLTETSPVV--AVNPLDGPR 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  761 RV-PIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlVDpfvagGRLyRTGDLARWLADGNL 839
Cdd:cd05936  293 KPgSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VD-----GWL-RTGDIGYMDEDGYF 365

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  840 EYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDPGQLRAGLSATLPDFMLP 917
Cdd:cd05936  366 FIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKegASLTEEEIIAFCREQLAGYKVP 445

                        490       500
                 ....*....|....*....|..
gi 15598523  918 AFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05936  446 RQVEFRDELPKSAVGKILRREL 467
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 216-1017 1.14e-67

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: 253.45  E-value: 1.14e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    216 RTARHRL---TLERTL--LDAIRDRGESPFLFLSAAVALYLARIHQNDDVVLGVpvlnradRAAKQvvghfANTLPLRIR 290
Cdd:TIGR03443   20 RPANNRLveaTYSLQLpsAEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT-------SSNKS-----GRPFVLRLN 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    291 TAPEQTVDEFLAQLREATRTLLRHQKMPLGDL---LRGAS------PLFDTtlsymrwpAAQAIPNASVETVAQTHAHDp 361
Cdd:TIGR03443   88 ITPELSFLQLYAKVSEEEKEGASDIGVPFDELsehIQAAKklertpPLFRL--------AFQDAPDNQQTTYSTGSTTD- 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    362 daLAIWVSEfdGHSDAQVDFEYACDVFDADfPMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELIH-TRNATDQA 440
Cdd:TIGR03443  159 --LTVFLTP--SSPELELSIYYNSLLFSSD-RITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLPDpTKDLDWSG 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    441 FpeQATLPTLFAEQVARTPQRTALLEADGG--------TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPA 512
Cdd:TIGR03443  234 F--RGAIHDIFADNAEKHPDRTCVVETPSFldpssktrSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVA 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    513 ILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDERAATLGESLGE---------TRVLHLE----------RLPQ 573
Cdd:TIGR03443  312 VMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAGTLDQLVRDyidkelelrTEIPALAlqddgslvggSLEG 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    574 STGDLPAAN-----------VAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSV 642
Cdd:TIGR03443  392 GETDVLAPYqalkdtptgvvVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQ 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    643 WELFWWSFTGArlSLLPPGAEK--DPREMLRSIQRDAVTVIHFVPSMLtpflDLLDGDptARAAASSLRLVFCSGEALAP 720
Cdd:TIGR03443  472 RDMFTPLFLGA--QLLVPTADDigTPGRLAEWMAKYGATVTHLTPAMG----QLLSAQ--ATTPIPSLHHAFFVGDILTK 543

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    721 LQVARFRRLfGDAVRLVNLYGPTEATVDVSDHECAS--DNPTR-------VPIGRPIDNLRLYVLDRALRPQP--LGAVG 789
Cdd:TIGR03443  544 RDCLRLQTL-AENVCIVNMYGTTETQRAVSYFEIPSrsSDSTFlknlkdvMPAGKGMKNVQLLVVNRNDRTQTcgVGEVG 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    790 ELYIGGVGVARGYLNRPELNAERFLVDPFVAGG----------------------RLYRTGDLARWLADGNLEYLGRADD 847
Cdd:TIGR03443  623 EIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADD 702

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    848 QVKIRGNRVEPDEVRDRLAALPGVRD-AAVVARDSAVRGThLVGYYV----------------AAAELDP---------- 900
Cdd:TIGR03443  703 QVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEPT-LVSYIVpqdksdeleefksevdDEESSDPvvkglikyrk 781

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    901 --GQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPAP-PEQVAAVAPR----------TATEAELAAVWADVL 967
Cdd:TIGR03443  782 liKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdTAQLAAVAKNrsasaadeefTETEREIRDLWLELL 861

                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15598523    968 --GVAEVGVHDDFYALGGDSILMLRIrAAAQRRGLGFE--LADLMRNPTVAGLA 1017
Cdd:TIGR03443  862 pnRPATISPDDSFFDLGGHSILATRM-IFELRKKLNVElpLGLIFKSPTIKGFA 914
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 446-941 9.50e-67

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: 236.22  E-value: 9.50e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    446 TLPTLFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVP 525
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDR-TLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    526 INPDHPLERVRLLLEDCGARV-VLVDERAATLGESLGETRVLH-----------LERLP----------QSTGD-LPAAN 582
Cdd:TIGR03098   80 INPLLKAEQVAHILADCNVRLlVTSSERLDLLHPALPGCHDLRtliivgdpahaSEGHPgeepaswpklLALGDaDPPHP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    583 VAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLppgA 662
Cdd:TIGR03098  160 VIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH---D 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    663 EKDPREMLRSIQRDAVTVIHFVPsmltPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAvRLVNLYGP 742
Cdd:TIGR03098  237 YLLPRDVLKALEKHGITGLAAVP----PLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNA-RLFLMYGL 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    743 TEATVDVS-DHECASDNPTRvpIGRPIDNLRLYVL-DRALRPQPlGAVGELYIGGVGVARGYLNRPELNAERFL-VDPFV 819
Cdd:TIGR03098  312 TEAFRSTYlPPEEVDRRPDS--IGKAIPNAEVLVLrEDGSECAP-GEEGELVHRGALVAMGYWNDPEKTAERFRpLPPFP 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    820 AGGRLYRT----GDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAV--VARDSAVRGTHLVGYYV 893
Cdd:TIGR03098  389 GELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfgVPDPTLGQAIVLVVTPP 468

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 15598523    894 AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPA 941
Cdd:TIGR03098  469 GGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 1467-2346 1.20e-66

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: 244.61  E-value: 1.20e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1467 AASQPEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGIL 1546
Cdd:COG3319    1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1547 RAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQLDELAMLLFTSGSTGR 1626
Cdd:COG3319   81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1627 PKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQR 1706
Cdd:COG3319  161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1707 VLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLlenQYGPTETHQVTYHSLSGDPAHYPDL 1786
Cdd:COG3319  241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAG---GTATTAAVTTTAAAAAPGVAGALGP 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1787 PPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVW 1866
Cdd:COG3319  318 IGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLG 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1867 LGRADTQVKVRGFRIEPAEVELAimrqAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMV 1946
Cdd:COG3319  398 LGRLRLQRLRRGLREELEEAEAA----LAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLP 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1947 PAHFAWVDGFALTPSGKRDDAALRALPLEHGTniEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFM 2026
Cdd:COG3319  474 PALLLLLLLLLLLLLAALLLAAAAPAAAAAAA--AAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLL 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2027 LLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRAFDPLVPIRAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVY 2106
Cdd:COG3319  552 LLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVY 631

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2107 ALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALDpQAVAQLIVLDSITVDrnhA 2186
Cdd:COG3319  632 GLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQG-EEVALLVLLDSYAPG---A 707

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2187 GSASDEALLLFFYWELVWFERSDKEVEPLPEGASLEQKLDHIVERAIEAGvLPAGTPRATVQRLYELFRASWQALIGYRP 2266
Cdd:COG3319  708 LARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLERLREAG-LPAGLDAERLRRLLRVFRANLRALRRYRP 786

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2267 EVSDQDMTLLRADGPLPlalkpmhdaagTHYGDPKNGWQHWTSGRLDVIDVPGDHLVLMKEPYVETVAAEIAALLEPSTS 2346
Cdd:COG3319  787 RPYDGPVLLFRAEEDPP-----------GRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVAELAAALRAALAAAEA 855
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 440-939 3.21e-64

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 228.92  E-value: 3.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   440 AFPEQATLPTLFAEQVARTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRA 519
Cdd:PRK06187    1 MQDYPLTIGRILRHGARKHPDKEAV-YFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   520 GGAYVPINPDHPLERVRLLLEDCGARVVLVD-ERAATLGESLGET-------------------RVLHLER-LPQSTGDL 578
Cdd:PRK06187   80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDsEFVPLLAAILPQLptvrtvivegdgpaaplapEVGEYEElLAAASDTF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   579 PAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtFDVSVWelfWWS----FTGAR 654
Cdd:PRK06187  160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAW---GLPylalMAGAK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   655 LsLLPpgAEKDPREMLRSIQRDAVTVIHFVPSMLTpflDLLDgDPTARAAA-SSLRLVFCSGEALAPLQVARFRRLFGda 733
Cdd:PRK06187  236 Q-VIP--RRFDPENLLDLIETERVTFFFAVPTIWQ---MLLK-APRAYFVDfSSLRLVIYGGAALPPALLREFKEKFG-- 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   734 VRLVNLYGPTE----ATVDVSDHECASDNPTRVPIGRPIDNLRLYVLDRALRPQP--LGAVGELYIGGVGVARGYLNRPE 807
Cdd:PRK06187  307 IDLVQGYGMTEtspvVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPE 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   808 LNAERFlvdpfvAGGRLyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTH 887
Cdd:PRK06187  387 ATAETI------DGGWL-HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGER 459

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15598523   888 LVGYYVAA--AELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK06187  460 PVAVVVLKpgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 455-936 1.23e-61

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: 218.63  E-value: 1.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  455 VARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLER 534
Cdd:cd17631    5 ARRHPDRTALVF-GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  535 VRLLLEDCGARVVLvderaatlgeslgetrvlhlerlpqstgdlpaanvapGDLAYVIYTSGSTGMPKGVMVEHRSVV-N 613
Cdd:cd17631   84 VAYILADSGAKVLF-------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLwN 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  614 RLNWMQRrYPIGERDVLLQKTPVtFDVSVWELFWWS--FTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLTPf 691
Cdd:cd17631  127 AVNALAA-LDLGPDDVLLVVAPL-FHIGGLGVFTLPtlLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTMIQA- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  692 ldLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLfgdAVRLVNLYGPTEATVDVS-----DHEcasdnPTRVPIGR 766
Cdd:cd17631  201 --LLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR---GVKFVQGYGMTETSPGVTflspeDHR-----RKLGSAGR 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  767 PIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlvdpfvAGGrLYRTGDLARWLADGNLEYLGRAD 846
Cdd:cd17631  271 PVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF------RDG-WFHTGDLGRLDEDGYLYIVDRKK 343

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  847 DQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDPGQLRAGLSATLPDFMLPAFFVRID 924
Cdd:cd17631  344 DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRpgAELDEDELIAHCRERLARYKIPKSVEFVD 423

                        490
                 ....*....|..
gi 15598523  925 SLPLSANGKLDR 936
Cdd:cd17631  424 ALPRNATGKILK 435
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1613-1965 2.25e-61

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: 214.46  E-value: 2.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1613 ELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLisnRERMDP 1692
Cdd:cd04433    1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVL---LPKFDP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1693 SALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFcAAMPGLLLENQYGPTETHQVT 1772
Cdd:cd04433   78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPP-ELLERF-EEAPGIKLVNGYGLTETGGTV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1773 yhSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEhpwrpgaRLYRT 1852
Cdd:cd04433  156 --ATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GWYRT 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1853 GDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVAR--ERQGNDAFlAAFLLGEPEAVDL 1930
Cdd:cd04433  227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVL----LGHPGVAEAAVVGVpdPEWGERVV-AVVVLRPGADLDA 301

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 15598523 1931 AELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 1965
Cdd:cd04433  302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1049-1452 1.49e-60

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: 215.01  E-value: 1.49e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1049 AFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARSEPL 1128
Cdd:cd19536    1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1129 ILDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAFVR--EDGLDLVFSFHHAILDGWSVANLIVALVAAYRGEP-- 1204
Cdd:cd19536   81 ELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKdeRERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLey 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1205 ----LPgPAPALACHVREELAALASPAAVGYWTGLLEGARMTRLdgfgaHEPQAAQGPASHREA---LPDGLLERLKATA 1277
Cdd:cd19536  161 kplsLP-PAQPYRDFVAHERASIQQAASERYWREYLAGATLATL-----PALSEAVGGGPEQDSellVSVPLPVRSRSLA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1278 AQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPE-LPDADRMVGLFLNTVPVRSEIAGCSWIEVADALFRQERDG 1356
Cdd:cd19536  235 KRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEeTTGAERLLGLFLNTLPLRVTLSEETVEDLLKRAQEQELES 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1357 HAHRRYPLSAIQQIVGDE--LSSAFNYVNLHVLE--PLWQL------RDFRVWEETNFALLVNViATPSDGMYLRIDSDG 1426
Cdd:cd19536  315 LSHEQVPLADIQRCSEGEplFDSIVNFRHFDLDFglPEWGSdegmrrGLLFSEFKSNYDVNLSV-LPKQDRLELKLAYNS 393

                        410       420
                 ....*....|....*....|....*.
gi 15598523 1427 RGISRSQAALIGATFVELLWRLADHP 1452
Cdd:cd19536  394 QVLDEEQAQRLAAYYKSAIAELATAP 419
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 481-939 2.35e-60

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: 215.77  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  481 VQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGA----YVPINPDHPLERVRLLLEDCGARVVLVDERAAT- 555
Cdd:cd05922    3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADr 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  556 ----LGESLGETRVLHLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLL 631
Cdd:cd05922   83 lrdaLPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  632 QKTPVTFDVSVWELFWWSFTGARLSLLPPGAEkdPREMLRSIQRDAVTVIHFVPSmLTPFLDLLDGDPtarAAASSLRLV 711
Cdd:cd05922  163 TVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPS-TYAMLTRLGFDP---AKLPSLRYL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  712 FCSGEALAPLQVARFRRLFGDAvRLVNLYGPTEATVDVS--DHECASDNPTrvPIGRPIDNLRLYVLDRALRPQPLGAVG 789
Cdd:cd05922  237 TQAGGRLPQETIARLRELLPGA-QVYVMYGQTEATRRMTylPPERILEKPG--SIGLAIPGGEFEILDDDGTPTPPGEPG 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  790 ELYIGGVGVARGYLNRPElnaerFLVDPFVAGGRLYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALP 869
Cdd:cd05922  314 EIVHRGPNVMKGYWNDPP-----YRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523  870 GVRDAAVVA-RDSAVRGTHLVGyyVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05922  388 LIIEAAAVGlPDPLGEKLALFV--TAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 454-939 4.07e-59

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: 213.77  E-value: 4.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  454 QVARTPQRTALLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLE 533
Cdd:cd05959   12 NLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  534 RVRLLLEDCGARVVLVD-ERAATLGESLG-----------------ETRVLHLERL-PQSTGDLPAANVAPGDLAYVIYT 594
Cdd:cd05959   92 DYAYYLEDSRARVVVVSgELAPVLAAALTksehtlvvlivsggagpEAGALLLAELvAAEAEQLKPAATHADDPAFWLYS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  595 SGSTGMPKGVMVEHRSvvnrLNWMQRRYP-----IGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKdPREM 669
Cdd:cd05959  172 SGSTGRPKGVVHLHAD----IYWTAELYArnvlgIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PAAV 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  670 LRSIQRDAVTVIHFVPSMLTPFLDllDGDPTARaAASSLRLVFCSGEALaPLQVA-RFRRLFGdaVRLVNLYGPTEATvd 748
Cdd:cd05959  247 FKRIRRYRPTVFFGVPTLYAAMLA--APNLPSR-DLSSLRLCVSAGEAL-PAEVGeRWKARFG--LDILDGIGSTEML-- 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  749 vsdHECASDNPTRV---PIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLvdpfvagGRLY 825
Cdd:cd05959  319 ---HIFLSNRPGRVrygTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GEWT 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  826 RTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV-----AAAELDP 900
Cdd:cd05959  389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALE 468

                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 15598523  901 GQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05959  469 EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 1476-1969 1.33e-57

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: 209.23  E-value: 1.33e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1476 DVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL 1555
Cdd:TIGR01734    1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1556 DVSYPAQRLALILETAQP---FRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAP-QLDELAMLLFTSGSTGRPKGVE 1631
Cdd:TIGR01734   81 DTSIPSERIEMIIEAAGPelvIHTAELSIDAVGTQIITLSALEQAETSGGPVSFDHAvKGDDNYYIIYTSGSTGNPKGVQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1632 LSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQR-VLLP 1710
Cdd:TIGR01734  161 ISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVwVSTP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1711 -FVALQRLAEASNAlGVRPGALRVVVsSGEQLrITEDVRAFCAAMPGLLLENQYGPTE-THQVTYHSLSGDP-AHYPDLp 1787
Cdd:TIGR01734  241 sFVDMCLLDPNFNQ-ENYPHLTHFLF-CGEEL-PVKTAKALLERFPKATIYNTYGPTEaTVAVTSVKITQEIlDQYPRL- 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1788 PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpwrPGARLYRTGDLGRIlGNGEIVWL 1867
Cdd:TIGR01734  317 PIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH---EGQPAYRTGDAGTI-TDGQLFYQ 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1868 GRADTQVKVRGFRIEPAEVELAImRQAERqpgLRGAAVVAR-ERQGNDAFLAAFLLGEPEAVD-----LAELKQALRSEL 1941
Cdd:TIGR01734  393 GRLDFQIKLHGYRIELEDIEFNL-RQSSY---IESAVVVPKyNKDHKVEYLIAAIVPETEDFEkefqlTKAIKKELKKSL 468

                          490       500
                   ....*....|....*....|....*...
gi 15598523   1942 PEHMVPAHFAWVDGFALTPSGKRDDAAL 1969
Cdd:TIGR01734  469 PAYMIPRKFIYRDQLPLTANGKIDRKAL 496
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 473-940 1.96e-57

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: 205.99  E-value: 1.96e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  473 SYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDer 552
Cdd:cd05934    5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  553 aatlgeslgetrvlhlerlpqstgdlpaanvapgdLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQ 632
Cdd:cd05934   83 -----------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLT 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  633 KTP--------VTFDVSVWelfwwsfTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLTPfldLLDGDPTARAA 704
Cdd:cd05934  128 VLPlfhinaqaVSVLAALS-------VGATLVLLP---RFSASRFWSDVRRYGATVTNYLGAMLSY---LLAQPPSPDDR 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  705 ASSLRLVFCSgeALAPLQVARFRRLFGdaVRLVNLYGPTEATVDV-SDHecasDNPTRVP-IGRPIDNLRLYVLDRALRP 782
Cdd:cd05934  195 AHRLRAAYGA--PNPPELHEEFEERFG--VRLLEGYGMTETIVGViGPR----DEPRRPGsIGRPAPGYEVRIVDDDGQE 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  783 QPLGAVGELYIGGV---GVARGYLNRPELNAERFlvdpfvAGGrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPD 859
Cdd:cd05934  267 LPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM------RNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  860 EVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV--AAAELDPGQLRAGLSATLPDFMLPAfFVRI-DSLPLSANGKLDR 936
Cdd:cd05934  340 EVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVlrPGETLDPEELFAFCEGQLAYFKVPR-YIRFvDDLPKTPTEKVAK 418


                 ....
gi 15598523  937 RQLP 940
Cdd:cd05934  419 AQLR 422
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 1477-1970 7.59e-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: 205.87  E-value: 7.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1477 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 1556
Cdd:cd05936    1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1557 VSYPAQRLALILETAQpfrvvahpehahVAAAERVLPVEELVADIEPETF-AAPQLDELAMLLFTSGSTGRPKGVELSHR 1635
Cdd:cd05936   81 PLYTPRELEHILNDSG------------AKALIVAVSFTDLLAAGAPLGErVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1636 -MWANYTQWQLRVA-SGVPGLRTLQFAPL--SFDMAFQeIFSTLCGGGELQLISnreRMDPSALLHVLERRQVQrvLLP- 1710
Cdd:cd05936  149 nLVANALQIKAWLEdLLEGDDVVLAALPLfhVFGLTVA-LLLPLALGATIVLIP---RFRPIGVLKEIRKHRVT--IFPg 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1711 ----FVAlqrLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENqYGPTETHQVTyhslSGDPAHYPDL 1786
Cdd:cd05936  223 vptmYIA---LLNAPEFKKRDFSSLRLCISGGAPLPV-EVAERFEELTGVPIVEG-YGLTETSPVV----AVNPLDGPRK 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1787 P-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIV 1865
Cdd:cd05936  294 PgSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG-W------LRTGDIGYMDEDGYFF 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1866 WLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA--RERQGnDAFLAAFLLGEPEAVDLAELKQALRSELPE 1943
Cdd:cd05936  367 IVDRKKDMIIVGGFNVYPREVEEVLY----EHPAVAEAAVVGvpDPYSG-EAVKAFVVLKEGASLTEEEIIAFCREQLAG 441

                        490       500
                 ....*....|....*....|....*..
gi 15598523 1944 HMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd05936  442 YKVPRQVEFRDELPKSAVGKILRRELR 468
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 471-939 9.95e-57

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: 205.01  E-value: 9.95e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD 550
Cdd:cd17654   16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 ERAATLGESLGETRVlhlerlpqsTGDLPaanvAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVL 630
Cdd:cd17654   96 KELDNAPLSFTPEHR---------HFNIR----TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDIL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  631 LQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMLRSI-QRDAVTVIHFVPSMLTPFLDLLDGDpTARAAASSLR 709
Cdd:cd17654  163 FLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSQSIKS-TVLSATSSLR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  710 LVFCSGEALAPLQVARFRRLFGDAVRLVNLYGPTEATVDVSDHECASDNPTrVPIGRPIDNLRLYVLDRALRPQPlgavG 789
Cdd:cd17654  242 VLALGGEPFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSP-VQLGSPLLGTVIEVRDQNGSEGT----G 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  790 ELYIGgvGVARGYLNRPELNaerflvdpfVAGGRLYRTGDLARwLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALP 869
Cdd:cd17654  317 QVFLG--GLNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCL 384

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  870 GVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDfmlpaFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd17654  385 GVESCAVTLSDQQRLIAFIVGESSSSRIHKELQLTLLSSHAIPD-----TFVQIDKLPLTSHGKVDKSEL 449
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
455-939 1.26e-56

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 208.04  E-value: 1.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  455 VARTPQRTALL-EADGG---TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDH 530
Cdd:COG0365   19 AEGRGDKVALIwEGEDGeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  531 PLERVRLLLEDCGARVVLVD----------ERAATLGESLGET----RVLHLER----------------LPQSTGDLPA 580
Cdd:COG0365   99 GAEALADRIEDAEAKVLITAdgglrggkviDLKEKVDEALEELpsleHVIVVGRtgadvpmegdldwdelLAAASAEFEP 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  581 ANVAPGDLAYVIYTSGSTGMPKGVMVEHRSV-VNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFW--WSFtGARlSL 657
Cdd:COG0365  179 EPTDADDPLFILYTSGTTGKPKGVVHTHGGYlVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYgpLLN-GAT-VV 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  658 LPPGAEK--DPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDgDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVR 735
Cdd:COG0365  257 LYEGRPDfpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGD-EPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG--VP 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  736 LVNLYGPTEATvdvsdHECASDNPTRVP----IGRPIDNLRLYVLDRALRPQPLGAVGELYIGG--VGVARGYLNRPELN 809
Cdd:COG0365  334 IVDGWGQTETG-----GIFISNLPGLPVkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERY 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  810 AERFLvDPFvagGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLV 889
Cdd:COG0365  409 RETYF-GRF---PGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVK 484

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15598523  890 GYYVAAAELDPG-----QLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:COG0365  485 AFVVLKPGVEPSdelakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 459-942 2.70e-56

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: 205.83  E-value: 2.70e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALLEADGG------TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPL 532
Cdd:cd17647    2 PERTCVVETPSLnssktrSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  533 ERVRLLLEDCGARVVLVDERAATLgeslgetrvlhlerlpqstgdlpaanVAPGDLAYVIYTSGSTGMPKGVMVEHRSVV 612
Cdd:cd17647   82 ARQNIYLGVAKPRGLIVIRAAGVV--------------------------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLA 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  613 NRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGArlSLLPPGAEK--DPREMLRSIQRDAVTVIHFVPSMLtp 690
Cdd:cd17647  136 YYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGA--QLLVPTQDDigTPGRLAEWMAKYGATVTHLTPAMG-- 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  691 flDLLDGDptARAAASSLRLVFCSGEALAPLQVARFRRLfGDAVRLVNLYGPTEATVDVSDHECAS--DNPTR------- 761
Cdd:cd17647  212 --QLLTAQ--ATTPFPKLHHAFFVGDILTKRDCLRLQTL-AENVRIVNMYGTTETQRAVSYFEVPSrsSDPTFlknlkdv 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  762 VPIGRPIDNLRLYVLDRALRPQ--PLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGG----------------- 822
Cdd:cd17647  287 MPAGRGMLNVQLLVVNRNDRTQicGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfw 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  823 -----RLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVA--- 894
Cdd:cd17647  367 lgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPrfd 446

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523  895 -------AAELDPGQ-------------------LRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPAP 942
Cdd:cd17647  447 kpddesfAQEDVPKEvstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1476-1969 6.31e-55

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 201.28  E-value: 6.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1476 DVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL 1555
Cdd:PRK04813    3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1556 DVSYPAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPET---FAAP-QLDELAMLLFTSGSTGRPKGVE 1631
Cdd:PRK04813   83 DVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNpydFDHAvKGDDNYYIIFTSGTTGKPKGVQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1632 LSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQR-VLLP 1710
Cdd:PRK04813  163 ISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVwVSTP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1711 -FVALQRLAEASNAlgVRPGALRVVVSSGEQLRITEdVRAFCAAMPGLLLENQYGPTETH------QVTYHSLsgdpAHY 1783
Cdd:PRK04813  243 sFADMCLLDPSFNE--EHLPNLTHFLFCGEELPHKT-AKKLLERFPSATIYNTYGPTEATvavtsiEITDEML----DQY 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1784 PDLPpIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPwrpGARLYRTGDLGrILGNGE 1863
Cdd:PRK04813  316 KRLP-IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFD---GQPAYHTGDAG-YLEDGL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1864 IVWLGRADTQVKVRGFRIEPAEVElAIMRQaerQPGLRGAAVVARERQGN-DAFLAAFLLGEPEAVDLAELKQALRSEL- 1941
Cdd:PRK04813  391 LFYQGRIDFQIKLNGYRIELEEIE-QNLRQ---SSYVESAVVVPYNKDHKvQYLIAYVVPKEEDFEREFELTKAIKKELk 466

                         490       500       510
                  ....*....|....*....|....*....|.
gi 15598523  1942 ---PEHMVPAHFAWVDGFALTPSGKRDDAAL 1969
Cdd:PRK04813  467 erlMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 8-431 1.09e-54

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: 199.10  E-value: 1.09e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523      8 PLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLG-ETDGTPYQWLDTDAEFEARHV 86
Cdd:pfam00668    6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFELEII 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     87 DLR--ADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALL-HSDQALYVYVRTHHIVSDAWGLQLFLSRVRAGYLG-ELGE 162
Cdd:pfam00668   86 DISdlSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFrIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQlLKGE 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    163 --PQAQMPTASLLAQLETDdYSGSEQYRGDRAYFAEALEGLEP--ALFTRRRPAGLRRTARHRLT--LERTLLDAIRDRG 236
Cdd:pfam00668  166 plPLPPKTPYKDYAEWLQQ-YLQSEDYQKDAAYWLEQLEGELPvlQLPKDYARPADRSFKGDRLSftLDEDTEELLRKLA 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    237 ES-----PFLFLsAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTL 311
Cdd:pfam00668  245 KAhgttlNDVLL-AAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSA 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    312 LRHQKMPLGDLLR--------GASPLFDTTLSYMRWPAAQAIPNASVETVA----QTHAHD--PDALAIWVSEFDGhsDA 377
Cdd:pfam00668  324 EPHQGYPFGDLVNdlrlprdlSRHPLFDPMFSFQNYLGQDSQEEEFQLSELdlsvSSVIEEeaKYDLSLTASERGG--GL 401

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15598523    378 QVDFEYACDVFDADFpMDAAARHIETFLRALVEGGERRLGELDPLSAAEREELI 431
Cdd:pfam00668  402 TIKIDYNTSLFDEET-IERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1058-1452 1.69e-53

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: 194.73  E-value: 1.69e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1058 GLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARSEPLILDLRGNPE 1137
Cdd:cd19543   10 GMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWRELDLSHLSE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1138 AG--TVLDEHIRQRRFHRYSLQQPGLFLFAAF-VREDGLDLVFSFHHAILDGWSVANLIVALVAAYR----GEPLPGPAP 1210
Cdd:cd19543   90 AEqeAELEALAEEDRERGFDLARAPLMRLTLIrLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalgeGQPPSLPPV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1211 A--------LACHVREelaalaspAAVGYWTGLLEGAR-MTRLDGFGAHEPQAAQGPASHREALPDGLLERLKATAAQRG 1281
Cdd:cd19543  170 RpyrdyiawLQRQDKE--------AAEAYWREYLAGFEePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1282 LPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPVRSEI-AGCSWIEVADALFRQERDGHAH 1359
Cdd:cd19543  242 VTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPaELPGIETMVGLFINTLPVRVRLdPDQTVLELLKDLQAQQLELREH 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1360 RRYPLSAIQQIV--GDEL-SSAFNYVNLHVLEPL--------WQLRDFRVWEETNFALlvNVIATPSDGMYLRIDSDGRG 1428
Cdd:cd19543  322 EYVPLYEIQAWSegKQALfDHLLVFENYPVDESLeeeqdedgLRITDVSAEEQTNYPL--TVVAIPGEELTIKLSYDAEV 399

                        410       420
                 ....*....|....*....|....
gi 15598523 1429 ISRSQAALIGATFVELLWRLADHP 1452
Cdd:cd19543  400 FDEATIERLLGHLRRVLEQVAANP 423
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 442-939 1.00e-52

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 195.12  E-value: 1.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   442 PEQATLPTLFAEQVARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGG 521
Cdd:PRK07656    2 NEWMTLPELLARAARRFGDKEAYVF-GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   522 AYVPINPDHPLERVRLLLEDCGARVVLVderaatLGESLGETRVLHlERLPQ---------------------------- 573
Cdd:PRK07656   81 VVVPLNTRYTADEAAYILARGDAKALFV------LGLFLGVDYSAT-TRLPAlehvviceteeddphtekmktftdflaa 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   574 STGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtFDVSVWELFWWS--FT 651
Cdd:PRK07656  154 GDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPF-FHVFGYKAGVNAplMR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   652 GARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTaraAASSLRLvFCSGEALAPLQ-VARFRRLF 730
Cdd:PRK07656  233 GATILPLP---VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAE---DLSSLRL-AVTGAASMPVAlLERFESEL 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   731 GdaVRLV-NLYGPTEAtvdvSDHEC---ASDNPTRVP--IGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLN 804
Cdd:PRK07656  306 G--VDIVlTGYGLSEA----SGVTTfnrLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYD 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   805 RPELNAERFLVDpfvagGRLYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVR 884
Cdd:PRK07656  380 DPEATAAAIDAD-----GWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERL 453

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523   885 GTHLVGYYVA--AAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK07656  454 GEVGKAYVVLkpGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 463-934 2.48e-52

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: 193.20  E-value: 2.48e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  463 ALLEADGG-TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLED 541
Cdd:cd05911    1 AQIDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  542 CGARVVLVD----ERAATLGESLGETR-----------VLHLERLPQSTG-----DLPAA-NVAPGDLAYVIYTSGSTGM 600
Cdd:cd05911   81 SKPKVIFTDpdglEKVKEAAKELGPKDkiivlddkpdgVLSIEDLLSPTLgeedeDLPPPlKDGKDDTAAILYSSGTTGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  601 PKGVMVEHRSVVNRLN--WMQRRYPIGERDVLLqkTPVTFDVS--VWELFWWSFTGARLSLLPpgaEKDPREMLRSIQRD 676
Cdd:cd05911  161 PKGVCLSHRNLIANLSqvQTFLYGNDGSNDVIL--GFLPLYHIygLFTTLASLLNGATVIIMP---KFDSELFLDLIEKY 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  677 AVTVIHFVPSMLTPFLDlldgDPTARAA-ASSLRLVFCSGealAPLQ---VARFRRLFGDAvRLVNLYGPTEATVDVSDH 752
Cdd:cd05911  236 KITFLYLVPPIAAALAK----SPLLDKYdLSSLRVILSGG---APLSkelQELLAKRFPNA-TIKQGYGMTETGGILTVN 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  753 ECASDNPTRVpiGRPIDNLRLYVLDRALRP-QPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLA 831
Cdd:cd05911  308 PDGDDKPGSV--GRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIG 379

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  832 RWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRG-------------------------T 886
Cdd:cd05911  380 YFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGelprayvvrkpgekltekevkdyvaK 459

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 15598523  887 HLVGYYvaaaeldpgQLRAGlsatlpdfmlpAFFVriDSLPLSANGKL 934
Cdd:cd05911  460 KVASYK---------QLRGG-----------VVFV--DEIPKSASGKI 485
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 460-939 9.08e-52

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: 190.19  E-value: 9.08e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  460 QRTALlEADGGTLSYAELDAKVQAVADALRAAG-VRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:cd05941    1 DRIAI-VDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  539 LEDCGARVVLvderaatlgeslgetrvlhlerlpqstgdlpaanvapgDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWM 618
Cdd:cd05941   80 ITDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  619 QRRYPIGERDVLLQKTPV-----TFDVSVWELfwwsFTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLTPFL- 692
Cdd:cd05941  122 VDAWRWTEDDVLLHVLPLhhvhgLVNALLCPL----FAGASVEFLP---KFDPKEVAISRLMPSITVFMGVPTIYTRLLq 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  693 --DLLDGDPT--ARAAASSLRLvFCSGEALAPLQV-ARFRRLFGDavRLVNLYGPTEATVDVSdhecasdNP---TRVP- 763
Cdd:cd05941  195 yyEAHFTDPQfaRAAAAERLRL-MVSGSAALPVPTlEEWEAITGH--TLLERYGMTEIGMALS-------NPldgERRPg 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  764 -IGRPIDNLRLYVLDR-ALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLADGNLEY 841
Cdd:cd05941  265 tVGMPLPGVQARIVDEeTGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWI 338

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  842 LGR-ADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAE---LDPGQLRAGLSATLPDFMLP 917
Cdd:cd05941  339 LGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaaaLSLEELKEWAKQRLAPYKRP 418

                        490       500
                 ....*....|....*....|..
gi 15598523  918 AFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05941  419 RRLILVDELPRNAMGKVNKKEL 440
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 443-943 1.18e-51

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 192.12  E-value: 1.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   443 EQATLPTLFAEQVARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGA 522
Cdd:PRK06188   10 SGATYGHLLVSALKRYPDRPALVL-GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   523 YVPINPDHPLERVRLLLEDCGARVVLVD-----ERAATLGESL-GETRVLHLERLPQSTGDLPAANV----------APG 586
Cdd:PRK06188   89 RTALHPLGSLDDHAYVLEDAGISTLIVDpapfvERALALLARVpSLKHVLTLGPVPDGVDLLAAAAKfgpaplvaaaLPP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   587 DLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTP------VTFDVSVWElfwwsftGARLSLLPp 660
Cdd:PRK06188  169 DIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPlshaggAFFLPTLLR-------GGTVIVLA- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   661 gaEKDPREMLRSIQRDAVTVIHFVPSMLtpfLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAvrLVNLY 740
Cdd:PRK06188  241 --KFDPAEVLRAIEEQRITATFLVPTMI---YALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPI--FAQYY 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   741 GPTEATVDVS-----DHeCASDNPTRVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlv 815
Cdd:PRK06188  314 GQTEAPMVITylrkrDH-DPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-- 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   816 dpfvAGGRLyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV-- 893
Cdd:PRK06188  391 ----RDGWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVlr 465

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 15598523   894 AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPAPP 943
Cdd:PRK06188  466 PGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARY 515
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 465-939 1.37e-51

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: 190.99  E-value: 1.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  465 LEADGGT--LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDC 542
Cdd:cd05926    6 LVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  543 GARVVLVD-ERAATLGESLGETRVLHLE---------------RLPQSTGDLPAA----NVAPGDLAYVIYTSGSTGMPK 602
Cdd:cd05926   86 GSKLVLTPkGELGPASRAASKLGLAILElaldvgvlirapsaeSLSNLLADKKNAksegVPLPDDLALILHTSGTTGRPK 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  603 GVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtFDVS--VWELFWWSFTGARLsLLPPGAekDPREMLRSIQRDAVTV 680
Cdd:cd05926  166 GVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSV-VLPPRF--SASTFWPDVRDYNATW 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  681 IHFVPSMLTPFLDllDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATvdvsdHECASDN-P 759
Cdd:cd05926  242 YTAVPTIHQILLN--RPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG--APVLEAYGMTEAA-----HQMTSNPlP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  760 TRVP----IGRPiDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLA 835
Cdd:cd05926  313 PGPRkpgsVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLDA 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  836 DGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV--AAAELDPGQLRAGLSATLPD 913
Cdd:cd05926  386 DGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlrEGASVTEEELRAFCRKHLAA 465

                        490       500
                 ....*....|....*....|....*.
gi 15598523  914 FMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05926  466 FKVPKKVYFVDELPKTATGKIQRRKV 491
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 443-941 2.25e-48

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 183.20  E-value: 2.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   443 EQATLPTLFAEqvaRTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGA 522
Cdd:PRK07788   50 PFAGLVAHAAR---RAPDRAALID-ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGAR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   523 YVPINPDHPLERVRLLLEDCGARVVLVDE----RAATLGESLGETRVL--HLERLPQSTGDLP-----AANVAPGDL--- 588
Cdd:PRK07788  126 IILLNTGFSGPQLAEVAAREGVKALVYDDeftdLLSALPPDLGRLRAWggNPDDDEPSGSTDEtlddlIAGSSTAPLpkp 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   589 ----AYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPV--TFDVSVWELFWwsFTGARLSLlppgA 662
Cdd:PRK07788  206 pkpgGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAM--ALGSTVVL----R 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   663 EK-DPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDgDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDavRLVNLYG 741
Cdd:PRK07788  280 RRfDPEATLEDIAKHKATALVVVPVMLSRILDLGP-EVLAKYDTSSLKIIFVSGSALSPELATRALEAFGP--VLYNLYG 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   742 PTE-ATVDVSDHECASDNPTRVpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPelnaerflvDPFVA 820
Cdd:PRK07788  357 STEvAFATIATPEDLAEAPGTV--GRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR---------DKQII 425

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   821 GGrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AEL 898
Cdd:PRK07788  426 DG-LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKApgAAL 504

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 15598523   899 DPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPA 941
Cdd:PRK07788  505 DEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 461-939 4.47e-48

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: 179.19  E-value: 4.47e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  461 RTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLE 540
Cdd:cd05919    1 KTAFYAADR-SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  541 DCGARVVLVDEraatlgeslgetrvlhlerlpqstgdlpaanvapGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQR 620
Cdd:cd05919   80 DCEARLVVTSA----------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  621 RY-PIGERDVLLQKTPVTFDVSVWELFWWS-FTGARLSLLPpgAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGD 698
Cdd:cd05919  126 EAlGLTPGDRVFSSAKMFFGYGLGNSLWFPlAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  699 PtarAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATvdvsdHECASDNPTRVPI---GRPIDNLRLYV 775
Cdd:cd05919  204 P---DALRSLRLCVSAGEALPRGLGERWMEHFG--GPILDGIGATEVG-----HIFLSNRPGAWRLgstGRPVPGYEIRL 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  776 LDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLvdpfvagGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNR 855
Cdd:cd05919  274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  856 VEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQ-----LRAGLSATLPDFMLPAFFVRIDSLPLSA 930
Cdd:cd05919  347 VSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslardIHRHLLERLSAHKVPRRIAFVDELPRTA 426


                 ....*....
gi 15598523  931 NGKLDRRQL 939
Cdd:cd05919  427 TGKLQRFKL 435
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 446-939 1.30e-47

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: 180.34  E-value: 1.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  446 TLPTLFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGayVP 525
Cdd:COG1021   26 TLGDLLRRRAERHPDRIAVVDGER-RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  526 IN--PDHPLERVRLLLEDCGARVVLVDERAA-----TLGESL-------------GETRVLH-LERLPQSTGDLPAANVA 584
Cdd:COG1021  103 VFalPAHRRAEISHFAEQSEAVAYIIPDRHRgfdyrALARELqaevpslrhvlvvGDAGEFTsLDALLAAPADLSEPRPD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  585 PGDLAYVIYTSGSTGMPKGV---------MVEHRSVVNRLNwmqrrypigERDVLLQKTPV--TFDVSVWELFWWSFTGA 653
Cdd:COG1021  183 PDDVAFFQLSGGTTGLPKLIprthddylySVRASAEICGLD---------ADTVYLAALPAahNFPLSSPGVLGVLYAGG 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  654 RLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLtpfLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGda 733
Cdd:COG1021  254 TVVLAP---DPSPDTAFPLIERERVTVTALVPPLA---LLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG-- 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  734 VRLVNLYGPTEATVDVSDHecasDNPTRVPI---GRPI---DNLRlyVLDRALRPQPLGAVGELYIGGVGVARGYLNRPE 807
Cdd:COG1021  326 CTLQQVFGMAEGLVNYTRL----DDPEEVILttqGRPIspdDEVR--IVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  808 LNAERFLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVkIR-GNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGT 886
Cdd:COG1021  400 HNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGE 472

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15598523  887 HLVGYYVAA-AELDPGQLRAGLSAT-LPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:COG1021  473 RSCAFVVPRgEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 472-939 9.93e-47

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: 174.83  E-value: 9.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDE 551
Cdd:cd05972    1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  552 RaatlgeslgetrvlhlerlpqstgdlpaanvapgDLAYVIYTSGSTGMPKGVMVEHRSVVNrlNWMQRRYPIGerdvlL 631
Cdd:cd05972   81 E----------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLG--HIPTAAYWLG-----L 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  632 QKTPVTFDVSV--WELF-WWSFTGARLSLLP----PGAEKDPREMLRSIQRDAVTVIHFVPS---MLTPfLDLLDGDPta 701
Cdd:cd05972  120 RPDDIHWNIADpgWAKGaWSSFFGPWLLGATvfvyEGPRFDAERILELLERYGVTSFCGPPTayrMLIK-QDLSSYKF-- 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  702 raaaSSLRLVFCSGEALAPLQVARFRRLFGDAVRlvNLYGPTEATVDVSDHECASDNPTRvpIGRPIDNLRLYVLDRALR 781
Cdd:cd05972  197 ----SHLRLVVSAGEPLNPEVIEWWRAATGLPIR--DGYGQTETGLTVGNFPDMPVKPGS--MGRPTPGYDVAIIDDDGR 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  782 PQPLGAVGELYI--GGVGVARGYLNRPELNAERFlvdpfvaGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPD 859
Cdd:cd05972  269 ELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASI-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPF 341

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  860 EVRDRLAALPGVRDAAVVARDSAVRGtHLVGYYV--AAAELDPGQLRAGLSATLPDFMLPAFFVRI----DSLPLSANGK 933
Cdd:cd05972  342 EVESALLEHPAVAEAAVVGSPDPVRG-EVVKAFVvlTSGYEPSEELAEELQGHVKKVLAPYKYPREiefvEELPKTISGK 420


                 ....*.
gi 15598523  934 LDRRQL 939
Cdd:cd05972  421 IRRVEL 426
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1480-1971 3.16e-46

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 176.15  E-value: 3.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1480 LFERQVEALPGSAALAFEEQRWTYRDLD-HVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVS 1558
Cdd:PRK06187   11 ILRHGARKHPDKEAVYFDGRRTTYAELDeRVNR-LANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1559 YPAQRLALILETAQPFRVVAHPEHAHVAAA-----------------------ERVLPVEELVADiEPETFAAPQLDE-- 1613
Cdd:PRK06187   90 LKPEEIAYILNDAEDRVVLVDSEFVPLLAAilpqlptvrtvivegdgpaaplaPEVGEYEELLAA-ASDTFDFPDIDEnd 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1614 LAMLLFTSGSTGRPKGVELSHR-MWANytqwqLRVASGVPGLRT----LQFAPLSFDMAFQEIFSTLCGGGELQLIsnrE 1688
Cdd:PRK06187  169 AAAMLYTSGTTGHPKGVVLSHRnLFLH-----SLAVCAWLKLSRddvyLVIVPMFHVHAWGLPYLALMAGAKQVIP---R 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1689 RMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGeqlritedvrafcAAMPGLLLEN------- 1761
Cdd:PRK06187  241 RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGG-------------AALPPALLREfkekfgi 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1762 ----QYGPTETHQVTyhSLSGDPAHYPDLPPI----GRPLDGVEVQVLDAALRPVPV--GVTGELYFGGDCLARGYHRAP 1831
Cdd:PRK06187  308 dlvqGYGMTETSPVV--SVLPPEDQLPGQWTKrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRP 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1832 KLTAERFVeHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--E 1909
Cdd:PRK06187  386 EATAETID-GGW------LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALY----GHPAVAEVAVIGVpdE 454

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598523  1910 RQGnDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 1971
Cdd:PRK06187  455 KWG-ERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 446-939 3.88e-46

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: 175.00  E-value: 3.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  446 TLPTLFAEQVARTPQRTALLEADGGT-LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYV 524
Cdd:cd05923    2 TVFEMLRRAASRAPDACAIADPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  525 PINPD-HPLERVRLLLEDCGARVVLVDERAATLGESLGETRVLHLE-----RLPQSTGDLPAANVA-PGDLAYVIYTSGS 597
Cdd:cd05923   82 LINPRlKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSdlvglGEPESAGPLIEDPPRePEQPAFVFYTSGT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  598 TGMPKGVMVEHRSVVNRLNWM--QRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPpgAEKDPREMLRSIQR 675
Cdd:cd05923  162 TGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVV--EEFDPADALKLIEQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  676 DAVTVIHFVPsmlTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFgdAVRLVNLYGPTEATVDVSDHeca 755
Cdd:cd05923  240 ERVTSLFATP---THLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHL--PGEKVNIYGTTEAMNSLYMR--- 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  756 sdNPTRVPIGRPIDNLRLYVLDRALRPQ---PLGAVGELYIGGVGVA--RGYLNRPELNAERfLVDpfvaggRLYRTGDL 830
Cdd:cd05923  312 --DARTGTEMRPGFFSEVRIVRIGGSPDealANGEEGELIVAAAADAafTGYLNQPEATAKK-LQD------GWYRTGDV 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  831 ARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVA------AAELDpgqlR 904
Cdd:cd05923  383 GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPregtlsADELD----Q 458

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15598523  905 AGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05923  459 FCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1498-1970 1.07e-45

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: 171.71  E-value: 1.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1498 EQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVV 1577
Cdd:cd05934    1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1578 AHPehahvaaaervlpveelvadiepetfaapqldelAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTL 1657
Cdd:cd05934   81 VDP----------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1658 QFAPLsFDMAFQE--IFSTLCGGGELQLisnRERMDPSALLHVLERRQVQR-----VLLPFVALQRLAEASNALGVRPGA 1730
Cdd:cd05934  127 TVLPL-FHINAQAvsVLAALSVGATLVL---LPRFSASRFWSDVRRYGATVtnylgAMLSYLLAQPPSPDDRAHRLRAAY 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1731 LRVVVSsgeqlritEDVRAFCAAMpGLLLENQYGPTETHqvtyHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPV 1810
Cdd:cd05934  203 GAPNPP--------ELHEEFEERF-GVRLLEGYGMTETI----VGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPA 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1811 GVTGELY---FGGDCLARGYHRAPKLTAERFvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 1887
Cdd:cd05934  270 GEPGELVirgLRGWGFFKGYYNMPEATAEAM-RNGW------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1888 LAIMrqaeRQPGLRGAAVVA-RERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDD 1966
Cdd:cd05934  343 RAIL----RHPAVREAAVVAvPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAK 418


                 ....
gi 15598523 1967 AALR 1970
Cdd:cd05934  419 AQLR 422
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 473-939 2.10e-45

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: 173.59  E-value: 2.10e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  473 SYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDER 552
Cdd:cd12119   27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  553 AATLGESLGE--TRVLHLERLPQSTGDLPAAnvAPGDLAY-----------------------VIYTSGSTGMPKGVMVE 607
Cdd:cd12119  107 FLPLLEAIAPrlPTVEHVVVMTDDAAMPEPA--GVGVLAYeellaaespeydwpdfdentaaaICYTSGTTGNPKGVVYS 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  608 HRSVVnrLNWMQRRYP----IGERDVLLQKTPVtFDVSVWEL-FWWSFTGARLSLlpPGAEKDPREMLRSIQRDAVTVIH 682
Cdd:cd12119  185 HRSLV--LHAMAALLTdglgLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIEREGVTFAA 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  683 FVPSMLTPFLDLLDGDPTARaaaSSLRLVFCSGEALAPLQVARFRRLFgdaVRLVNLYGPTE----ATVDVSDHECASDN 758
Cdd:cd12119  260 GVPTVWQGLLDHLEANGRDL---SSLRRVVIGGSAVPRSLIEAFEERG---VRVIHAWGMTEtsplGTVARPPSEHSNLS 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  759 P-----TRVPIGRPIDNLRLYVLDRALRPQPL--GAVGELYIGGVGVARGYLNRPElNAERFLVDPFvaggrlYRTGDLA 831
Cdd:cd12119  334 EdeqlaLRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGW------LRTGDVA 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  832 RWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDPGQLRAGLSA 909
Cdd:cd12119  407 TIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKegATVTAEELLEFLAD 486

                        490       500       510
                 ....*....|....*....|....*....|
gi 15598523  910 TLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd12119  487 KVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 473-939 4.36e-45

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: 170.69  E-value: 4.36e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  473 SYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDEr 552
Cdd:cd05971    8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  553 aatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQ 632
Cdd:cd05971   87 --------------------------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLY 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  633 KTPVTfdvsvwelfwWSFTGARLSLLPPG-----------AEK-DPREMLRSIQRDAVTVIHFVPSMLTPFLDllDGDPT 700
Cdd:cd05971  135 WTPAD----------WAWIGGLLDVLLPSlyfgvpvlahrMTKfDPKAALDLMSRYGVTTAFLPPTALKMMRQ--QGEQL 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  701 ARAAASsLRLVFCSGEALAPLQVARFRRLFGDAVRlvNLYGPTEATVDVSDheCASDNPTR-VPIGRPIDNLRLYVLDRA 779
Cdd:cd05971  203 KHAQVK-LRAIATGGESLGEELLGWAREQFGVEVN--EFYGQTECNLVIGN--CSALFPIKpGSMGKPIPGHRVAIVDDN 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  780 LRPQPLGAVGElyiggVGVAR-------GYLNRPELNAERFlvdpfvAGGRLyRTGDLARWLADGNLEYLGRADDQVKIR 852
Cdd:cd05971  278 GTPLPPGEVGE-----IAVELpdpvaflGYWNNPSATEKKM------AGDWL-LTGDLGRKDSDGYFWYVGRDDDVITSS 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  853 GNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQ-----LRAGLSATLPDFMLPAFFVRIDSLP 927
Cdd:cd05971  346 GYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalareIQELVKTRLAAHEYPREIEFVNELP 425

                        490
                 ....*....|..
gi 15598523  928 LSANGKLDRRQL 939
Cdd:cd05971  426 RTATGKIRRREL 437
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 444-937 5.78e-45

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 172.38  E-value: 5.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   444 QATLPTLFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAY 523
Cdd:PRK07798    2 AWNIADLFEAVADAVPDRVALVCGDR-RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   524 VPINPDHPLERVRLLLEDCGARVVLVDER-AATLGESLGETRVLHL--------------------ERLPQSTGDLPAAN 582
Cdd:PRK07798   81 VNVNYRYVEDELRYLLDDSDAVALVYEREfAPRVAEVLPRLPKLRTlvvvedgsgndllpgavdyeDALAAGSPERDFGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   583 VAPGDLaYVIYTSGSTGMPKGVMVEH----RSVVNRLNWMQRRYPIGERDVLLQKT----PVTFDVS-------VWELFW 647
Cdd:PRK07798  161 RSPDDL-YLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDEEELAKRAAagpgMRRFPAPplmhgagQWAAFA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   648 WSFTGARLsLLPPGAEKDPREMLRSIQRDAVTVIHFV-PSMLTPFLDLLdgDPTARAAASSLRLVFCSGEALAPLQVARF 726
Cdd:PRK07798  240 ALFSGQTV-VLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDAL--EARGPYDLSSLFAIASGGALFSPSVKEAL 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   727 RRLFGDAVrLVNLYGPTEA----TVDVSDHECASDNPtRVPIGRpidnlRLYVLDRALRPQPLG--AVGELYIGGVgVAR 800
Cdd:PRK07798  317 LELLPNVV-LTDSIGSSETgfggSGTVAKGAVHTGGP-RFTIGP-----RTVVLDEDGNPVEPGsgEIGWIARRGH-IPL 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   801 GYLNRPELNAERFlvdPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARD 880
Cdd:PRK07798  389 GYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVP 465

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523   881 SAVRGTHLVGYYVAA--AELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRR 937
Cdd:PRK07798  466 DERWGQEVVAVVQLRegARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 1481-1963 1.68e-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: 168.56  E-value: 1.68e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1481 FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDvsyp 1560
Cdd:cd17631    1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1561 aQRLaliletaqpfrvvahpehahvAAAErvlpVEELVADIEPETFaapqLDELAMLLFTSGSTGRPKGVELSHRMWANY 1640
Cdd:cd17631   77 -FRL---------------------TPPE----VAYILADSGAKVL----FDDLALLMYTSGTTGRPKGAMLTHRNLLWN 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1641 TQWQLRVASGVPGLRTLQFAPLS-FDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQRLAE 1719
Cdd:cd17631  127 AVNALAALDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFLVPTMIQALLQ 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1720 ASNALGVRPGALRVVVSSGEQLRitEDVRAFCAAMpGLLLENQYGPTETHQVTYHSLSGDpaHYPDLPPIGRPLDGVEVQ 1799
Cdd:cd17631  204 HPRFATTDLSSLRAVIYGGAPMP--ERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPED--HRRKLGSAGRPVFFVEVR 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1800 VLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGF 1879
Cdd:cd17631  279 IVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGW------FHTGDLGRLDEDGYLYIVDRKKDMIISGGE 351

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1880 RIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGnDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFA 1957
Cdd:cd17631  352 NVYPAEVEDVLY----EHPAVAEVAVIGVpdEKWG-EAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALP 426


                 ....*.
gi 15598523 1958 LTPSGK 1963
Cdd:cd17631  427 RNATGK 432
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 442-938 3.51e-44

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 170.95  E-value: 3.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   442 PEQATLPTLFAEQVARTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGG 521
Cdd:PRK05605   29 YGDTTLVDLYDNAVARFGDRPAL-DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   522 AYVPINPDHPLERVRLLLEDCGARVVLVDERAATLGESLGETRVLH-----------------LERLP---------QST 575
Cdd:PRK05605  108 VVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLEtivsvnmiaampllqrlALRLPipalrkaraALT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   576 GDLPAA---------------------NVAPGDLAYVIYTSGSTGMPKGVMVEHRSVvnRLNWMQRRY---PIGERD-VL 630
Cdd:PRK05605  188 GPAPGTvpwetlvdaaiggdgsdvshpRPTPDDVALILYTSGTTGKPKGAQLTHRNL--FANAAQGKAwvpGLGDGPeRV 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   631 LQKTP----------VTFDVSVwelfwwsftGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLtpfldlldgDPT 700
Cdd:PRK05605  266 LAALPmfhaygltlcLTLAVSI---------GGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLY---------EKI 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   701 ARAAA------SSLRLVFCSGEALAPLQVARFRRLFGDavRLVNLYGPTEATVDVSdheCASDNPTRVP--IGRPIDNLR 772
Cdd:PRK05605  325 AEAAEergvdlSGVRNAFSGAMALPVSTVELWEKLTGG--LLVEGYGLTETSPIIV---GNPMSDDRRPgyVGVPFPDTE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   773 LYVLDR--ALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDpfvaggrLYRTGDLARWLADGNLEYLGRADDQVK 850
Cdd:PRK05605  400 VRIVDPedPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELII 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   851 IRGNRVEPDEVRDRLAALPGVRDAAVVARDSAvRGTHLVgyyVAA------AELDPGQLRAGLSATLPDFMLPAFFVRID 924
Cdd:PRK05605  473 TGGFNVYPAEVEEVLREHPGVEDAAVVGLPRE-DGSEEV---VAAvvlepgAALDPEGLRAYCREHLTRYKVPRRFYHVD 548

                         570
                  ....*....|....
gi 15598523   925 SLPLSANGKLDRRQ 938
Cdd:PRK05605  549 ELPRDQLGKVRRRE 562
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 1497-1963 2.14e-43

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: 166.62  E-value: 2.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1497 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRV 1576
Cdd:cd05911    7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1577 VAHPEHAHV--AAAERVLPVEELV------------------ADIEPETFAAPQL----DELAMLLFTSGSTGRPKGVEL 1632
Cdd:cd05911   87 FTDPDGLEKvkEAAKELGPKDKIIvlddkpdgvlsiedllspTLGEEDEDLPPPLkdgkDDTAAILYSSGTTGLPKGVCL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1633 SHRmwaNYTQWQLRVASGVPGL---RTLQFAPLSFDMAFQeIFSTLCGG--GELQLISNreRMDPSALLHVLERRQVQRV 1707
Cdd:cd05911  167 SHR---NLIANLSQVQTFLYGNdgsNDVILGFLPLYHIYG-LFTTLASLlnGATVIIMP--KFDSELFLDLIEKYKITFL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1708 LLPFVALQRLAEASNALGVRPGALRVVVSSGEqlRITEDVRAFCAAMPGLLLENQ-YGPTETHQVTYHSlsgdPAHYPDL 1786
Cdd:cd05911  241 YLVPPIAAALAKSPLLDKYDLSSLRVILSGGA--PLSKELQELLAKRFPNATIKQgYGMTETGGILTVN----PDGDDKP 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1787 PPIGRPLDGVEVQVLDAALRP-VPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIV 1865
Cdd:cd05911  315 GSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLY 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1866 WLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDAflAAFLLGEPEAVDLAElkqalrsELPE 1943
Cdd:cd05911  389 IVDRKKELIKYKGFQVAPAELEAVLL----EHPGVADAAVigIPDEVSGELP--RAYVVRKPGEKLTEK-------EVKD 455

                        490       500
                 ....*....|....*....|....*....
gi 15598523 1944 HM---VPAHFAW------VDGFALTPSGK 1963
Cdd:cd05911  456 YVakkVASYKQLrggvvfVDEIPKSASGK 484
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
442-877 2.66e-43

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 169.13  E-value: 2.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  442 PEQATLPTLFAEQVARTPQRTALLEADGG---TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQR 518
Cdd:COG1022    8 PPADTLPDLLRRRAARFPDRVALREKEDGiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  519 AGGAYVPINPDHPLERVRLLLEDCGARVVLV--DERAATL------------------GESLGETRVLHLERL------- 571
Cdd:COG1022   88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVedQEQLDKLlevrdelpslrhivvldpRGLRDDPRLLSLDELlalgrev 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  572 -PQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLqktpvtfdvsvweLF---W 647
Cdd:COG1022  168 aDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-------------SFlplA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  648 WSF----------TGARLSLLPpgaekDPREMLRSIQRDAVTVIHFVP----SMLT------------------------ 689
Cdd:COG1022  235 HVFertvsyyalaAGATVAFAE-----SPDTLAEDLREVKPTFMLAVPrvweKVYAgiqakaeeagglkrklfrwalavg 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  690 --PFLDLLDGDPTARAAASSL----RLVF---------------CSGEALAPlQVARFRRLFGdaVRLVNLYGPTEATVD 748
Cdd:COG1022  310 rrYARARLAGKSPSLLLRLKHaladKLVFsklrealggrlrfavSGGAALGP-ELARFFRALG--IPVLEGYGLTETSPV 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  749 VSDHEcasdnPTRVPI---GRPIDNLRLyvldRalrpqpLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlY 825
Cdd:COG1022  387 ITVNR-----PGDNRIgtvGPPLPGVEV----K------IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------L 445

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15598523  826 RTGDLARWLADGNLEYLGRADDQVKIR-GNRVEPDEVRDRLAALPGVRDAAVV 877
Cdd:COG1022  446 HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1480-1972 5.34e-43

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 167.21  E-value: 5.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1480 LFERQVEALPGSAALAFE-----EQRWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCV 1553
Cdd:COG0365   14 CLDRHAEGRGDKVALIWEgedgeERTLTYAELrREVNR-FANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1554 PLDVSYPAQRLALILETAQPfRVV-----------AHPEHAHVAAA-------ERVLPV---------------EELVAD 1600
Cdd:COG0365   93 PVFPGFGAEALADRIEDAEA-KVLitadgglrggkVIDLKEKVDEAleelpslEHVIVVgrtgadvpmegdldwDELLAA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1601 iEPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR---MWANYT-QWQLRVASG-----------VPGLRTLQFAPLS 1663
Cdd:COG0365  172 -ASAEFEPEPTdaDDPLFILYTSGTTGKPKGVVHTHGgylVHAATTaKYVLDLKPGdvfwctadigwATGHSYIVYGPLL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1664 FDMAfqeifSTLCGGgelqlisNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPG--ALRVVVSSGEql 1741
Cdd:COG0365  251 NGAT-----VVLYEG-------RPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDlsSLRLLGSAGE-- 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1742 RITEDVRAFCAAMPGLLLENQYGPTET-HQVTyhslsgdpAHYPDLPP----IGRPLDGVEVQVLDAALRPVPVGVTGEL 1816
Cdd:COG0365  317 PLNPEVWEWWYEAVGVPIVDGWGQTETgGIFI--------SNLPGLPVkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGEL 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1817 YFGGDC--LARGYHRAPKLTAERFVEHPwrPGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQ- 1893
Cdd:COG0365  389 VIKGPWpgMFRGYWNDPERYRETYFGRF--PG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHp 464

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1894 --AErqpglrgAAVVARERQGNDAFLAAFLL---GEPEAVDLA-ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDA 1967
Cdd:COG0365  465 avAE-------AAVVGVPDEIRGQVVKAFVVlkpGVEPSDELAkELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRR 537


                 ....*
gi 15598523 1968 ALRAL 1972
Cdd:COG0365  538 LLRKI 542
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 441-939 5.35e-43

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: 165.87  E-value: 5.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  441 FPEQATLPTLFAEQVARTPQRTALLEADGG-TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRA 519
Cdd:cd05904    1 LPTDLPLDSVSFLFASAHPSRPALIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  520 GGAYVPINPDHPLERVRLLLEDCGAR------------------VVLVDEraaTLGESLGETRVLHLErlpqSTGDLPAA 581
Cdd:cd05904   81 GAVVTTANPLSTPAEIAKQVKDSGAKlafttaelaeklaslalpVVLLDS---AEFDSLSFSDLLFEA----DEAEPPVV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  582 NVAPGDLAYVIYTSGSTGMPKGVMVEHR---SVVNRLNWMQRRYPIGErDVLLQKTPVtFDVsvwelfwWSFTGARLSLL 658
Cdd:cd05904  154 VIKQDDVAALLYSSGTTGRSKGVMLTHRnliAMVAQFVAGEGSNSDSE-DVFLCVLPM-FHI-------YGLSSFALGLL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  659 PPGA------EKDPREMLRSIQRDAVTVIHFVPSMLtpfLDLLDGDPTARAAASSLRLVFCSGealAPLQ---VARFRRL 729
Cdd:cd05904  225 RLGAtvvvmpRFDLEELLAAIERYKVTHLPVVPPIV---LALVKSPIVDKYDLSSLRQIMSGA---APLGkelIEAFRAK 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  730 FGDaVRLVNLYGPTEATVDVSDHECASDNPTRV-PIGRPIDNLRLYVLD-RALRPQPLGAVGELYIGGVGVARGYLNRPE 807
Cdd:cd05904  299 FPN-VDLGQGYGMTESTGVVAMCFAPEKDRAKYgSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPE 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  808 LNAERFLVDPFVaggrlyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVAR--DSA--- 882
Cdd:cd05904  378 ATAATIDKEGWL------HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYpdEEAgev 451

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523  883 -----VR--GTHL----VGYYVAaaeldpGQLraglsatlpdfmlpAFF--VR----IDSLPLSANGKLDRRQL 939
Cdd:cd05904  452 pmafvVRkpGSSLtedeIMDFVA------KQV--------------APYkkVRkvafVDAIPKSPSGKILRKEL 505
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1392-2056 6.54e-43

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: 173.33  E-value: 6.54e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1392 QLRDFRVWEETNFALLVnviATPSDGMYLRIDSDGRGISRSQAALIGATFVELLWRLADHPDEAADFAFLAPRRDAASQP 1471
Cdd:TIGR03443  147 QQTTYSTGSTTDLTVFL---TPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLP 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1472 EPLVD---------VVSLFERQVEALP---------GSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALN 1533
Cdd:TIGR03443  224 DPTKDldwsgfrgaIHDIFADNAEKHPdrtcvvetpSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAY 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1534 RSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAhpehahVAAAERVLP-VE-------ELVADI---- 1601
Cdd:TIGR03443  304 RGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIV------IEKAGTLDQlVRdyidkelELRTEIpala 377

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1602 ---------------EPETFAAPQL------------DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGL 1654
Cdd:TIGR03443  378 lqddgslvggsleggETDVLAPYQAlkdtptgvvvgpDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSEND 457

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1655 RTLQFAPLSFDMAFQEIFSTLCGGGELqLISNRERM-DPSALLHVLERRQVQRV-LLPfvALQRL--AEASNALGVRPGA 1730
Cdd:TIGR03443  458 KFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTADDIgTPGRLAEWMAKYGATVThLTP--AMGQLlsAQATTPIPSLHHA 534

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1731 LRVvvssGEQLrITEDVRAFCAAMPGLLLENQYGPTETHQ-VTYH---SLSGDP---AHYPDLPPIGRPLDGVEVQVLDA 1803
Cdd:TIGR03443  535 FFV----GDIL-TKRDCLRLQTLAENVCIVNMYGTTETQRaVSYFeipSRSSDStflKNLKDVMPAGKGMKNVQLLVVNR 609

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1804 ALRPVPVGV--TGELYFGGDCLARGYHRAPKLTAERFV-----------------EHPWR-----PGARLYRTGDLGRIL 1859
Cdd:TIGR03443  610 NDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkenNKPERefwlgPRDRLYRTGDLGRYL 689

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1860 GNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQA--- 1936
Cdd:TIGR03443  690 PDGNVECCGRADDQVKIRGFRIELGEIDTHL----SQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKSDELEEFKSEvdd 765

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1937 ------------------------LRSELPEHMVPAHFAWVDGFALTPSGKRDDAalrALPLEHGTNIEYLAPRDD---- 1988
Cdd:TIGR03443  766 eessdpvvkglikyrklikdireyLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKP---ALPFPDTAQLAAVAKNRSasaa 842

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523   1989 ------YERTLAGLLGELL-DRP-RVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLA---ERLR 2056
Cdd:TIGR03443  843 deefteTEREIRDLWLELLpNRPaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAkevDRLK 921
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 455-937 8.38e-43

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: 166.26  E-value: 8.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  455 VARTPQRTAL--LEADGG---TLSYAELDAKVQAVADALRAAGvRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD 529
Cdd:cd05931    3 AAARPDRPAYtfLDDEGGreeTLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  530 HP---LERVRLLLEDCGARVVLVDERAATL-------GESLGETRVLHLERLPQSTGDL-PAANVAPGDLAYVIYTSGST 598
Cdd:cd05931   82 TPgrhAERLAAILADAGPRVVLTTAAALAAvrafaasRPAAGTPRLLVVDLLPDTSAADwPPPSPDPDDIAYLQYTSGST 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  599 GMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFD---VSVWELFWWSftGARLSLLPPGA-EKDPREMLRSIQ 674
Cdd:cd05931  162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmglIGGLLTPLYS--GGPSVLMSPAAfLRRPLRWLRLIS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  675 RDAVTVIhFVPSM-------------LTPfLDLldgdptaraaaSSLRLVFCSGEALAPLQVARFRRLFGDAvrlvNL-- 739
Cdd:cd05931  240 RYRATIS-AAPNFaydlcvrrvrdedLEG-LDL-----------SSWRVALNGAEPVRPATLRRFAEAFAPF----GFrp 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  740 ------YGPTEATVDVS-------------------DHECASDNPTR-----VPIGRPIDNLRLYVLDRA-LRPQPLGAV 788
Cdd:cd05931  303 eafrpsYGLAEATLFVSggppgtgpvvlrvdrdalaGRAVAVAADDPaarelVSCGRPLPDQEVRIVDPEtGRELPDGEV 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  789 GELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRTGDLARwLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAAL 868
Cdd:cd05931  383 GEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEA 461

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523  869 PGVRDAAVVA-----RDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPD---FMLPAF-FVRIDSLPLSANGKLDRR 937
Cdd:cd05931  462 HPALRPGCVAafsvpDDGEERLVVVAEVERGADPADLAAIAAAIRAAVARehgVAPADVvLVRPGSIPRTSSGKIQRR 539
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 471-939 8.41e-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: 8.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD 550
Cdd:cd05903    1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 ERaatlgesLGETRVLHLerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVL 630
Cdd:cd05903   81 ER-------FRQFDPAAM----------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  631 LQKTPVT-FDVSVWELFWWSFTGARLSLLppgAEKDPREMLRSIQRDAVTviHFVPSmlTPFL-DLLDGDPTARAAASSL 708
Cdd:cd05903  138 LVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVT--FMMGA--TPFLtDLLNAVEEAGEPLSRL 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  709 RLVFCSGEALAPLQVARFRRLFGDAVrlVNLYGPTEATVDVSDHECASDNPTRVPIGRPIDNLRLYVLDRALRPQPLGAV 788
Cdd:cd05903  211 RTFVCGGATVPRSLARRAAELLGAKV--CSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVE 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  789 GELYIGGVGVARGYLNRPELNAERFlvdpfvaGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAAL 868
Cdd:cd05903  289 GELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGH 361

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523  869 PGVRDAAVVARDSAVRGTHLVGYYV--AAAELDPGQLRAGLSAT-LPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05903  362 PGVIEAAVVALPDERLGERACAVVVtkSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 7-410 1.10e-42

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: 162.96  E-value: 1.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    7 LPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAE-FEARH 85
Cdd:cd19066    2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVrFRIEI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   86 VDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLH-SDQALYVYVRTHHIVSDAWGLQLFLSRVRAGYLG-ELGEP 163
Cdd:cd19066   82 IDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRlADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaERQKP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  164 QAQMPTAS---LLAQLETddYSGSEQYRGDRAYFAEALEGLEP--ALFTRRRPAGLRRTARHRLTLE------RTLLDAI 232
Cdd:cd19066  162 TLPPPVGSyadYAAWLEK--QLESEAAQADLAYWTSYLHGLPPplPLPKAKRPSQVASYEVLTLEFFlrseetKRLREVA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  233 RDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTLL 312
Cdd:cd19066  240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  313 RHQKMPLGDLLR--------GASPLFDTTLSYMRWPAAQAIPNASvETVAQTHAHDPDA---LAIWVSEfDGHSDAQVDF 381
Cdd:cd19066  320 EHQRVPFIELVRhlgvvpeaPKHPLFEPVFTFKNNQQQLGKTGGF-IFTTPVYTSSEGTvfdLDLEASE-DPDGDLLLRL 397

                        410       420
                 ....*....|....*....|....*....
gi 15598523  382 EYACDVFDADFpMDAAARHIETFLRALVE 410
Cdd:cd19066  398 EYSRGVYDERT-IDRFAERYMTALRQLIE 425
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
 468-939 1.14e-42

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 165.01  E-value: 1.14e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    468 DGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVV 547
Cdd:TIGR02262   27 DISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVV 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    548 LVDER-----AATLGESLGETRVLHLERLPQSTGDLP-----------AANVAPGDLAYVIYTSGSTGMPKGVMVEHRS- 610
Cdd:TIGR02262  107 FVSGAllpviKAALGKSPHLEHRVVVGRPEAGEVQLAellateseqfkPAATQADDPAFWLYSSGSTGMPKGVVHTHSNp 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    611 VVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWE-LFWWSFTGARLSLLPpgAEKDPREMLRSIQRDAVTVIHFVPSMLT 689
Cdd:TIGR02262  187 YWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNaLTFPMSVGATTVLMG--ERPTPDAVFDRLRRHQPTIFYGVPTLYA 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    690 PFLdlldGDPTARAAAS-SLRLVFCSGEALaPLQVA-RFRRLFGdaVRLVNLYGPTEATvdvsdHECASDNPTRV---PI 764
Cdd:TIGR02262  265 AML----ADPNLPSEDQvRLRLCTSAGEAL-PAEVGqRWQARFG--VDIVDGIGSTEML-----HIFLSNLPGDVrygTS 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    765 GRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLvdpfvagGRLYRTGDLARWLADGNLEYLGR 844
Cdd:TIGR02262  333 GKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQ-------GEWTRSGDKYVRNDDGSYTYAGR 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    845 ADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDPGQLRAGLSATLPDFMLPAFFVR 922
Cdd:TIGR02262  406 TDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRpgQTALETELKEHVKDRLAPYKYPRWIVF 485

                          490
                   ....*....|....*..
gi 15598523    923 IDSLPLSANGKLDRRQL 939
Cdd:TIGR02262  486 VDDLPKTATGKIQRFKL 502
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 459-933 2.73e-42

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 163.89  E-value: 2.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   459 PQRTALLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLL 538
Cdd:PRK07514   16 RDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   539 LEDCGARVVLVDERA----ATLGESLGETRVLHL---------ERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVM 605
Cdd:PRK07514   96 IGDAEPALVVCDPANfawlSKIAAAAGAPHVETLdadgtgsllEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAM 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   606 VEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtFDVSvwELFWWS----FTGARLSLLPpgaEKDPREMLRSIQRdaVTVI 681
Cdd:PRK07514  176 LSHGNLLSNALTLVDYWRFTPDDVLIHALPI-FHTH--GLFVATnvalLAGASMIFLP---KFDPDAVLALMPR--ATVM 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   682 HFVPsmlTPFLDLLDGDPTARAAASSLRLvFCSGEalAPLQVARFRRLF---GDAV--RlvnlYGPTEATVDVSdhecas 756
Cdd:PRK07514  248 MGVP---TFYTRLLQEPRLTREAAAHMRL-FISGS--APLLAETHREFQertGHAIleR----YGMTETNMNTS------ 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   757 dNP---TRVP--IGRPIDNLRLYVLDRAL-RPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDL 830
Cdd:PRK07514  312 -NPydgERRAgtVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDL 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   831 ARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVA--AAELDPGQLRAGLS 908
Cdd:PRK07514  385 GKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPkpGAALDEAAILAALK 464

                         490       500
                  ....*....|....*....|....*
gi 15598523   909 ATLPDFMLPAFFVRIDSLPLSANGK 933
Cdd:PRK07514  465 GRLARFKQPKRVFFVDELPRNTMGK 489
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 1501-1971 8.94e-42

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: 160.58  E-value: 8.94e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1501 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAhp 1580
Cdd:cd05972    1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1581 ehahvaaaervlpveelvadiepetfaapQLDELAMLLFTSGSTGRPKGVELSHRmwanYTQWQLRVASGVPGLRT--LQ 1658
Cdd:cd05972   79 -----------------------------DAEDPALIYFTSGTTGLPKGVLHTHS----YPLGHIPTAAYWLGLRPddIH 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1659 FAPLsfDMAFQE-IFSTLCG---GGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGaLRVV 1734
Cdd:cd05972  126 WNIA--DPGWAKgAWSSFFGpwlLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSH-LRLV 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1735 VSSGEQLRiTEDVRAFCAAMpGLLLENQYGPTETHQVTyhslsgdpAHYPDLPP----IGRPLDGVEVQVLDAALRPVPV 1810
Cdd:cd05972  203 VSAGEPLN-PEVIEWWRAAT-GLPIRDGYGQTETGLTV--------GNFPDMPVkpgsMGRPTPGYDVAIIDDDGRELPP 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1811 GVTGELYF--GGDCLARGYHRAPKLTAERFVEHpwrpgarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVEL 1888
Cdd:cd05972  273 GEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVES 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1889 AIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLL---GEPEAVDLA-ELKQALRSELPEHMVPAHFAWVDGFALTPSGKR 1964
Cdd:cd05972  346 ALL----EHPAVAEAAVVGSPDPVRGEVVKAFVVltsGYEPSEELAeELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421


                 ....*..
gi 15598523 1965 DDAALRA 1971
Cdd:cd05972  422 RRVELRD 428
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 6-410 5.98e-41

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: 157.90  E-value: 5.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    6 RLPLSPYQRDIWVAAaQF-PELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEAR 84
Cdd:cd19531    1 PLPLSFAQQRLWFLD-QLePGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   85 HVDLRA--DRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGELG 161
Cdd:cd19531   80 VVDLSGlpEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTmHHIVSDGWSMGVLLRELAALYAAFLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  162 EpqaqmpTASLLAQLETD--DYS-------GSEQYRGDRAYFAEALEGLEPAL---FTRRRPAGLR-RTARHRLTLERTL 228
Cdd:cd19531  160 G------RPSPLPPLPIQyaDYAvwqrewlQGEVLERQLAYWREQLAGAPPVLelpTDRPRPAVQSfRGARVRFTLPAEL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  229 LDAIRD----RGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQL 304
Cdd:cd19531  234 TAALRAlarrEGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARV 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  305 REATRTLLRHQKMPLGDLLR--------GASPLFDTTLSYMRWP-AAQAIPNASVETVAQTHAH---DpdaLAIWVSEFD 372
Cdd:cd19531  314 RETALEAYAHQDLPFEKLVEalqperdlSRSPLFQVMFVLQNAPaAALELPGLTVEPLEVDSGTakfD---LTLSLTETD 390

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15598523  373 GHsdAQVDFEYACDVFDADFpMDAAARHIETFLRALVE 410
Cdd:cd19531  391 GG--LRGSLEYNTDLFDAAT-IERMAGHFQTLLEAIVA 425
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 1483-1963 9.20e-41

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: 160.48  E-value: 9.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1483 RQVEALPGSAALAF------EEQRWTYRDLDHVARCVATRLVRAGaRRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 1556
Cdd:cd05931    1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1557 VSYP---AQRLALILETAQPfRVV--AHPEHAHVAAAERVLPVEEL----------VADIEPETFAAPQLDELAMLLFTS 1621
Cdd:cd05931   80 PPTPgrhAERLAAILADAGP-RVVltTAAALAAVRAFAASRPAAGTprllvvdllpDTSAADWPPPSPDPDDIAYLQYTS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1622 GSTGRPKGVELSHR-MWANytQWQLRVASGV-PGLRTLQFAPLSFDMA-FQEIFSTLCGGGELQLISNRERM-DPSALLH 1697
Cdd:cd05931  159 GSTGTPKGVVVTHRnLLAN--VRQIRRAYGLdPGDVVVSWLPLYHDMGlIGGLLTPLYSGGPSVLMSPAAFLrRPLRWLR 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1698 VLERRQVQRVLLPFVALQRLAEASNALGVRP---GALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQ-----YG----- 1764
Cdd:cd05931  237 LISRYRATISAAPNFAYDLCVRRVRDEDLEGldlSSWRVALNGAEPVRP-ATLRRFAEAFAPFGFRPEafrpsYGlaeat 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1765 -----------------PTETHQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAA-LRPVPVGVTGELYFGGDCLARG 1826
Cdd:cd05931  316 lfvsggppgtgpvvlrvDRDALAGRAVAVAADDPAARELVSCGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASG 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1827 YHRAPKLTAERFVEHPWRPGARLYRTGDLGRILGnGEIVWLGRADTQVKVRGFRIEPAEVELAImrqAERQPGLRGAAVV 1906
Cdd:cd05931  396 YWGRPEATAETFGALAATDEGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEATA---EEAHPALRPGCVA 471

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523 1907 A---RERQGNDAFLAAFLLGEPEAVDLAELKQALRSELP-EHMVPAHFAWV---DGFALTPSGK 1963
Cdd:cd05931  472 AfsvPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVArEHGVAPADVVLvrpGSIPRTSSGK 535
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 425-939 1.04e-40

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 159.92  E-value: 1.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   425 AEREELIHTRNATDQAFPEQATLPTLFAEQVARTPQRTaLLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVA 504
Cdd:PRK06155    1 GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRP-LLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   505 RGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDERAATLGESLgETRVLHLER-------------- 570
Cdd:PRK06155   80 NRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAA-DPGDLPLPAvwlldapasvsvpa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   571 ------LPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHrsvvNRLNW----MQRRYPIGERDVLLQKTPVTFDV 640
Cdd:PRK06155  159 gwstapLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH----AQFYWwgrnSAEDLEIGADDVLYTTLPLFHTN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   641 SVWELFWWSFTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLTPfldLLDGDPTARAAASSLRLVFcsGEALAP 720
Cdd:PRK06155  235 ALNAFFQALLAGATYVLEP---RFSASGFWPAVRRHGATVTYLLGAMVSI---LLSQPARESDRAHRVRVAL--GPGVPA 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   721 LQVARFRRLFGdaVRLVNLYGPTEATVdvsdhECASDNPTRVP--IGRPIDNLRLYVLDRALRPQPLGAVGELYIGG--- 795
Cdd:PRK06155  307 ALHAAFRERFG--VDLLDGYGSTETNF-----VIAVTHGSQRPgsMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdep 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   796 VGVARGYLNRPE--LNAERFLvdpfvaggrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRD 873
Cdd:PRK06155  380 FAFATGYFGMPEktVEAWRNL---------WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA 450

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598523   874 AAVVARDSavrgtHLVGYYVAAA-------ELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK06155  451 AAVFPVPS-----ELGEDEVMAAvvlrdgtALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 1500-1963 1.68e-40

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: 156.77  E-value: 1.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1500 RWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPfrvvah 1579
Cdd:cd05903    1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1580 pehahvaaaeRVLPVEELVADIEPetfaAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGvPGLRTLQ 1658
Cdd:cd05903   75 ----------KVFVVPERFRQFDP----AAMPDAVALLLFTSGTTGEPKGVMHSHNtLSASIRQYAERLGLG-PGDVFLV 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1659 FAPLSFDMAFqeifstlCGGGELQLISN-----RERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRV 1733
Cdd:cd05903  140 ASPMAHQTGF-------VYGFTLPLLLGapvvlQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1734 VVSSGEQlrITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAH--YPDlppiGRPLDGVEVQVLDAALRPVPVG 1811
Cdd:cd05903  213 FVCGGAT--VPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRrlYTD----GRPLPGVEIKVVDDTGATLAPG 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1812 VTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIM 1891
Cdd:cd05903  287 VEGELLSRGPSVFLGYLDRPDLTADAAPEG-W------FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLL 359

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523 1892 rqaeRQPGLRGAAVVA--RERQGNDAflAAFLLGEPEA-VDLAELKQAL-RSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd05903  360 ----GHPGVIEAAVVAlpDERLGERA--CAVVVTKSGAlLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGK 429
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 457-945 9.62e-40

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 157.51  E-value: 9.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   457 RTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVR 536
Cdd:PRK06178   45 ERPQRPAI-IFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   537 LLLEDCGARVVLV-DERAATLGESLGETRVLH-----------------------------------LERLPQSTGDLPA 580
Cdd:PRK06178  124 YELNDAGAEVLLAlDQLAPVVEQVRAETSLRHvivtsladvlpaeptlplpdslraprlaaagaidlLPALRACTAPVPL 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   581 ANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVnrlnWMQRRY-----PIGERDVLLQKTPvtfdvsvweLFWWS------ 649
Cdd:PRK06178  204 PPPALDALAALNYTGGTTGMPKGCEHTQRDMV----YTAAAAyavavVGGEDSVFLSFLP---------EFWIAgenfgl 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   650 ----FTGARLSLLppgAEKDPREMLRSIQRDAVTVIhfvpSMLTP-FLDLLDGDPTARAAASSLRLVFCSG--EALAPLQ 722
Cdd:PRK06178  271 lfplFSGATLVLL---ARWDAVAFMAAVERYRVTRT----VMLVDnAVELMDHPRFAEYDLSSLRQVRVVSfvKKLNPDY 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   723 VARFRRLFGDAVRLVNlYGPTEA-TVD-------VSDHECASDnPTRVpiGRPIDNLRLYVLDRAL-RPQPLGAVGELYI 793
Cdd:PRK06178  344 RQRWRALTGSVLAEAA-WGMTEThTCDtftagfqDDDFDLLSQ-PVFV--GLPVPGTEFKICDFETgELLPLGAEGEIVV 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   794 GGVGVARGYLNRPELNAERfLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRD 873
Cdd:PRK06178  420 RTPSLLKGYWNKPEATAEA-LRDGW------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLG 492

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598523   874 AAVVARDSAVRGTHLVGYYV--AAAELDPGQLRAGLSATLPDFMLPAffVRI-DSLPLSANGKLDRRQLPAPPEQ 945
Cdd:PRK06178  493 SAVVGRPDPDKGQVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPE--IRIvDALPMTATGKVRKQDLQALAEE 565
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
446-939 1.37e-39

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 155.51  E-value: 1.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   446 TLPTLFAEQVARTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVP 525
Cdd:PRK03640    3 TMPNWLKQRAFLTPDRTAI-EFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   526 INPDHPLERVRLLLEDCGARVVLVDERAATLGESLGETRVLHLERLPQSTGDLpaanVAPGDL---AYVIYTSGSTGMPK 602
Cdd:PRK03640   82 LNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEI----QEEFDLdevATIMYTSGTTGKPK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   603 GVMVE-----HRSVVNRLNwmqrrypIG--ERDVLLQKTPVtFDVSVWELFWWSFT-GARLSLLppgaEK-DPREMLRSI 673
Cdd:PRK03640  158 GVIQTygnhwWSAVGSALN-------LGltEDDCWLAAVPI-FHISGLSILMRSVIyGMRVVLV----EKfDAEKINKLL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   674 QRDAVTVIHFVPSMLTPFLDLLDGDPTAraaaSSLRLVFCSG--EALAPLQVARFRRLfgdavRLVNLYGPTE-----AT 746
Cdd:PRK03640  226 QTGGVTIISVVSTMLQRLLERLGEGTYP----SSFRCMLLGGgpAPKPLLEQCKEKGI-----PVYQSYGMTEtasqiVT 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   747 VDvsdhecASDNPTRV-PIGRPIDNLRLYVLDRaLRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlvdpfvAGGRLY 825
Cdd:PRK03640  297 LS------PEDALTKLgSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF------QDGWFK 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   826 rTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRA 905
Cdd:PRK03640  364 -TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRH 442

                         490       500       510
                  ....*....|....*....|....*....|....
gi 15598523   906 GLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK03640  443 FCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 472-941 1.85e-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: 154.20  E-value: 1.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDE 551
Cdd:cd05969    1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  552 RAAtlgeslgetrvlhlERLpqstgdlpaanvAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRlnWMQRRYpigerdvll 631
Cdd:cd05969   81 ELY--------------ERT------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFY--YFTGKY--------- 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  632 qktpvTFDVSVWELFW------WsFTGARLSLLPP----------GAEKDPREMLRSIQRDAVTVIHFVPSMLTpFLDLL 695
Cdd:cd05969  124 -----VLDLHPDDIYWctadpgW-VTGTVYGIWAPwlngvtnvvyEGRFDAESWYGIIERVKVTVWYTAPTAIR-MLMKE 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  696 DGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTE-ATVDVSDHECASDNPTRvpIGRPIDNLRLY 774
Cdd:cd05969  197 GDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG--VPIHDTWWQTEtGSIMIANYPCMPIKPGS--MGKPLPGVKAA 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  775 VLDRALRPQPLGAVGELYI--GGVGVARGYLNRPElNAERFLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKIR 852
Cdd:cd05969  273 VVDENGNELPPGTKGILALkpGWPSMFRGIWNDEE-RYKNSFIDGW------YLTGDLAYRDEDGYFWFVGRADDIIKTS 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  853 GNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQ---------LRAGLSATLpdfmLPAFFVRI 923
Cdd:cd05969  346 GHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkeeiinfVRQKLGAHV----APREIEFV 421

                        490
                 ....*....|....*...
gi 15598523  924 DSLPLSANGKLDRRQLPA 941
Cdd:cd05969  422 DNLPKTRSGKIMRRVLKA 439
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1499-1971 1.98e-39

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: 153.74  E-value: 1.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1499 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLdvsypaqrLALILETAQPFRVvA 1578
Cdd:cd05971    5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL--------FALFGPEALEYRL-S 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1579 HPEhahvAAAervlpveeLVADIEpetfaapqlDELAMLLFTSGSTGRPKGVELSHRMwanytqwqlrVASGVPGLR-TL 1657
Cdd:cd05971   76 NSG----ASA--------LVTDGS---------DDPALIIYTSGTTGPPKGALHAHRV----------LLGHLPGVQfPF 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1658 QFAPLSFDMAFQEIFSTLCGG-----------GELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGV 1726
Cdd:cd05971  125 NLFPRDGDLYWTPADWAWIGGlldvllpslyfGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKH 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1727 RPGALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPahyPDLPPIGRPLDGVEVQVLDAALR 1806
Cdd:cd05971  205 AQVKLRAIATGGESL--GEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFP---IKPGSMGKPIPGHRVAIVDDNGT 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1807 PVPVGVTGELYFGGDCLAR--GYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPA 1884
Cdd:cd05971  280 PLPPGEVGEIAVELPDPVAflGYWNNPSATEKKMAGD-W------LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPA 352

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1885 EVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQAL----RSELPEHMVPAHFAWVDGFALTP 1960
Cdd:cd05971  353 EIEECLL----KHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIqelvKTRLAAHEYPREIEFVNELPRTA 428

                        490
                 ....*....|.
gi 15598523 1961 SGKRDDAALRA 1971
Cdd:cd05971  429 TGKIRRRELRA 439
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 444-939 2.34e-39

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 155.48  E-value: 2.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   444 QATLPTLFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAY 523
Cdd:PRK08316   10 RQTIGDILRRSARRYPDKTALVFGDR-SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   524 VPINPDHPLERVRLLLEDCGARVVLVD-ERAATLGESLGETRVLHLERLPQSTGDL-------------------PAANV 583
Cdd:PRK08316   89 VPVNFMLTGEELAYILDHSGARAFLVDpALAPTAEAALALLPVDTLILSLVLGGREapggwldfadwaeagsvaePDVEL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   584 APGDLAYVIYTSGSTGMPKGVMVEHRSVVNrlnwmqrRY-------PIGERDVLLQKTPV----TFDVSVWELFWwsfTG 652
Cdd:PRK08316  169 ADDDLAQILYTSGTESLPKGAMLTHRALIA-------EYvscivagDMSADDIPLHALPLyhcaQLDVFLGPYLY---VG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   653 ARLSLLPpgaEKDPREMLRSIQRDAVTVIhFVPSmlTPFLDLLDGDPTARAAASSLRLVFcSGEALAPLQV-ARFRRLFG 731
Cdd:PRK08316  239 ATNVILD---APDPELILRTIEAERITSF-FAPP--TVWISLLRHPDFDTRDLSSLRKGY-YGASIMPVEVlKELRERLP 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   732 DaVRLVNLYGPTE----ATV-DVSDHECASDNPtrvpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRP 806
Cdd:PRK08316  312 G-LRFYNCYGQTEiaplATVlGPEEHLRRPGSA-----GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDP 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   807 ELNAERFlvdpfvAGGrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGT 886
Cdd:PRK08316  386 EKTAEAF------RGG-WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIE 458

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15598523   887 HLVGYYV--AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK08316  459 AVTAVVVpkAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 446-939 2.54e-39

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: 154.41  E-value: 2.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  446 TLPTLFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVP 525
Cdd:cd05920   16 PLGDLLARSAARHPDRIAVVDGDR-RLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  526 INPDHPLERVRLLLEDCGARVVLVDERAAtlgeslgetRVLHLERLPQSTGDLPaanvapgDLAYVIYTSGSTGMPKGVM 605
Cdd:cd05920   95 ALPSHRRSELSAFCAHAEAVAYIVPDRHA---------GFDHRALARELAESIP-------EVALFLLSGGTTGTPKLIP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  606 VEHrsvvNRLNWMQRRYP----IGERDVLLQKTPV--TFDVSVWELFWWSFTGARLSLLPPGaekDPREMLRSIQRDAVT 679
Cdd:cd05920  159 RTH----NDYAYNVRASAevcgLDQDTVYLAVLPAahNFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIEREGVT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  680 VIHFVPSMLTPFLDLLDGDptaRAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVSdhecASDNP 759
Cdd:cd05920  232 VTALVPALVSLWLDAAASR---RADLSSLRLLQVGGARLSPALARRVPPVLG--CTLQQVFGMAEGLLNYT----RLDDP 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  760 TRVPI---GRPI---DNLRlyVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARW 833
Cdd:cd05920  303 DEVIIhtqGRPMspdDEIR--VVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRR 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  834 LADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA-AELDPGQLRAGLSAT-L 911
Cdd:cd05920  375 TPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRdPPPSAAQLRRFLRERgL 454

                        490       500
                 ....*....|....*....|....*...
gi 15598523  912 PDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05920  455 AAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 1501-1963 6.51e-39

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: 153.62  E-value: 6.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1501 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPfRVVAHP 1580
Cdd:cd05926   15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS-KLVLTP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1581 EH----AHVAAAERVLPVEELVAD--------------------IEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRM 1636
Cdd:cd05926   94 KGelgpASRAASKLGLAILELALDvgvlirapsaeslsnlladkKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRN 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1637 WANYTQWQLRVASGVPGLRTLQFAPLsfdmaFQ------EIFSTLCGGGELQLisnRERMDPSALLHVLERRQV------ 1704
Cdd:cd05926  174 LAASATNITNTYKLTPDDRTLVVMPL-----FHvhglvaSLLSTLAAGGSVVL---PPRFSASTFWPDVRDYNAtwytav 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1705 ---QRVLLPFvalqrlaEASNALGVRPGaLRVVVSSGEQLriTEDV-RAFCAAMPGLLLEnQYGPTET-HQVTYHSLsgd 1779
Cdd:cd05926  246 ptiHQILLNR-------PEPNPESPPPK-LRFIRSCSASL--PPAVlEALEATFGAPVLE-AYGMTEAaHQMTSNPL--- 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1780 PAHYPDLPPIGRPlDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRIL 1859
Cdd:cd05926  312 PPGPRKPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1860 GNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA--RERQGnDAFLAAFLLGEPEAVDLAELKQAL 1937
Cdd:cd05926  385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLL----SHPAVLEAVAFGvpDEKYG-EEVAAAVVLREGASVTEEELRAFC 459

                        490       500
                 ....*....|....*....|....*.
gi 15598523 1938 RSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd05926  460 RKHLAAFKVPKKVYFVDELPKTATGK 485
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 472-939 1.02e-38

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: 151.48  E-value: 1.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVde 551
Cdd:cd05935    2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  552 raatlGESLGetrvlhlerlpqstgdlpaanvapgDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLL 631
Cdd:cd05935   80 -----GSELD-------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVIL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  632 QKTPVtFDVS--VWELFWWSFTGARLSLLppgAEKDPREMLRSIQRDAVTVIHFVPSMLtpfLDLLDGDPTARAAASSLR 709
Cdd:cd05935  130 ACLPL-FHVTgfVGSLNTAVYVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTML---VDLLATPEFKTRDLSSLK 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  710 LVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVsdHECASDNPTRVPIGRPIDNLRLYVLD-RALRPQPLGAV 788
Cdd:cd05935  203 VLTGGGAPMPPAVAEKLLKLTG--LRFVEGYGLTETMSQT--HTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEV 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  789 GELYIGGVGVARGYLNRPELNAERFLVDpfvAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAAL 868
Cdd:cd05935  279 GEIVVRGPQIFKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  869 PGVRDAAVVARDSAVRGTHLVGYYVaaaeLDPGqLRAGLSA---------TLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05935  356 PAI*EVCVISVPDERVGEEVKAFIV----LRPE-YRGKVTEediiewareQMAAYKYPREVEFVDELPRSASGKILWRLL 430
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 459-934 2.67e-38

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: 153.50  E-value: 2.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  459 PQRTALL-EADGG----TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLE 533
Cdd:cd17634   67 GDRTAIIyEGDDTsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  534 RVRLLLEDCGARVVL-----------------VDERAATLGESLGETRVLHLERLP-----------------QSTGDLP 579
Cdd:cd17634  147 AVAGRIIDSSSRLLItadggvragrsvplkknVDDALNPNVTSVEHVIVLKRTGSDidwqegrdlwwrdliakASPEHQP 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  580 AAnVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNW-MQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLL 658
Cdd:cd17634  227 EA-MNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLL 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  659 PPGAEK--DPREMLRSIQRDAVTVIHFVPSMLTPfLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAVR- 735
Cdd:cd17634  306 YEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRA-LMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCp 384

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  736 LVNLYGPTEatvdvSDHECASDNPTRVPIG-----RPIDNLRLYVLDRALRPQPLGAVGELYIGGV--GVARGYLNRPEl 808
Cdd:cd17634  385 VVDTWWQTE-----TGGFMITPLPGAIELKagsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE- 458

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  809 naeRFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHL 888
Cdd:cd17634  459 ---RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAP 535

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15598523  889 VGYYV-AAAELDPGQLRAGLSATLPDFMLPAFFVR----IDSLPLSANGKL 934
Cdd:cd17634  536 YAYVVlNHGVEPSPELYAELRNWVRKEIGPLATPDvvhwVDSLPKTRSGKI 586
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 1470-1972 2.81e-38

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: 152.61  E-value: 2.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1470 QPEPLVDVvslFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG 1549
Cdd:COG1021   23 RGETLGDL---LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1550 LVCVpldVSYPAQRLALIL---ETAQP-------------FRVVA--------HPEHAHVAA-AERVLPVEELVADIEPE 1604
Cdd:COG1021  100 AIPV---FALPAHRRAEIShfaEQSEAvayiipdrhrgfdYRALArelqaevpSLRHVLVVGdAGEFTSLDALLAAPADL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1605 TFAAPQLDELAMLLFTSGSTGRPKGVELSHrmwANYTqWQLRVASGVPGL----RTLQFAPLS--FDMAFQEIFSTLCGG 1678
Cdd:COG1021  177 SEPRPDPDDVAFFQLSGGTTGLPKLIPRTH---DDYL-YSVRASAEICGLdadtVYLAALPAAhnFPLSSPGVLGVLYAG 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1679 GELQLISNrerMDPSALLHVLERRQVQRVLL-PFVALqRLAEASNALGVRPGALRVVVSSGEQLrITEDVRAFCAAMpGL 1757
Cdd:COG1021  253 GTVVLAPD---PSPDTAFPLIERERVTVTALvPPLAL-LWLDAAERSRYDLSSLRVLQVGGAKL-SPELARRVRPAL-GC 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1758 LLENQYGPTEThQVTYHSLsGDP----AHYpdlppIGRPL-DGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPK 1832
Cdd:COG1021  327 TLQQVFGMAEG-LVNYTRL-DDPeeviLTT-----QGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1833 LTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQaerqPGLRGAAVVARErqg 1912
Cdd:COG1021  400 HNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAH----PAVHDAAVVAMP--- 466

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598523 1913 nDAFLA----AFLLGEPEAVDLAELKQALRS-ELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:COG1021  467 -DEYLGerscAFVVPRGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 457-939 3.29e-38

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 151.58  E-value: 3.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   457 RTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVR 536
Cdd:PRK06145   14 RTPDRAALVYRDQ-EISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   537 LLLEDCGARVVLVDERAATLGeSLGETRVLHLERLPQSTGDL--------PAANVAPGDLAYVIYTSGSTGMPKGVMVEH 608
Cdd:PRK06145   93 YILGDAGAKLLLVDEEFDAIV-ALETPKIVIDAAAQADSRRLaqggleipPQAAVAPTDLVRLMYTSGTTDRPKGVMHSY 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   609 rsvvNRLNWMQRRYPIG----ERDVLLQKTPV----TFDVSVWELFWwsfTGARLSLLppgAEKDPREMLRSIQRDAVTV 680
Cdd:PRK06145  172 ----GNLHWKSIDHVIAlgltASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRIH---REFDPEAVLAAIERHRLTC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   681 IHFVPSMLTPFLDLLDGDptaRAAASSLRLVFCSGEALAPLQVARFRRLFGDAvRLVNLYGPTEATVDVSDHECASDNPT 760
Cdd:PRK06145  242 AWMAPVMLSRVLTVPDRD---RFDLDSLAWCIGGGEKTPESRIRDFTRVFTRA-RYIDAYGLTETCSGDTLMEAGREIEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   761 RVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlyRTGDLARWLADGNLE 840
Cdd:PRK06145  318 IGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLY 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   841 YLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV--AAAELDPGQLRAGLSATLPDFMLPA 918
Cdd:PRK06145  391 LTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlnPGATLTLEALDRHCRQRLASFKVPR 470

                         490       500
                  ....*....|....*....|.
gi 15598523   919 FFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK06145  471 QLKVRDELPRNPSGKVLKRVL 491
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1047-1453 4.53e-38

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: 150.18  E-value: 4.53e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1047 EDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARSE 1126
Cdd:pfam00668    2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPFE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1127 PLILDLRG--NPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAF-VREDGLDLVFSFHHAILDGWSVANLIVALVAAY--- 1200
Cdd:pfam00668   82 LEIIDISDlsESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFrIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqql 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1201 -RGEPLP-GPAPALACHVREELAALASPA---AVGYWTGLLEGARMTrLDGFGAHEPQAAQGPASHREA--LPDGLLERL 1273
Cdd:pfam00668  162 lKGEPLPlPPKTPYKDYAEWLQQYLQSEDyqkDAAYWLEQLEGELPV-LQLPKDYARPADRSFKGDRLSftLDEDTEELL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1274 KATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIAGC-SWIEVADALFRQ 1352
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS-PDIERMVGMFVNTLPLRIDPKGGkTFSELIKRVQED 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1353 ERDGHAHRRYPL------SAIQQIVGDE--LSSAFNYVNL---HVLEPLWQLRDFRV------WEETNFALlvNVIATPS 1415
Cdd:pfam00668  320 LLSAEPHQGYPFgdlvndLRLPRDLSRHplFDPMFSFQNYlgqDSQEEEFQLSELDLsvssviEEEAKYDL--SLTASER 397

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 15598523   1416 DG-MYLRIDSDGRGISRSQAALIGATFVELLWRLADHPD 1453
Cdd:pfam00668  398 GGgLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPS 436
PRK13382 PRK13382
bile acid CoA ligase;
449-942 2.88e-37

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 149.52  E-value: 2.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   449 TLFAEQVARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINP 528
Cdd:PRK13382   47 SGFAIAAQRCPDRPGLID-ELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   529 DHPLERVRLLLEDCGARVVLVDER-AATLGESL--------------GETRVLHLERLPQSTGDLPAANVAPGDLayVIY 593
Cdd:PRK13382  126 SFAGPALAEVVTREGVDTVIYDEEfSATVDRALadcpqatrivawtdEDHDLTVEVLIAAHAGQRPEPTGRKGRV--ILL 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   594 TSGSTGMPKGV-------MVEHRSVVNRLNWMQRRypigerdvllqktPVtfdVSVWELFW-WSFTGARLSLLPPGA--- 662
Cdd:PRK13382  204 TSGTTGTPKGArrsgpggIGTLKAILDRTPWRAEE-------------PT---VIVAPMFHaWGFSQLVLAASLACTivt 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   663 --EKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDgDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAvrLVNLY 740
Cdd:PRK13382  268 rrRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPA-EVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV--IYNNY 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   741 GPTE----ATVDVSDHECASDNPtrvpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNrpelNAERFLVD 816
Cdd:PRK13382  345 NATEagmiATATPADLRAAPDTA-----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTS----GSTKDFHD 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   817 PFVAggrlyrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAA 896
Cdd:PRK13382  416 GFMA------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 15598523   897 ELD--PGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPAP 942
Cdd:PRK13382  490 GASatPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 447-939 2.97e-37

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 149.42  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   447 LPTLFAEQVARTPQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPI 526
Cdd:PRK07470    9 LAHFLRQAARRFPDRIALVWGDR-SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   527 NPDHPLERVRLLLEDCGARVVLV-----DERAATLGESLGETRVLHLERLPQSTG--DLPAAN---------VAPGDLAY 590
Cdd:PRK07470   88 NFRQTPDEVAYLAEASGARAMIChadfpEHAAAVRAASPDLTHVVAIGGARAGLDyeALVARHlgarvanaaVDHDDPCW 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   591 VIYTSGSTGMPKGVMVEHRS---VVNrlNWMQRRYP-IGERDVLLQKTPVTFDVSVWELFWwSFTGARlSLLPPGAEKDP 666
Cdd:PRK07470  168 FFFTSGTTGRPKAAVLTHGQmafVIT--NHLADLMPgTTEQDASLVVAPLSHGAGIHQLCQ-VARGAA-TVLLPSERFDP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   667 REMLRSIQRDAVTVIHFVPSMLTpfldLLDGDP-TARAAASSLRLVFCSGealAPLQVA---RFRRLFGDAvrLVNLYGP 742
Cdd:PRK07470  244 AEVWALVERHRVTNLFTVPTILK----MLVEHPaVDRYDHSSLRYVIYAG---APMYRAdqkRALAKLGKV--LVQYFGL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   743 TEATVDVS-----DHECASDNPTRV-PIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVD 816
Cdd:PRK07470  315 GEVTGNITvlppaLHDAEDGPDARIgTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   817 PFvaggrlyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGThlVGYYV--- 893
Cdd:PRK07470  395 WF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGE--VGVAVcva 465

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 15598523   894 -AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK07470  466 rDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 1501-1969 3.70e-37

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: 148.82  E-value: 3.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1501 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAhp 1580
Cdd:cd17647   21 FTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV-- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1581 ehahVAAAERVLpveelvadiepetfaAPqlDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFA 1660
Cdd:cd17647   99 ----IRAAGVVV---------------GP--DSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1661 PLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRL-AEASNALGVRPGALRVvvssGE 1739
Cdd:cd17647  158 GIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLtAQATTPFPKLHHAFFV----GD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1740 QLrITEDVRAFCAAMPGLLLENQYGPTETHQ-VTYH---SLSGDPAHY---PDLPPIGRPLDGVEVQVLDAALRP--VPV 1810
Cdd:cd17647  234 IL-TKRDCLRLQTLAENVRIVNMYGTTETQRaVSYFevpSRSSDPTFLknlKDVMPAGRGMLNVQLLVVNRNDRTqiCGI 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1811 GVTGELYFGGDCLARGYHRAPKLTAERFV-----------------EHPWR-----PGARLYRTGDLGRILGNGEIVWLG 1868
Cdd:cd17647  313 GEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvepdhwnyldkdnNEPWRqfwlgPRDRLYRTGDLGRYLPNGDCECCG 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1869 RADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL------------------ 1930
Cdd:cd17647  393 RADDQVKIRGFRIELGEIDTHI----SQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDesfaqedvpkevstdpiv 468

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 15598523 1931 ----------AELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAAL 1969
Cdd:cd17647  469 kgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 587-939 4.04e-37

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: 144.01  E-value: 4.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  587 DLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtFDVS-VWELFWWSFTGARLSLLPPGaekd 665
Cdd:cd17630    1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPL-YHVGgLAILVRSLLAGAELVLLERN---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  666 pREMLRSIQRDAVTVIHFVPSMLTPFLDlldgDPTARAAASSLRLVFCSGealAPLQVARFRRLFGDAVRLVNLYGPTEA 745
Cdd:cd17630   76 -QALAEDLAPPGVTHVSLVPTQLQRLLD----SGQGPAALKSLRAVLLGG---APIPPELLERAADRGIPLYTTYGMTET 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  746 TVDVSDheCASDNPTRVPIGRPIDNLRLYVLDRalrpqplgavGELYIGGVGVARGYLNRPelnaerfLVDPFVAGGrLY 825
Cdd:cd17630  148 ASQVAT--KRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEFNEDG-WF 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  826 RTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRA 905
Cdd:cd17630  208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRA 287

                        330       340       350
                 ....*....|....*....|....*....|....
gi 15598523  906 GLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd17630  288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 452-951 9.60e-37

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 146.88  E-value: 9.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   452 AEQVARTPQRTALLE-ADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDH 530
Cdd:PRK09088    2 AFHARLQPQRLAAVDlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   531 PLERVRLLLEDCGARVVLVDERAATlgeslGETRVLHLERLPQSTGDLPAANVAPGD---LAYVIYTSGSTGMPKGVMVE 607
Cdd:PRK09088   82 SASELDALLQDAEPRLLLGDDAVAA-----GRTDVEDLAAFIASADALEPADTPSIPperVSLILFTSGTSGQPKGVMLS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   608 HRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVwelfwwsFTGARLSLLPPGAEK-----DPREMLRSIQRDAVTVIH 682
Cdd:PRK09088  157 ERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGL-------ITSVRPVLAVGGSILvsngfEPKRTLGRLGDPALGITH 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   683 F--VPSMLTPFLDLLDGDPtarAAASSLRLVFCSGealAPLQVARFRRLFGDAVRLVNLYGPTEA-TVDVSDHECASDNP 759
Cdd:PRK09088  230 YfcVPQMAQAFRAQPGFDA---AALRHLTALFTGG---APHAAEDILGWLDDGIPMVDGFGMSEAgTVFGMSVDCDVIRA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   760 TRVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLADGNL 839
Cdd:PRK09088  304 KAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADGFF 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   840 EYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGT--HLVGYYVAAAELDPGQLRAGLSATLPDFMLP 917
Cdd:PRK09088  378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEvgYLAIVPADGAPLDLERIRSHLSTRLAKYKVP 457

                         490       500       510
                  ....*....|....*....|....*....|....
gi 15598523   918 AFFVRIDSLPLSANGKLDRRQLpapPEQVAAVAP 951
Cdd:PRK09088  458 KHLRLVDALPRTASGKLQKARL---RDALAAGRK 488
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 1473-1972 1.02e-36

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 148.65  E-value: 1.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1473 PLVDVVSLFERQVealPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVC 1552
Cdd:PRK06178   34 PLTEYLRAWARER---PQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1553 VPLDVSYPAQRLALILETAQP---------------------FRVVAHPEHAHVAAAERVLPVEELV----------ADI 1601
Cdd:PRK06178  111 VPVSPLFREHELSYELNDAGAevllaldqlapvveqvraetsLRHVIVTSLADVLPAEPTLPLPDSLraprlaaagaIDL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1602 --------EPETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-----MWANYTQWQLRVASGVpglrTLQFAPLsFDMA- 1667
Cdd:PRK06178  191 lpalractAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAVVGGEDSV----FLSFLPE-FWIAg 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1668 --FQEIFSTLCgGGELQLISnreRMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITE 1745
Cdd:PRK06178  266 enFGLLFPLFS-GATLVLLA---RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSFVKKLNP 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1746 DVR-AFCAAMPGLLLENQYGPTETH---------QVTYHSLSGDPAHypdlppIGRPLDGVEVQVLD-AALRPVPVGVTG 1814
Cdd:PRK06178  342 DYRqRWRALTGSVLAEAAWGMTETHtcdtftagfQDDDFDLLSQPVF------VGLPVPGTEFKICDfETGELLPLGAEG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1815 ELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqa 1894
Cdd:PRK06178  416 EIVVRTPSLLKGYWNKPEATAEALRDG-W------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLG--- 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1895 eRQPGLRGAAVVAR--ERQGNDAFlaAFLLGEPEA-VDLAELKQALRSELPEHMVPaHFAWVDGFALTPSGKRDDAALRA 1971
Cdd:PRK06178  486 -QHPAVLGSAVVGRpdPDKGQVPV--AFVQLKPGAdLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQA 561


                  .
gi 15598523  1972 L 1972
Cdd:PRK06178  562 L 562
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1512-1970 6.41e-36

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: 143.73  E-value: 6.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1512 CVATRLVR-AGARRGDAIGVALNRSPEMIATIWGILRAG----LVCVPLDVSYPAQRLALILETAQPFRVVAHPEHA-HV 1585
Cdd:cd05922    4 SAAASALLeAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAAdRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1586 AAAERVLP-------VEELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQ 1658
Cdd:cd05922   84 RDALPASPdpgtvldADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1659 FAPLSFDMAFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQRVLLP--FVALQRLAEASNALgvrpGALRVVVS 1736
Cdd:cd05922  164 VLPLSYDYGLSVLNTHLLRGATL-VLTNDGVLDDAFWEDLREHGATGLAGVPstYAMLTRLGFDPAKL----PSLRYLTQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1737 SGEQLRiTEDVRAFCAAMPGLLLENQYGPTE-THQVTYHslsgdPAHYPDLPP--IGRPLDGVEVQVLDAALRPVPVGVT 1813
Cdd:cd05922  239 AGGRLP-QETIARLRELLPGAQVYVMYGQTEaTRRMTYL-----PPERILEKPgsIGLAIPGGEFEILDDDGTPTPPGEP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1814 GELYFGGDCLARGYHRAPKLTAErfvehPWRPGARLYrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQ 1893
Cdd:cd05922  313 GEIVHRGPNVMKGYWNDPPYRRK-----EGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523 1894 AErqpgLRGAAVVARERQGNDAfLAAFLLGEPEaVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd05922  387 GL----IIEAAAVGLPDPLGEK-LALFVTAPDK-IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 1470-1969 7.67e-36

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: 144.01  E-value: 7.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1470 QPEPLVDVVSlfeRQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG 1549
Cdd:cd05920   13 QDEPLGDLLA---RSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1550 LVCVpldVSYPAQRLALIL---ETAQPFRVVAHPEHA---HVAAAervlpvEELVADIEpetfaapqldELAMLLFTSGS 1623
Cdd:cd05920   90 AVPV---LALPSHRRSELSafcAHAEAVAYIVPDRHAgfdHRALA------RELAESIP----------EVALFLLSGGT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1624 TGRPKGVELSHRMWAnytqWQLRVASGVPGL--RTLQFAPLS----FDMAFQEIFSTLCGGGELQLISNrerMDPSALLH 1697
Cdd:cd05920  151 TGTPKLIPRTHNDYA----YNVRASAEVCGLdqDTVYLAVLPaahnFPLACPGVLGTLLAGGRVVLAPD---PSPDAAFP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1698 VLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEqlRITEDVRAFCAAMPGLLLENQYGPTEThQVTYHSLs 1777
Cdd:cd05920  224 LIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGA--RLSPALARRVPPVLGCTLQQVFGMAEG-LLNYTRL- 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1778 GDPA---HYPDlppiGRPLD-GVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTG 1853
Cdd:cd05920  300 DDPDeviIHTQ----GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1854 DLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARErqgnDAFLA----AFLLGEPEAVD 1929
Cdd:cd05920  370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVE----NLLLRHPAVHDAAVVAMP----DELLGerscAFVVLRDPPPS 441

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 15598523 1930 LAELKQALRS-ELPEHMVPAHFAWVDGFALTPSGKRDDAAL 1969
Cdd:cd05920  442 AAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 1502-1963 9.60e-36

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: 142.62  E-value: 9.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1502 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPE 1581
Cdd:cd05935    3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1582 hahvaaaervlpveelvadiepetfaapqLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQwqLRVASGV-PGLRTLQF 1659
Cdd:cd05935   83 -----------------------------LDDLALIPYTSGTTGLPKGCMHTHFsAAANALQ--SAVWTGLtPSDVILAC 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1660 APLSFDMAFQEIFST-LCGGGELQLISnreRMDPSALLHVLERRQVQ------RVLLPFVALQRLAEA--SNALGVRPGA 1730
Cdd:cd05935  132 LPLFHVTGFVGSLNTaVYVGGTYVLMA---RWDRETALELIEKYKVTfwtnipTMLVDLLATPEFKTRdlSSLKVLTGGG 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1731 LRVVVSSGEQLRitedvrafcaAMPGLLLENQYGPTETHQVTyHSlsgDPAHYPDLPPIGRPLDGVEVQVLDA-ALRPVP 1809
Cdd:cd05935  209 APMPPAVAEKLL----------KLTGLRFVEGYGLTETMSQT-HT---NPPLRPKLQCLGIP*FGVDARVIDIeTGRELP 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1810 VGVTGELYFGGDCLARGYHRAPKLTAERFVEhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElA 1889
Cdd:cd05935  275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE-A 350

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523 1890 IMRQaerQPGLRGAAVVAR--ERQGNDAflAAFLLGEPE---AVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd05935  351 KLYK---HPAI*EVCVISVpdERVGEEV--KAFIVLRPEyrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGK 424
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 6-410 1.09e-35

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: 142.52  E-value: 1.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    6 RLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETD-GTPYQWLDTDAEFEAR 84
Cdd:cd19539    1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   85 HVDL-RADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALL-HSDQALYVYVRTHHIVSDAWGLQLF-------LSRVRAG 155
Cdd:cd19539   81 VRDLsDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGrFDPDDHVLVLVAHHTAFDAWSLDVFardlaalYAARRKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  156 YLGELGEPQAQMPTASLlaqlETDDYSGSEQYRGDRAYFAEALEGLEPA--LFTRRRPAGL-RRTARHRLTLERTLLDAI 232
Cdd:cd19539  161 PAAPLPELRQQYKEYAA----WQREALAAPRAAELLDFWRRRLRGAEPTalPTDRPRPAGFpYPGADLRFELDAELVAAL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  233 R----DRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREAT 308
Cdd:cd19539  237 RelakRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKAL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  309 RTLLRHQKMPLGDLLRGASPLFDTtlsyMRWPAAQAI------PNASVET---VAQTHAHDPDALAIW---VSEFDGHSD 376
Cdd:cd19539  317 VDAQRHQELPFQQLVAELPVDRDA----GRHPLVQIVfqvtnaPAGELELaggLSYTEGSDIPDGAKFdlnLTVTEEGTG 392

                        410       420       430
                 ....*....|....*....|....*....|....
gi 15598523  377 AQVDFEYACDVFDADFpMDAAARHIETFLRALVE 410
Cdd:cd19539  393 LRGSLGYATSLFDEET-IQGFLADYLQVLRQLLA 425
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 1497-1947 1.74e-35

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: 144.35  E-value: 1.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1497 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDV--SYPAQRLAL-----ILE 1569
Cdd:cd05906   36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVppTYDEPNARLrklrhIWQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1570 TAQPFRVVAHPE-HAHVAAAE--------RVLPVEELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANY 1640
Cdd:cd05906  116 LLGSPVVLTDAElVAEFAGLEtlsglpgiRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILAR 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1641 TQWQLRVASGVPGLRTLQFAPLSFDMAFQE--IFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLA 1718
Cdd:cd05906  196 SAGKIQHNGLTPQDVFLNWVPLDHVGGLVElhLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLN 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1719 EASNALGVRPG---ALRVVVSSGEQLritedVRAFCAAMPGLLLENQ---------YGPTET-HQVTYHSLSGDPAHYPD 1785
Cdd:cd05906  276 DLLEEIEDGTWdlsSLRYLVNAGEAV-----VAKTIRRLLRLLEPYGlppdairpaFGMTETcSGVIYSRSFPTYDHSQA 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1786 LP--PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGrILGNGE 1863
Cdd:cd05906  351 LEfvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGN 423

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1864 IVWLGRADTQVKVRGFRIEPAEVELAIMRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSEL-- 1941
Cdd:cd05906  424 LTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVsr 503

                        490
                 ....*....|.
gi 15598523 1942 -----PEHMVP 1947
Cdd:cd05906  504 evgvsPAYLIP 514
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 586-937 1.88e-35

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: 140.21  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  586 GDLAYVIYTSGSTGMPKGVMVEHRSVVNRL--------------NWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFT 651
Cdd:cd05924    3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLmggadfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  652 GARLSLlpPGAEKDPREMLRSIQRDAVTVIHFV-PSMLTPFLDLLDGDPTAraAASSLRLVFCSGEALAPLQVARFRRLF 730
Cdd:cd05924   83 GQTVVL--PDDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPY--DLSSLFAISSGGALLSPEVKQGLLELV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  731 GDAVrLVNLYGPTEATVDVSDHECASDNPTRVPIGRpidNLRLYVLDRALRPQPLGAVGELYIGGVG-VARGYLNRPELN 809
Cdd:cd05924  159 PNIT-LVDAFGSSETGFTGSGHSAGSGPETGPFTRA---NPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKT 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  810 AERFlvdPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLV 889
Cdd:cd05924  235 AETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 15598523  890 GYYVA--AAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRR 937
Cdd:cd05924  312 AVVQLreGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 461-939 2.29e-35

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: 141.85  E-value: 2.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  461 RTALLeADGGTLSYAELDAKVQAVADALRAAGV-RTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLL 539
Cdd:cd05958    1 RTCLR-SPEREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  540 EDCGARVVLVDERaatlgeslgetrvlhlerlpQSTGDlpaanvapgDLAYVIYTSGSTGMPKGVMVEHRSVVNrlnwMQ 619
Cdd:cd05958   80 DKARITVALCAHA--------------------LTASD---------DICILAFTSGTTGAPKATMHFHRDPLA----SA 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  620 RRYPIG-----ERDVLLQKTPV--TFDVSVWELFWWSfTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLTPFL 692
Cdd:cd05958  127 DRYAVNvlrlrEDDRFVGSPPLafTFGLGGVLLFPFG-VGASGVLLE---EATPDLLLSAIARYKPTVLFTAPTAYRAML 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  693 DLLDgdpTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATvdvsdHECASDNPTRVPIGR---PID 769
Cdd:cd05958  203 AHPD---AAGPDLSSLRKCVSAGEALPAALHRAWKEATG--IPIIDGIGSTEMF-----HIFISARPGDARPGAtgkPVP 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  770 NLRLYVLDRALRPQPLGAVGELYIGGvgvARGYlnrpelnaeRFLVDP----FVAGGRLYrTGDLARWLADGNLEYLGRA 845
Cdd:cd05958  273 GYEAKVVDDEGNPVPDGTIGRLAVRG---PTGC---------RYLADKrqrtYVQGGWNI-TGDTYSRDPDGYFRHQGRS 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  846 DDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPG-----QLRAGLSATLPDFMLPAFF 920
Cdd:cd05958  340 DDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlarELQDHAKAHIAPYKYPRAI 419

                        490
                 ....*....|....*....
gi 15598523  921 VRIDSLPLSANGKLDRRQL 939
Cdd:cd05958  420 EFVTELPRTATGKLQRFAL 438
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 1478-1963 4.65e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 143.60  E-value: 4.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1478 VSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCV---P 1554
Cdd:PRK05605   35 VDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1555 LdvsYPAQRLALILE----------------------TAQPFRVV------AHPEHAHVA-----------------AAE 1589
Cdd:PRK05605  115 L---YTAHELEHPFEdhgarvaivwdkvaptverlrrTTPLETIVsvnmiaAMPLLQRLAlrlpipalrkaraaltgPAP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1590 RVLPVEELVADIEP-----ETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQ---WqlrvasgVPGL-----R 1655
Cdd:PRK05605  192 GTVPWETLVDAAIGgdgsdVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRnLFANAAQgkaW-------VPGLgdgpeR 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1656 TLQFAPLsfdmaFQEIFSTLCG------GGELQLISnreRMDPSALLHVLERRQVqrVLLPFVA--LQRLAEASNALGVR 1727
Cdd:PRK05605  265 VLAALPM-----FHAYGLTLCLtlavsiGGELVLLP---APDIDLILDAMKKHPP--TWLPGVPplYEKIAEAAEERGVD 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1728 PGALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENqYGPTETHQVtyhsLSGDPAHyPDLPP--IGRPLDGVEVQVLDA-- 1803
Cdd:PRK05605  335 LSGVRNAFSGAMALP-VSTVELWEKLTGGLLVEG-YGLTETSPI----IVGNPMS-DDRRPgyVGVPFPDTEVRIVDPed 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1804 ALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEP 1883
Cdd:PRK05605  408 PDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-W------FRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYP 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1884 AEVELAImrqaERQPGLRGAAVVARERQ-GNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 1962
Cdd:PRK05605  481 AEVEEVL----REHPGVEDAAVVGLPREdGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLG 556


                  .
gi 15598523  1963 K 1963
Cdd:PRK05605  557 K 557
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 447-942 4.84e-35

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 141.67  E-value: 4.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   447 LPTLFAEQVARTPQRTALLEADGGTLSYAELDAKVQAVADALRAAGvrtdeRVALLVARGPHLLPAILGVQRAGGAYVPI 526
Cdd:PRK07787    1 LASLNPAAVAAAADIADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   527 NPDHPLERVRLLLEDCGARVVLVDERAATLGeslgetrvlhLERLPQST---GDLPAANVAPGDLAYVIYTSGSTGMPKG 603
Cdd:PRK07787   76 PPDSGVAERRHILADSGAQAWLGPAPDDPAG----------LPHVPVRLharSWHRYPEPDPDAPALIVYTSGTTGPPKG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   604 VMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtFDVSvwelfwwsftGARLSLLPP---------GAEKDPREMLRSIQ 674
Cdd:PRK07787  146 VVLSRRAIAADLDALAEAWQWTADDVLVHGLPL-FHVH----------GLVLGVLGPlrignrfvhTGRPTPEAYAQALS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   675 RDAvTVIHFVPSMLTPfldlLDGDPTARAAASSLRLVfCSGEALAPLQV-ARFRRLFGDAVrlVNLYGPTEATVDVSDHE 753
Cdd:PRK07787  215 EGG-TLYFGVPTVWSR----IAADPEAARALRGARLL-VSGSAALPVPVfDRLAALTGHRP--VERYGMTETLITLSTRA 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   754 CASDNPTRVpiGRPIDNLRLYVLDRALRPQPLG--AVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLA 831
Cdd:PRK07787  287 DGERRPGWV--GLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVA 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   832 RWLADGNLEYLGR-ADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSAT 910
Cdd:PRK07787  359 VVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQ 438

                         490       500       510
                  ....*....|....*....|....*....|..
gi 15598523   911 LPDFMLPAFFVRIDSLPLSANGKLDRRQLPAP 942
Cdd:PRK07787  439 LSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 1493-1970 7.58e-35

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: 140.29  E-value: 7.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1493 ALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ 1572
Cdd:cd05919    3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1573 PFRVVAHPehahvaaaervlpveelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGV- 1651
Cdd:cd05919   83 ARLVVTSA-------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLt 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1652 PGLRTLQFAPLSF--DMAFQEIFSTLCGGgelQLISNRERMDPSALLHVLERRQvQRVL--LP--FVALQRLAEASNALG 1725
Cdd:cd05919  132 PGDRVFSSAKMFFgyGLGNSLWFPLAVGA---SAVLNPGWPTAERVLATLARFR-PTVLygVPtfYANLLDSCAGSPDAL 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1726 VrpgALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTyhsLSGDPAHYpDLPPIGRPLDGVEVQVLDAAL 1805
Cdd:cd05919  208 R---SLRLCVSAGEAL--PRGLGERWMEHFGGPILDGIGATEVGHIF---LSNRPGAW-RLGSTGRPVPGYEIRLVDEEG 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1806 RPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAE 1885
Cdd:cd05919  279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-W------YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1886 VELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVD---LAE-LKQALRSELPEHMVPAHFAWVDGFALTPS 1961
Cdd:cd05919  352 VESLII----QHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPqesLARdIHRHLLERLSAHKVPRRIAFVDELPRTAT 427


                 ....*....
gi 15598523 1962 GKRDDAALR 1970
Cdd:cd05919  428 GKLQRFKLR 436
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 442-939 9.02e-35

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: 142.04  E-value: 9.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  442 PEQATLPTLFAEQVARTPQRTAL-----LEADGG--TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAIL 514
Cdd:cd05906    3 HRPEGAPRTLLELLLRAAERGPTkgityIDADGSeeFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  515 GVQRAGGAYVPINP-------DHPLERVRLLLEDCGARVVLVDERAATLGESLGET------RVLHLERLPQSTGDLPAA 581
Cdd:cd05906   83 ACVLAGFVPAPLTVpptydepNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLsglpgiRVLSIEELLDTAADHDLP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  582 NVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRL---NWMQRRypiGERDVLLQKTPVTFDVSVWELFWWS-FTGARLSL 657
Cdd:cd05906  163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSagkIQHNGL---TPQDVFLNWVPLDHVGGLVELHLRAvYLGCQQVH 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  658 LPPGAE-KDPREMLRSIQRDAVTvIHFVPS-MLTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRL---FG- 731
Cdd:cd05906  240 VPTEEIlADPLRWLDLIDRYRVT-ITWAPNfAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLlepYGl 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  732 --DAVRLVnlYGPTE----ATVDVSDHECASDNPTR-VPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLN 804
Cdd:cd05906  319 ppDAIRPA--FGMTEtcsgVIYSRSFPTYDHSQALEfVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYN 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  805 RPELNAERFLVDPFvaggrlYRTGDLArWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRD--AAVVARDSA 882
Cdd:cd05906  397 NPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDP 469

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523  883 VRGT-HLVGYYVAAAELDPG---QLRA-----GLSATL-PDFMLPaffVRIDSLPLSANGKLDRRQL 939
Cdd:cd05906  470 GAETeELAIFFVPEYDLQDAlseTLRAirsvvSREVGVsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 1477-1971 9.19e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 141.58  E-value: 9.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1477 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 1556
Cdd:PRK07656    7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1557 VSYPAQRLALILET--------AQPF---------------RVVAHPEHAHVAAAERVLPVEELVADIEPETFAAP-QLD 1612
Cdd:PRK07656   87 TRYTADEAAYILARgdakalfvLGLFlgvdysattrlpaleHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEvDPD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1613 ELAMLLFTSGSTGRPKGVELSHR-MWANYTQW----QLRvasgvPGLRTLQFAPLsfdmafqeiFSTLC-GGGELQLISN 1686
Cdd:PRK07656  167 DVADILFTSGTTGRPKGAMLTHRqLLSNAADWaeylGLT-----EGDRYLAANPF---------FHVFGyKAGVNAPLMR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1687 RERM------DPSALLHVLERRQVqrVLLPFVA------LQRLAEASNALgvrpGALRVVVSSGeqlritedvrafcAAM 1754
Cdd:PRK07656  233 GATIlplpvfDPDEVFRLIETERI--TVLPGPPtmynslLQHPDRSAEDL----SSLRLAVTGA-------------ASM 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1755 PGLLLEN------------QYGPTETHQVTYHSLSGDPAHypDLP-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGD 1821
Cdd:PRK07656  294 PVALLERfeselgvdivltGYGLSEASGVTTFNRLDDDRK--TVAgTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGP 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1822 CLARGYHRAPKLTAERFVEHPWrpgarLYrTGDLGRI--LGNGEIVwlGRADTQVKVRGFRIEPAEVELAIMrqaeRQPG 1899
Cdd:PRK07656  372 NVMKGYYDDPEATAAAIDADGW-----LH-TGDLGRLdeEGYLYIV--DRKKDMFIVGGFNVYPAEVEEVLY----EHPA 439

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523  1900 LRGAAV--VARERQGnDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 1971
Cdd:PRK07656  440 VAEAAVigVPDERLG-EVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 1527-1969 1.46e-34

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: 139.53  E-value: 1.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1527 AIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAhpehahvaaaERVLPVEELVADIEPETF 1606
Cdd:cd17654   43 AIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQ----------NKELDNAPLSFTPEHRHF 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1607 AAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQwQLRVASGVPGLRTLQFA-PLSFDMAFQEIFSTLCGGGELQLIS 1685
Cdd:cd17654  113 NIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQ-HFRSLFNITSEDILFLTsPLTFDPSVVEIFLSLSSGATLLIVP 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1686 NRERMDPSALLHVL-ERRQVQRVLLPFVALQRLAEASNALGV--RPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQ 1762
Cdd:cd17654  192 TSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPFPSLVILSSWRGKGNRTRIFNI 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1763 YGPTETH--QVTYHSLSGDpahypdLP-PIGRPLDGVEVQVLDAALRPVpvgvTGELYFGGdcLARGYHRAPKLTaerfv 1839
Cdd:cd17654  272 YGITEVScwALAYKVPEED------SPvQLGSPLLGTVIEVRDQNGSEG----TGQVFLGG--LNRVCILDDEVT----- 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1840 ehpwRPGARLYRTGDLGRIlGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARERQGndafLAA 1919
Cdd:cd17654  335 ----VPKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQ----QVIESCLGVESCAVTLSDQQR----LIA 401

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15598523 1920 FLLGEPEAvdlAELKQALRSE-LPEHMVPAHFAWVDGFALTPSGKRDDAAL 1969
Cdd:cd17654  402 FIVGESSS---SRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 456-939 2.07e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 141.25  E-value: 2.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   456 ARTPQRTALLEAdGGTLSYAELDAKVQAVADAL-RAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLER 534
Cdd:PRK08314   21 RRYPDKTAIVFY-GRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   535 VRLLLEDCGARVVLV-DERAATLGESLGETRVLHL------ERLPQSTGDLP-------------------------AAN 582
Cdd:PRK08314  100 LAHYVTDSGARVAIVgSELAPKVAPAVGNLRLRHVivaqysDYLPAEPEIAVpawlraepplqalapggvvawkealAAG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   583 VAPG-------DLAYVIYTSGSTGMPKGVMVEHRSV----VNRLNWMQrrypIGERDVLLQKTPVtFDVS--VWELFWWS 649
Cdd:PRK08314  180 LAPPphtagpdDLAVLPYTSGTTGVPKGCMHTHRTVmanaVGSVLWSN----STPESVVLAVLPL-FHVTgmVHSMNAPI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   650 FTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLTPFLdlldGDPT-ARAAASSLRLVFCSGEALaPLQVA-RFR 727
Cdd:PRK08314  255 YAGATVVLMP---RWDREAAARLIERYRVTHWTNIPTMVVDFL----ASPGlAERDLSSLRYIGGGGAAM-PEAVAeRLK 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   728 RLFGdaVRLVNLYGPTEaTVDVSdHECASDNPTRVPIGRPIDNLRLYVLD-RALRPQPLGAVGELYIGGVGVARGYLNRP 806
Cdd:PRK08314  327 ELTG--LDYVEGYGLTE-TMAQT-HSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRP 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   807 ELNAERFLVdpfVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGT 886
Cdd:PRK08314  403 EATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGE 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523   887 HLVGYYV----AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK08314  480 TVKAVVVlrpeARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 451-961 2.24e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 141.07  E-value: 2.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   451 FAEQVAR----TPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPI 526
Cdd:PRK07786   19 WVNQLARhalmQPDAPAL-RFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   527 NPDHPLERVRLLLEDCGARVVL-----------VDERAATLGESL-----GETRVLHLERLPQSTGDLPAANVAPGDL-A 589
Cdd:PRK07786   98 NFRLTPPEIAFLVSDCGAHVVVteaalapvataVRDIVPLLSTVVvaggsSDDSVLGYEDLLAEAGPAHAPVDIPNDSpA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   590 YVIYTSGSTGMPKGVMVEHRSVVNRLNWMQR--RYPIGErDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAeKDPR 667
Cdd:PRK07786  178 LIMYTSGTTGRPKGAVLTHANLTGQAMTCLRtnGADINS-DVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGA-FDPG 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   668 EMLRSIQRDAVTVIHFVPSMLTPFLDlldgDPTARAAASSLRlVFCSGEALAPLQVAR-FRRLFGDAvRLVNLYGPTEat 746
Cdd:PRK07786  256 QLLDVLEAEKVTGIFLVPAQWQAVCA----EQQARPRDLALR-VLSWGAAPASDTLLRqMAATFPEA-QILAAFGQTE-- 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   747 vdVSDHECASDNPTRV----PIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlvdpfvAGG 822
Cdd:PRK07786  328 --MSPVTCMLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   823 rLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV---AAAELD 899
Cdd:PRK07786  400 -WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAvrnDDAALT 478

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598523   900 PGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLpapPEQVAAVAPRTATEAELAA 961
Cdd:PRK07786  479 LEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL---RERYGACVNVERRSASAGF 537
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 432-939 2.43e-34

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 141.06  E-value: 2.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   432 HTRNATDQAFPEQaTLPTLFAEQVARTPQRTALLEADGGT-LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLL 510
Cdd:PRK12583    6 YYQGGGDKPLLTQ-TIGDAFDATVARFPDREALVVRHQALrYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   511 PAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDER------AATLGE-----SLGETRVLHLERLPQSTGDLP 579
Cdd:PRK12583   85 LTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAfktsdyHAMLQEllpglAEGQPGALACERLPELRGVVS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   580 -AANVAPGDLAY-----------------------------VIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDV 629
Cdd:PRK12583  165 lAPAPPPGFLAWhelqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   630 LLQKTPV--TFDVSVWELFWWSfTGArlSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMltpFLDLLDGDPTARAAASS 707
Cdd:PRK12583  245 LCVPVPLyhCFGMVLANLGCMT-VGA--CLVYPNEAFDPLATLQAVEEERCTALYGVPTM---FIAELDHPQRGNFDLSS 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   708 LRLVFCSGealAPLQVARFRRLFGD--AVRLVNLYGPTEATvDVSDHECASDN-PTRV-PIGRPIDNLRLYVLDRALRPQ 783
Cdd:PRK12583  319 LRTGIMAG---APCPIEVMRRVMDEmhMAEVQIAYGMTETS-PVSLQTTAADDlERRVeTVGRTQPHLEVKVVDPDGATV 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   784 PLGAVGELYIGGVGVARGYLNRPELNAERFLVDpfvagGRLYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRD 863
Cdd:PRK12583  395 PRGEIGELCTRGYSVMKGYWNNPEATAESIDED-----GWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEE 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   864 RLAALPGVRDAAVVARDSAVRGTHLvgyyVAAAELDPGQ------LRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRR 937
Cdd:PRK12583  469 FLFTHPAVADVQVFGVPDEKYGEEI----VAWVRLHPGHaaseeeLREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKF 544


                  ..
gi 15598523   938 QL 939
Cdd:PRK12583  545 RM 546
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 1480-1965 2.77e-34

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 140.41  E-value: 2.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1480 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1560 PAQRLALILETAQPFRVVAH-----------PEHAHVAAAERV------------LPVEELVADIEPET-FAAPQLDELa 1615
Cdd:PRK07798   88 VEDELRYLLDDSDAVALVYErefaprvaevlPRLPKLRTLVVVedgsgndllpgaVDYEDALAAGSPERdFGERSPDDL- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1616 MLLFTSGSTGRPKGVelshrMW------------ANY-------TQWQL--RVASGvPGLRTLQFAPLSFDMAFQEIFST 1674
Cdd:PRK07798  167 YLLYTGGTTGMPKGV-----MWrqedifrvllggRDFatgepieDEEELakRAAAG-PGMRRFPAPPLMHGAGQWAAFAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1675 LCGGGELQLISNReRMDPSALLHVLERRQVQRVLLPFVALQR--LAEASNALGVRPGALRVVVSSGEQLriTEDVR-AFC 1751
Cdd:PRK07798  241 LFSGQTVVLLPDV-RFDADEVWRTIEREKVNVITIVGDAMARplLDALEARGPYDLSSLFAIASGGALF--SPSVKeALL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1752 AAMPGLLLENQYGPTEThQVTYHSLSGDPAHYPDLPPIGRpldGVEVQVLDAALRPVPVGvTGELYFggdcLAR------ 1825
Cdd:PRK07798  318 ELLPNVVLTDSIGSSET-GFGGSGTVAKGAVHTGGPRFTI---GPRTVVLDEDGNPVEPG-SGEIGW----IARrghipl 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1826 GYHRAPKLTAERFVEHpwrPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAV 1905
Cdd:PRK07798  389 GYYKDPEKTAETFPTI---DGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEAL----KAHPDVADALV 461

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598523  1906 VAR--ERQGNdAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 1965
Cdd:PRK07798  462 VGVpdERWGQ-EVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
438-937 6.37e-34

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 139.64  E-value: 6.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   438 DQAFPEQATLPTLFA---EQVARTPQRTALL-EADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAI 513
Cdd:PRK05852    6 GAAPMASDFGPRIADlveVAATRLPEAPALVvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   514 LGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD-----ERAA----------TLGESLGETRVLHLERLPQSTGDL 578
Cdd:PRK05852   86 LAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDadgphDRAEpttrwwpltvNVGGDSGPSGGTLSVHLDAATEPT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   579 PAANVAPG---DLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARL 655
Cdd:PRK05852  166 PATSTPEGlrpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   656 SLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARAAAsSLRLVFCSGEALAPLQVARFRRLFGDAVr 735
Cdd:PRK05852  246 VLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPA-ALRFIRSCSAPLTAETAQALQTEFAAPV- 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   736 lVNLYGPTEATVDVS----DHECASDNPTRV--PIGRPiDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELN 809
Cdd:PRK05852  324 -VCAFGMTEATHQVTttqiEGIGQTENPVVStgLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTIT 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   810 AERFlvdpfvAGGRLyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLV 889
Cdd:PRK05852  402 AANF------TDGWL-RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVA 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 15598523   890 GYYV--AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRR 937
Cdd:PRK05852  475 AVIVprESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 593-939 7.85e-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: 135.10  E-value: 7.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  593 YTSGSTGMPKGVMVEHRSVVNrlnwmqRRYPIGERDVLLQKTPVTFDVSVWELFwwsftGARLSLL----------PPGA 662
Cdd:cd05917    9 FTSGTTGSPKGATLTHHNIVN------NGYFIGERLGLTEQDRLCIPVPLFHCF-----GSVLGVLaclthgatmvFPSP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  663 EKDPREMLRSIQRDAVTVIHFVPSMltpFLDLLDGDPTARAAASSLRLVFCSGealAPLQVARFRRLFGD--AVRLVNLY 740
Cdd:cd05917   78 SFDPLAVLEAIEKEKCTALHGVPTM---FIAELEHPDFDKFDLSSLRTGIMAG---APCPPELMKRVIEVmnMKDVTIAY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  741 GPTEATVDVSDHECASDNPTRV-PIGRPIDNLRLYVLDRALRPQP-LGAVGELYIGGVGVARGYLNRPELNAERFLVDpf 818
Cdd:cd05917  152 GMTETSPVSTQTRTDDSIEKRVnTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD-- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  819 vaggRLYRTGDLARWLADGNLEYLGRADDQVkIRGNR-VEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV--AA 895
Cdd:cd05917  230 ----GWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRlkEG 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 15598523  896 AELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05917  305 AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
PRK07529 PRK07529
AMP-binding domain protein; Validated
 445-1005 1.50e-33

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 139.71  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   445 ATLPTLFAEQVARTPQRTAL---LEADGG----TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQ 517
Cdd:PRK07529   25 ASTYELLSRAAARHPDAPALsflLDADPLdrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   518 RAGGAyVPINPDHPLERVRLLLEDCGARV-----------------------------VLVDER---------AATLGES 559
Cdd:PRK07529  105 AAGIA-NPINPLLEPEQIAELLRAAGAKVlvtlgpfpgtdiwqkvaevlaalpelrtvVEVDLArylpgpkrlAVPLIRR 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   560 LGETRVLHLERL--PQSTGDLPAA-NVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPV 636
Cdd:PRK07529  184 KAHARILDFDAElaRQPGDRLFSGrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   637 --TFDVSVWELFWWSfTGARLSLLPPGAEKDPREMLR---SIQRDAVTVIHFVPSMLTPFLDLldgdPTARAAASSLRLV 711
Cdd:PRK07529  264 fhVNALLVTGLAPLA-RGAHVVLATPQGYRGPGVIANfwkIVERYRINFLSGVPTVYAALLQV----PVDGHDISSLRYA 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   712 FCSGealAPLQVARFRRlFGDA--VRLVNLYGPTEATvdvsdheCAS-----DNPTRV-PIGRPI--DNLRLYVLD---R 778
Cdd:PRK07529  339 LCGA---APLPVEVFRR-FEAAtgVRIVEGYGLTEAT-------CVSsvnppDGERRIgSVGLRLpyQRVRVVILDdagR 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   779 ALRPQPLGAVGELYIGGVGVARGYLNrPELNAERFLvdpfvaGGRLYRTGDLARWLADGNLEYLGRADDQVkIR-GNRVE 857
Cdd:PRK07529  408 YLRDCAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNID 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   858 PDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGY--YVAAAELDPGQLRAGLSATLPD-FMLPAFFVRIDSLPLSANGKL 934
Cdd:PRK07529  480 PAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYvqLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKI 559

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523   935 DRRQLpappeqvAAVAPRTATEAELAAVWADvLGVAEVGVHDdfyalGGDSILMLRIRAAAQRRGLGFELA 1005
Cdd:PRK07529  560 FKPAL-------RRDAIRRVLRAALRDAGVE-AEVVDVVEDG-----RRGLVAQVALRGAEDREAVAAVLG 617
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 471-880 2.26e-33

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: 136.19  E-value: 2.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD 550
Cdd:cd05907    5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 EraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVL 630
Cdd:cd05907   85 D---------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  631 LQKTPVT--FDVSVWELFWWSfTGARLSLLPPgaEKDPREMLRSIQRdavTVIHFVPSMLTPFLDL--------LDGDPT 700
Cdd:cd05907  132 LSFLPLAhvFERRAGLYVPLL-AGARIYFASS--AETLLDDLSEVRP---TVFLAVPRVWEKVYAAikvkavpgLKRKLF 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  701 ARAAASSLRLVFCSGEALAPlQVARFRRLFGdaVRLVNLYGPTEATVDVSdhecaSDNPTRVPI---GRPIDNLRLYVld 777
Cdd:cd05907  206 DLAVGGRLRFAASGGAPLPA-ELLHFFRALG--IPVYEGYGLTETSAVVT-----LNPPGDNRIgtvGKPLPGVEVRI-- 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  778 ralrpqplGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAggrlyrTGDLARWLADGNLEYLGRADD-QVKIRGNRV 856
Cdd:cd05907  276 --------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKKDlIITSGGKNI 341

                        410       420
                 ....*....|....*....|....
gi 15598523  857 EPDEVRDRLAALPGVRDAAVVARD 880
Cdd:cd05907  342 SPEPIENALKASPLISQAVVIGDG 365
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 446-939 4.44e-33

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 137.11  E-value: 4.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   446 TLPTLFAEQVARTPQRTAL--LEADGG---TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAG 520
Cdd:PRK13295   25 TINDDLDACVASCPDKTAVtaVRLGTGaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   521 GAYVPINPDHPLERVRLLLEDCGARVVLVDER---------AATLGESL----------GET-----RVL---HLERLPQ 573
Cdd:PRK13295  105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfdhaamARRLRPELpalrhvvvvgGDGadsfeALLitpAWEQEPD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   574 STGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTfdvsvwelfwwSFTGA 653
Cdd:PRK13295  185 APAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMA-----------HQTGF 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   654 RLSLLPP---GAEK------DPREMLRSIQRDAVTVihfvpSML-TPFL-DLLDGDPTARAAASSLRLVFCSGEALAPLQ 722
Cdd:PRK13295  254 MYGLMMPvmlGATAvlqdiwDPARAAELIRTEGVTF-----TMAsTPFLtDLTRAVKESGRPVSSLRTFLCAGAPIPGAL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   723 VARFRRLFGdaVRLVNLYGPTE---ATV----DVSDHECASDnptrvpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGG 795
Cdd:PRK13295  329 VERARAALG--AKIVSAWGMTEngaVTLtkldDPDERASTTD-------GCPLPGVEVRVVDADGAPLPAGQIGRLQVRG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   796 VGVARGYLNRPELNAERflvdpfvAGGrLYRTGDLARWLADGNLEYLGRADDqVKIRGNRVEP-DEVRDRLAALPGVRDA 874
Cdd:PRK13295  400 CSNFGGYLKRPQLNGTD-------ADG-WFDTGDLARIDADGYIRISGRSKD-VIIRGGENIPvVEIEALLYRHPAIAQV 470

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523   875 AVVARDSAVRGTHLVGYYVaaaeldpgqLRAGLSATLP---DFM---------LPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK13295  471 AIVAYPDERLGERACAFVV---------PRPGQSLDFEemvEFLkaqkvakqyIPERLVVRDALPRTPSGKIQKFRL 538
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 461-939 4.52e-33

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 136.19  E-value: 4.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   461 RTALLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLE 540
Cdd:PRK08276    1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   541 DCGARVVLVDERAATLGESLGETRVLHLERLPQSTGDL----------------PAANVAPGDLayVIYTSGSTGMPKGV 604
Cdd:PRK08276   81 DSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVpgfrsyeealaaqpdtPIADETAGAD--MLYSSGTTGRPKGI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   605 MVE--HRSVVNRLNWMQR----RYPIGERDVLLQKTPV------TFDVSVWELfwwsftGARLSLLppgaEK-DPREMLR 671
Cdd:PRK08276  159 KRPlpGLDPDEAPGMMLAllgfGMYGGPDSVYLSPAPLyhtaplRFGMSALAL------GGTVVVM----EKfDAEEALA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   672 SIQRDAVTVIHFVPSMltpFLDLLDGDPTARAA--ASSLRLVFCSGealAPLQVARFRRL---FGDAVrlVNLYGPTEAT 746
Cdd:PRK08276  229 LIERYRVTHSQLVPTM---FVRMLKLPEEVRARydVSSLRVAIHAA---APCPVEVKRAMidwWGPII--HEYYASSEGG 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   747 -VDVSDHECASDNPTRVpiGRPIDNlRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLvdpfvaGGRLY 825
Cdd:PRK08276  301 gVTVITSEDWLAHPGSV--GKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------PHGWV 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   826 RTGDLArWL-ADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVA----------------RDSAVRGTHL 888
Cdd:PRK08276  372 TVGDVG-YLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGvpdeemgervkavvqpADGADAGDAL 450

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15598523   889 vgyyvaAAELDpGQLRAGLSAtlpdFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK08276  451 ------AAELI-AWLRGRLAH----YKCPRSIDFEDELPRTPTGKLYKRRL 490
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 471-939 5.81e-33

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: 134.01  E-value: 5.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINpdhplervrllledcgarvvlvd 550
Cdd:cd05912    1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN----------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 eraatlgeslgeTRVLHLERLPQstgdLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVL 630
Cdd:cd05912   58 ------------TRLTPNELAFQ----LKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNW 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  631 LQKTPVtFDVSvwelfwwsftGarLSLLPPGA---------EK-DPREMLRSIQRDAVTVIHFVPSMLTpflDLLDGDPt 700
Cdd:cd05912  122 LCALPL-FHIS----------G--LSILMRSViygmtvylvDKfDAEQVLHLINSGKVTIISVVPTMLQ---RLLEILG- 184

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  701 aRAAASSLRLVFCSGEALAP--LQVARFRRLfgdavRLVNLYGPTEAT---VDVSdhecASDNPTRV-PIGRPIDNLRLY 774
Cdd:cd05912  185 -EGYPNNLRCILLGGGPAPKplLEQCKEKGI-----PVYQSYGMTETCsqiVTLS----PEDALNKIgSAGKPLFPVELK 254

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  775 VLDRAlrpQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlyRTGDLARWLADGNLEYLGRADDQVKIRGN 854
Cdd:cd05912  255 IEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGE 324

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  855 RVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKL 934
Cdd:cd05912  325 NIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKL 404


                 ....*
gi 15598523  935 DRRQL 939
Cdd:cd05912  405 LRHEL 409
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 1491-1971 8.69e-33

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: 134.34  E-value: 8.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1491 SAALAFEEQRWTYRDLDHVARCVATRLVRAGA-RRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILE 1569
Cdd:cd05941    2 RIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1570 TAQPFRVVahpehahvaaaervlpveelvadiepetfaapqldELAMLLFTSGSTGRPKGVELSHRMWANYTQ-----WQ 1644
Cdd:cd05941   82 DSEPSLVL-----------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRalvdaWR 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1645 LRvasgvPGLRTLQFAPLsFDM--AFQEIFSTLCGGGELQLISnreRMDPSAllhVLERRQVQRVLLpFVAL----QRLA 1718
Cdd:cd05941  127 WT-----EDDVLLHVLPL-HHVhgLVNALLCPLFAGASVEFLP---KFDPKE---VAISRLMPSITV-FMGVptiyTRLL 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1719 EASNA--------LGVRPGALRVVVSSGEQLrITEDVRAFCAAMPGLLLEnQYGPTETHQVTYHSLSGDPahypdLP-PI 1789
Cdd:cd05941  194 QYYEAhftdpqfaRAAAAERLRLMVSGSAAL-PVPTLEEWEAITGHTLLE-RYGMTEIGMALSNPLDGER-----RPgTV 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1790 GRPLDGVEVQVLD-AALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLG 1868
Cdd:cd05941  267 GMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILG 340

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1869 R-ADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVV--ARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHM 1945
Cdd:cd05941  341 RsSVDIIKSGGYKVSALEIERVL----LAHPGVSECAVIgvPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQRLAPYK 416

                        490       500
                 ....*....|....*....|....*.
gi 15598523 1946 VPAHFAWVDGFALTPSGKRDDAALRA 1971
Cdd:cd05941  417 RPRRLILVDELPRNAMGKVNKKELRK 442
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1049-1452 1.47e-32

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: 132.42  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1049 AFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLawDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARSEPl 1128
Cdd:cd19545    1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDI--DLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISW- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1129 ildlrgnpEAGTVLDEHIRQRRFHRYSLQQPgLFLFAaFVREDGLD--LVFSFHHAILDGWSVANLIVALVAAYRGEPLP 1206
Cdd:cd19545   78 --------TESTSLDEYLEEDRAAPMGLGGP-LVRLA-LVEDPDTEryFVWTIHHALYDGWSLPLILRQVLAAYQGEPVP 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1207 GPAPALacHVREELAALASPAAVGYWTGLLEGARMtrldgfgahePQAAQGPASHREALPDGLLER--LKATAAQRGLPL 1284
Cdd:cd19545  148 QPPPFS--RFVKYLRQLDDEAAAEFWRSYLAGLDP----------AVFPPLPSSRYQPRPDATLEHsiSLPSSASSGVTL 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1285 KSLLLAAHCLTLHLFSRSDSVVTGAISNGR--PeLPDADRMVGLFLNTVPVRSEIAGCSwiEVADALFRQERDGHAHRRY 1362
Cdd:cd19545  216 ATVLRAAWALVLSRYTGSDDVVFGVTLSGRnaP-VPGIEQIVGPTIATVPLRVRIDPEQ--SVEDFLQTVQKDLLDMIPF 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1363 PLSAIQQI--VGDELSSAFNYVNLHVLEP-----LWQLRDFRVWEE-------TNFALLVnVIATPSDGMYLRIDSDGRG 1428
Cdd:cd19545  293 EHTGLQNIrrLGPDARAACNFQTLLVVQPalpssTSESLELGIEEEsedledfSSYGLTL-ECQLSGSGLRVRARYDSSV 371

                        410       420
                 ....*....|....*....|....
gi 15598523 1429 ISRSQAALIGATFVELLWRLADHP 1452
Cdd:cd19545  372 ISEEQVERLLDQFEHVLQQLASAP 395
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 403-941 4.54e-32

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 133.58  E-value: 4.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   403 TFLRALVeggerRLGELDPLSAAEREELIHtrnatdQAFPEQATLPTLFAEQVARTPQRTALLEaDGGTLSYAELDAKVQ 482
Cdd:PRK13383    4 TAARALV-----RSGLLNPPSPRAVLRLLR------EASRGGTNPYTLLAVTAARWPGRTAIID-DDGALSYRELQRATE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   483 AVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD----ERAATLGE 558
Cdd:PRK13383   72 SLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADnefaERIAGADD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   559 SlgetrVLHLERLPQSTGDLPA--ANVAPGDLayVIYTSGSTGMPKGV--MVEHRSVVN-RLNWMQR-RYPIGERDVLlq 632
Cdd:PRK13383  152 A-----VAVIDPATAGAEESGGrpAVAAPGRI--VLLTSGTTGKPKGVprAPQLRSAVGvWVTILDRtRLRTGSRISV-- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   633 KTPVTFDVSVWELFWW-SFTGARLSLLPPGAEKDPREMlrSIQR-DAVTVihfVPSMLTPFLDLLDgDPTARAAASSLRL 710
Cdd:PRK13383  223 AMPMFHGLGLGMLMLTiALGGTVLTHRHFDAEAALAQA--SLHRaDAFTA---VPVVLARILELPP-RVRARNPLPQLRV 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   711 VFCSGEALAPLQVARFRRLFGDAvrLVNLYGPTEATVD-VSDHECASDNPTRVpiGRPIDNLRLYVLDRALRPQPLGAVG 789
Cdd:PRK13383  297 VMSSGDRLDPTLGQRFMDTYGDI--LYNGYGSTEVGIGaLATPADLRDAPETV--GKPVAGCPVRILDRNNRPVGPRVTG 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   790 ELYIGGvgvargylnrpELNAERFLVdpfvAGGR-----LYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDR 864
Cdd:PRK13383  373 RIFVGG-----------ELAGTRYTD----GGGKavvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENA 437

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523   865 LAALPGVRDAAVVARDSAVRGTHLVGYYVA--AAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPA 941
Cdd:PRK13383  438 LAAHPAVADNAVIGVPDERFGHRLAAFVVLhpGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 440-932 6.09e-32

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 133.33  E-value: 6.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   440 AFPEQATLPTLFAEQVARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRA 519
Cdd:PRK06164    5 AAPRADTLASLLDAHARARPDAVALID-EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   520 GGAYVPINPDHPLERVRLLLEDCGARVV------------------------------LVDERAATLGESLGETRVLHLE 569
Cdd:PRK06164   84 GATVIAVNTRYRSHEVAHILGRGRARWLvvwpgfkgidfaailaavppdalpplraiaVVDDAADATPAPAPGARVQLFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   570 RLPQSTGDLPAANVAPGDLAYVIY-TSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWW 648
Cdd:PRK06164  164 LPDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   649 SFTGARLSLLPPgaeKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGdptaRAAASSLRLV----FCSGEA-LAPLQV 723
Cdd:PRK06164  244 LAGGAPLVCEPV---FDAARTARALRRHRVTHTFGNDEMLRRILDTAGE----RADFPSARLFgfasFAPALGeLAALAR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   724 ARfrrlfgdAVRLVNLYGPTEATVDVSDHECASDNPTR-VPIGRPIdnlRLYVLDRALRPQ-----PLGAVGELYIGGVG 797
Cdd:PRK06164  317 AR-------GVPLTGLYGSSEVQALVALQPATDPVSVRiEGGGRPA---SPEARVRARDPQdgallPDGESGEIEIRAPS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   798 VARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVV 877
Cdd:PRK06164  387 LMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVV 460

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598523   878 ARDSAvrgthlvGYYVAAA--------ELDPGQLRAGLSATLPDFMLPAFFVRIDSLP--LSANG 932
Cdd:PRK06164  461 GATRD-------GKTVPVAfviptdgaSPDEAGLMAACREALAGFKVPARVQVVEAFPvtESANG 518
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1050-1452 6.49e-32

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: 130.50  E-value: 6.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1050 FPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLawDEAAFRHALDRVVAAYPALRSSFDLSGASEPL-QLVHtqARSEPL 1128
Cdd:cd19542    2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSV--DVERLRNAWRQLVQRHDILRTVFVESSAEGTFlQVVL--KSLDPP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1129 ILDLRGNPEAgtvLDEHIRQrrFHRYSLQQPGLFLFAAFVR--EDGLDLVFSFHHAILDGWSVANLIVALVAAYRGEPLP 1206
Cdd:cd19542   78 IEEVETDEDS---LDALTRD--LLDDPTLFGQPPHRLTLLEtsSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1207 gPAPALACHVReELAALASPAAVGYWTGLLEGARMTrldgfgaHEPQAAQGPASHRE-ALPDGLLERLKATAAQRGLPLK 1285
Cdd:cd19542  153 -PAPPFSDYIS-YLQSQSQEESLQYWRKYLQGASPC-------AFPSLSPKRPAERSlSSTRRSLAKLEAFCASLGVTLA 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1286 SLLLAAHCLTLHLFSRSDSVVTGAISNGR--PeLPDADRMVGLFLNTVPVRSEIAgCSW--IEVADALFRQERDGHAHRR 1361
Cdd:cd19542  224 SLFQAAWALVLARYTGSRDVVFGYVVSGRdlP-VPGIDDIVGPCINTLPVRVKLD-PDWtvLDLLRQLQQQYLRSLPHQH 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1362 YPLSAIQQIVGDELS-----SAFNYVNL--HVLEPLWQLRDFRVWEETN---FALLVNVIATPsDGMYLRIDSDGRGISR 1431
Cdd:cd19542  302 LSLREIQRALGLWPSgtlfnTLVSYQNFeaSPESELSGSSVFELSAAEDpteYPVAVEVEPSG-DSLKVSLAYSTSVLSE 380

                        410       420
                 ....*....|....*....|.
gi 15598523 1432 SQAALIGATFVELLWRLADHP 1452
Cdd:cd19542  381 EQAEELLEQFDDILEALLANP 401
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 1486-1970 9.94e-32

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: 132.49  E-value: 9.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1486 EALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA 1565
Cdd:cd05959   15 EGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1566 LILETAQPFRVVAHPEHAHVAAAE--------RVLPV-------------EELVADIEPETFAAP-QLDELAMLLFTSGS 1623
Cdd:cd05959   95 YYLEDSRARVVVVSGELAPVLAAAltksehtlVVLIVsggagpeagalllAELVAAEAEQLKPAAtHADDPAFWLYSSGS 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1624 TGRPKGVELSHR----MWANYTQWQLRVASGVPGLRT--LQFA-----PLSFDMAFqeifstlcgGGELQLISnrERMDP 1692
Cdd:cd05959  175 TGRPKGVVHLHAdiywTAELYARNVLGIREDDVCFSAakLFFAyglgnSLTFPLSV---------GATTVLMP--ERPTP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1693 SALLHVLERRQvqrvllP--FVALQRLaeaSNALGVRPGA-------LRVVVSSGEQLriTEDVRAFCAAMPGLLLENQY 1763
Cdd:cd05959  244 AAVFKRIRRYR------PtvFFGVPTL---YAAMLAAPNLpsrdlssLRLCVSAGEAL--PAEVGERWKARFGLDILDGI 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1764 GPTETHQVTYHSLSGDpAHYPDlppIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFvEHPW 1843
Cdd:cd05959  313 GSTEMLHIFLSNRPGR-VRYGT---TGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEW 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1844 rpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLL- 1922
Cdd:cd05959  388 ------TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALV----QHPAVLEAAVVGVEDEDGLTKPKAFVVl 457

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15598523 1923 ---GEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd05959  458 rpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1502-1970 1.52e-31

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: 130.33  E-value: 1.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1502 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVahpe 1581
Cdd:cd05973    2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1582 hahVAAAERvlpveelvADIEPETFaapqldelaMLLFTSGSTGRPKGVELSHRM---WANYTQWQLRVASG-------- 1650
Cdd:cd05973   78 ---TDAANR--------HKLDSDPF---------VMMFTSGTTGLPKGVPVPLRAlaaFGAYLRDAVDLRPEdsfwnaad 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1651 ---VPGLRTLQFAPLSFDMAfqeifSTLCGGGelqlisnrerMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVR 1727
Cdd:cd05973  138 pgwAYGLYYAITGPLALGHP-----TILLEGG----------FSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPAR 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1728 P-GALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQV--TYHSLsGDPAHYPDLppiGRPLDGVEVQVLDAA 1804
Cdd:cd05973  203 PkGRLRRVSSAGEPL--TPEVIRWFDAALGVPIHDHYGQTELGMVlaNHHAL-EHPVHAGSA---GRAMPGWRVAVLDDD 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1805 LRPVPVGVTGELyfggdclARGYHRAPKLTAERFVEHPWR-PGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEP 1883
Cdd:cd05973  277 GDELGPGEPGRL-------AIDIANSPLMWFRGYQLPDTPaIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1884 AEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLL------GEPEAVDlaELKQALRSELPEHMVPAHFAWVDGFA 1957
Cdd:cd05973  350 FDVESALI----EHPAVAEAAVIGVPDPERTEVVKAFVVlrggheGTPALAD--ELQLHVKKRLSAHAYPRTIHFVDELP 423

                        490
                 ....*....|...
gi 15598523 1958 LTPSGKRDDAALR 1970
Cdd:cd05973  424 KTPSGKIQRFLLR 436
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 466-935 5.09e-31

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: 129.76  E-value: 5.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  466 EADGGTLSYAELDAKVQAVADALRAaGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGAR 545
Cdd:cd05909    2 DTLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  546 VVLVDERAATLGESLG------ETRVLHLERLPQ--STGD------------------LPAANVAPGDLAYVIYTSGSTG 599
Cdd:cd05909   81 TVLTSKQFIEKLKLHHlfdveyDARIVYLEDLRAkiSKADkckaflagkfppkwllriFGVAPVQPDDPAVILFTSGSEG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  600 MPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtFDVsvwelfwWSFTGARLSLLPPGAE-------KDPREMLRS 672
Cdd:cd05909  161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPF-FHS-------FGLTGCLWLPLLSGIKvvfhpnpLDYKKIPEL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  673 IQRDAVTVIHFVPSMLTPFldlldgdptARAAA----SSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVD 748
Cdd:cd05909  233 IYDKKATILLGTPTFLRGY---------ARAAHpedfSSLRLVVAGAEKLKDTLRQEFQEKFG--IRILEGYGTTECSPV 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  749 VSdheCASDNPTRVP--IGRPIDNLRLYVLDRA-LRPQPLGAVGELYIGGVGVARGYLNRPELNAerflvdpFVAGGRLY 825
Cdd:cd05909  302 IS---VNTPQSPNKEgtVGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWY 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  826 RTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRL-AALPGVRDAAVVARDSAVRGTHLVGYYVaAAELDPGQLR 904
Cdd:cd05909  372 DTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVAVVSVPDGRKGEKIVLLTT-TTDTDPSSLN 450

                        490       500       510
                 ....*....|....*....|....*....|..
gi 15598523  905 AGL-SATLPDFMLPAFFVRIDSLPLSANGKLD 935
Cdd:cd05909  451 DILkNAGISNLAKPSYIHQVEEIPLLGTGKPD 482
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 472-936 5.83e-31

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: 128.79  E-value: 5.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDe 551
Cdd:cd05973    1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  552 raatlgeslgetrvlhlerlpqstgdlpAANVAP--GDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMqrRYPIGERDv 629
Cdd:cd05973   80 ----------------------------AANRHKldSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYL--RDAVDLRP- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  630 llqktpvtfDVSVWELF--WWSFtGARLSLLPPGAEKDPREML----------RSIQRDAVTVIHFVPsmlTPFLDLL-D 696
Cdd:cd05973  129 ---------EDSFWNAAdpGWAY-GLYYAITGPLALGHPTILLeggfsvestwRVIERLGVTNLAGSP---TAYRLLMaA 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  697 GDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDAVRlvNLYGPTEATVDVSDHEcASDNPTRV-PIGRPIDNLRLYV 775
Cdd:cd05973  196 GAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIH--DHYGQTELGMVLANHH-ALEHPVHAgSAGRAMPGWRVAV 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  776 LDRALRPQPLGAVGELYIGgvgVAR-------GYLNRPELNAErflvdpfvagGRLYRTGDLARWLADGNLEYLGRADDQ 848
Cdd:cd05973  273 LDDDGDELGPGEPGRLAID---IANsplmwfrGYQLPDTPAID----------GGYYLTGDTVEFDPDGSFSFIGRADDV 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  849 VKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAF-FVR----I 923
Cdd:cd05973  340 ITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHaYPRtihfV 419

                        490
                 ....*....|...
gi 15598523  924 DSLPLSANGKLDR 936
Cdd:cd05973  420 DELPKTPSGKIQR 432
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1482-1969 1.23e-30

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 128.82  E-value: 1.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1482 ERQVEALPGSAALAFEEQRWTYRDL-DHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 1560
Cdd:PRK06839    9 EKRAYLHPDRIAIITEEEEMTYKQLhEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1561 AQRLALILETAQPFRVVAHPEHAHVAAA-------ERVLPVEEL--VADIEPETFAAPQLDELAMLLFTSGSTGRPKGVE 1631
Cdd:PRK06839   89 ENELIFQLKDSGTTVLFVEKTFQNMALSmqkvsyvQRVISITSLkeIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1632 L-SHRMWANYTQWQLRVASGVPGlRTLQFAPLsFDMAFQEIFS--TLCGGGELQLisnRERMDPSALLHVLERRQVQRVL 1708
Cdd:PRK06839  169 LtQENMFWNALNNTFAIDLTMHD-RSIVLLPL-FHIGGIGLFAfpTLFAGGVIIV---PRKFEPTKALSMIEKHKVTVVM 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1709 LPFVALQRLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFCAAmpGLLLENQYGPTETHQVTYHSLSGDPAHYPDlpP 1788
Cdd:PRK06839  244 GVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPE-ELMREFIDR--GFLFGQGFGMTETSPTVFMLSEEDARRKVG--S 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1789 IGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERfVEHPWrpgarlYRTGDLGRILGNGEIVWLG 1868
Cdd:PRK06839  319 IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW------LCTGDLARVDEDGFVYIVG 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1869 RADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL-AELKQALRSELPEHMVP 1947
Cdd:PRK06839  392 RKKEMIISGGENIYPLEVEQVI----NKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIeKDVIEHCRLFLAKYKIP 467

                         490       500
                  ....*....|....*....|..
gi 15598523  1948 AHFAWVDGFALTPSGKRDDAAL 1969
Cdd:PRK06839  468 KEIVFLKELPKNATGKIQKAQL 489
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
458-939 1.67e-30

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 128.44  E-value: 1.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   458 TPQRTALLeADGGTLSYAELDAKVQAVADALR-AAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVR 536
Cdd:PRK06839   15 HPDRIAII-TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   537 LLLEDCGARVVLVDERAATLGESL----GETRVLHLERLPQSTGDLPAANVAPG-DLAYVI-YTSGSTGMPKG-VMVEHR 609
Cdd:PRK06839   94 FQLKDSGTTVLFVEKTFQNMALSMqkvsYVQRVISITSLKEIEDRKIDNFVEKNeSASFIIcYTSGTTGKPKGaVLTQEN 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   610 SVVNRLNWMQrRYPIGERDVLLQKTPVtFDVSVWELFWWS--FTGARLSLlpPGaEKDPREMLRSIQRDAVTVIHFVPSM 687
Cdd:PRK06839  174 MFWNALNNTF-AIDLTMHDRSIVLLPL-FHIGGIGLFAFPtlFAGGVIIV--PR-KFEPTKALSMIEKHKVTVVMGVPTI 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   688 LTPFLDLLDgdpTARAAASSLRLvFCSGEALAPLQVAR-FRR---LFGDAvrlvnlYGPTEATVDVsdHECASDNPTRVP 763
Cdd:PRK06839  249 HQALINCSK---FETTNLQSVRW-FYNGGAPCPEELMReFIDrgfLFGQG------FGMTETSPTV--FMLSEEDARRKV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   764 --IGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERflvdpfVAGGRLYrTGDLARWLADGNLEY 841
Cdd:PRK06839  317 gsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET------IQDGWLC-TGDLARVDEDGFVYI 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   842 LGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV--AAAELDPGQLRAGLSATLPDFMLPAF 919
Cdd:PRK06839  390 VGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVkkSSSVLIEKDVIEHCRLFLAKYKIPKE 469

                         490       500
                  ....*....|....*....|
gi 15598523   920 FVRIDSLPLSANGKLDRRQL 939
Cdd:PRK06839  470 IVFLKELPKNATGKIQKAQL 489
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
446-939 1.79e-30

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 129.23  E-value: 1.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   446 TLPTLFAEQVARTPQRTALlEADGGTLSYAELDAKV-QAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYV 524
Cdd:PRK08751   26 TVAEVFATSVAKFADRPAY-HSFGKTITYREADQLVeQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   525 PINPDHPLERVRLLLEDCGARV-VLVDERAATLGESLGETRVLHLerLPQSTGDL------------------------- 578
Cdd:PRK08751  105 NVNPLYTPRELKHQLIDSGASVlVVIDNFGTTVQQVIADTPVKQV--ITTGLGDMlgfpkaalvnfvvkyvkklvpeyri 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   579 ------------------PAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRL----NWMQRRYPIGE-RDVLLQKTP 635
Cdd:PRK08751  183 ngairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqahQWLAGTGKLEEgCEVVITALP 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   636 V--TFDVSVWELFWWSFTGARLSLLPPgaeKDPREMLRSIQRDAVTVIHFVPSML-----TPFLDLLDgdptaraaASSL 708
Cdd:PRK08751  263 LyhIFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFngllnTPGFDQID--------FSSL 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   709 RLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATvdvsdhECASDNPTRVP-----IGRPIDNLRLYVLDRALRPQ 783
Cdd:PRK08751  332 KMTLGGGMAVQRSVAERWKQVTG--LTLVEAYGLTETS------PAACINPLTLKeyngsIGLPIPSTDACIKDDAGTVL 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   784 PLGAVGELYIGGVGVARGYLNRPELNAErfLVDpfvAGGRLyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRD 863
Cdd:PRK08751  404 AIGEIGELCIKGPQVMKGYWKRPEETAK--VMD---ADGWL-HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIED 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   864 RLAALPGVRDAAVVARDSAVRGTHLvgyYVAAAELDPG----QLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK08751  478 VIAMMPGVLEVAAVGVPDEKSGEIV---KVVIVKKDPAltaeDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 1483-1963 2.03e-30

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: 128.01  E-value: 2.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1483 RQVEALPGSAALAFEEQ--RWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 1560
Cdd:cd05923    9 RAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1561 AQRLALILETAQPFRVV----AHPEHAHVAAAERVLPVEELVADIEPETFA------APQLDELAMLLFTSGSTGRPKGV 1630
Cdd:cd05923   89 AAELAELIERGEMTAAViavdAQVMDAIFQSGVRVLALSDLVGLGEPESAGpliedpPREPEQPAFVFYTSGTTGLPKGA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1631 ELSHRMWAN-----YTQWQLRVASGVpglRTLQFAPLSFDMAFQEIF-STLCGGGELQLIsnrERMDPSALLHVLERRQV 1704
Cdd:cd05923  169 VIPQRAAESrvlfmSTQAGLRHGRHN---VVLGLMPLYHVIGFFAVLvAALALDGTYVVV---EEFDPADALKLIEQERV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1705 QRVLLPFVALQRLAEASNALGVRPGALRVVVSSGeqlritedvrafcAAMPGLLLE-----------NQYGPTETHQVTY 1773
Cdd:cd05923  243 TSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAG-------------ATMPDAVLErvnqhlpgekvNIYGTTEAMNSLY 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1774 hslsgDPAHYPDlpPIGRPLDGVEVQVLDAALRPV---PVGVTGELYF--GGDCLARGYHRAPKLTAERFVEhpwrpgaR 1848
Cdd:cd05923  310 -----MRDARTG--TEMRPGFFSEVRIVRIGGSPDealANGEEGELIVaaAADAAFTGYLNQPEATAKKLQD-------G 375

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1849 LYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAV--VARERQGNdaFLAAFLLGEPE 1926
Cdd:cd05923  376 WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE----RVLSRHPGVTEVVVigVADERWGQ--SVTACVVPREG 449

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 15598523 1927 AVDLAELKQALR-SELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd05923  450 TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNK 487
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 1480-1954 4.31e-30

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 127.30  E-value: 4.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1480 LFERQVEALPGSAALAFE---EQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 1556
Cdd:PRK07514    5 LFDALRAAFADRDAPFIEtpdGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1557 VSYPAQRLALILETAQPFRVVAHPEH----AHVAAAERVLPVEEL----------VADIEPETFA--APQLDELAMLLFT 1620
Cdd:PRK07514   85 TAYTLAELDYFIGDAEPALVVCDPANfawlSKIAAAAGAPHVETLdadgtgslleAAAAAPDDFEtvPRGADDLAAILYT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1621 SGSTGRPKGVELSHRMWANYTQwQLRVASGV-PGLRTLQFAPlsfdmafqeIFST----------LCGGGELQLISnreR 1689
Cdd:PRK07514  165 SGTTGRSKGAMLSHGNLLSNAL-TLVDYWRFtPDDVLIHALP---------IFHThglfvatnvaLLAGASMIFLP---K 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1690 MDPSALLHVLERRQV--------QRvLLPFVALQRLAEASnalgvrpgaLRVVVSSGEQLrITEDVRAFCAAMPGLLLEn 1761
Cdd:PRK07514  232 FDPDAVLALMPRATVmmgvptfyTR-LLQEPRLTREAAAH---------MRLFISGSAPL-LAETHREFQERTGHAILE- 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1762 QYGPTETHQVTYHSLSGD--PAhypdlpPIGRPLDGVEVQVLD-AALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERF 1838
Cdd:PRK07514  300 RYGMTETNMNTSNPYDGErrAG------TVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1839 VEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLA 1918
Cdd:PRK07514  374 RADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEI----DELPGVVESAVIGVPHPDFGEGVT 443

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 15598523  1919 AFLLGEPEA-VDLAELKQALRSELPEHMVPAHFAWVD 1954
Cdd:PRK07514  444 AVVVPKPGAaLDEAAILAALKGRLARFKQPKRVFFVD 480
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 1463-1973 4.50e-30

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 127.95  E-value: 4.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1463 PRRDAASQPEPLVDVV--SLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIA 1540
Cdd:PRK06155    7 GLAARAVDPLPPSERTlpAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1541 TIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEH-AHVAAAE-RVLPVEE--------------------LV 1598
Cdd:PRK06155   87 VFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALlAALEAADpGDLPLPAvwlldapasvsvpagwstapLP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1599 ADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRM---WANYTQWQLRVASGVPGLRTLqfaPLSFDMAFQEIFSTL 1675
Cdd:PRK06155  167 PLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQfywWGRNSAEDLEIGADDVLYTTL---PLFHTNALNAFFQAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1676 CGGGELQLisnRERMDPSALLHVLERRQ--VQRVLLPFVA--LQRLAEASNalgvRPGALRVVVSSGEQLRITEDVRAFC 1751
Cdd:PRK06155  244 LAGATYVL---EPRFSASGFWPAVRRHGatVTYLLGAMVSilLSQPARESD----RAHRVRVALGPGVPAALHAAFRERF 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1752 aampGLLLENQYGPTETHQVTYHSLSGDPAHYpdlppIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGD---CLARGYH 1828
Cdd:PRK06155  317 ----GVDLLDGYGSTETNFVIAVTHGSQRPGS-----MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYF 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1829 RAPKLTAErfvehPWRpgARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR 1908
Cdd:PRK06155  388 GMPEKTVE-----AWR--NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLL----SHPAVAAAAVFPV 456

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  1909 ERQ-GNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRALP 1973
Cdd:PRK06155  457 PSElGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQG 522
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
445-939 4.96e-30

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 127.94  E-value: 4.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   445 ATLPTLFAEQVARTPQRTALLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYV 524
Cdd:PRK06087   23 ASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   525 PINPDHPLERVRLLLEDCGARVVL----------------VDERAATLGESLG------ETRVLHLERLPQSTGDLPAA- 581
Cdd:PRK06087  103 PLLPSWREAELVWVLNKCQAKMFFaptlfkqtrpvdlilpLQNQLPQLQQIVGvdklapATSSLSLSQIIADYEPLTTAi 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   582 NVAPGDLAYVIYTSGSTGMPKGVMVEH-------RSVVNRLN--WMqrrypigerDVLLQKTPVT----FDVSVWELFww 648
Cdd:PRK06087  183 TTHGDELAAVLFTSGTEGLPKGVMLTHnnilaseRAYCARLNltWQ---------DVFMMPAPLGhatgFLHGVTAPF-- 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   649 sFTGARLSLLppgAEKDPREMLRSIQRDAVTVIHFVpsmlTPFL-DLLDGDPTARAAASSLRLVFCSGeALAPLQVARfr 727
Cdd:PRK06087  252 -LIGARSVLL---DIFTPDACLALLEQQRCTCMLGA----TPFIyDLLNLLEKQPADLSALRFFLCGG-TTIPKKVAR-- 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   728 RLFGDAVRLVNLYGPTEAT--VDVSDHECASDNPTRVpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNR 805
Cdd:PRK06087  321 ECQQRGIKLLSVYGSTESSphAVVNLDDPLSRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   806 PELNAeRFLVDPfvagGRLYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRG 885
Cdd:PRK06087  399 PELTA-RALDEE----GWYY-SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLG 472

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523   886 THLVGYYVAAAE---LDPGQLRAGLSAT-LPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK06087  473 ERSCAYVVLKAPhhsLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 472-942 6.55e-30

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 126.74  E-value: 6.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLV-D 550
Cdd:PRK12406   12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   551 ERAATLGESLGET-RVLHLERLP--QSTGDLPAANVAP--GDLAY--------------------VIYTSGSTGMPKGVM 605
Cdd:PRK12406   92 DLLHGLASALPAGvTVLSVPTPPeiAAAYRISPALLTPpaGAIDWegwlaqqepydgppvpqpqsMIYTSGTTGHPKGVR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   606 VEHRSVVNRLNWMQRR-----YPIGERDV----LLQKTPVTFDVSVWELfwwsftGARLSLLPpgaEKDPREMLRSIQRD 676
Cdd:PRK12406  172 RAAPTPEQAAAAEQMRaliygLKPGIRALltgpLYHSAPNAYGLRAGRL------GGVLVLQP---RFDPEELLQLIERH 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   677 AVTVIHFVPSMltpFLDLLDGDPTARAA--ASSLRLVFcSGEALAPLQVARFRRLFGDAVrLVNLYGPTEA-TVDVSDHE 753
Cdd:PRK12406  243 RITHMHMVPTM---FIRLLKLPEEVRAKydVSSLRHVI-HAAAPCPADVKRAMIEWWGPV-IYEYYGSTESgAVTFATSE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   754 CASDNPTRVpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVAR-GYLNRPELNAErflvdpfVAGGRLYRTGDLAR 832
Cdd:PRK12406  318 DALSHPGTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-------IDRGGFITSGDVGY 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   833 WLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYY--VAAAELDPGQLRAGLSAT 910
Cdd:PRK12406  389 LDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVepQPGATLDEADIRAQLKAR 468

                         490       500       510
                  ....*....|....*....|....*....|..
gi 15598523   911 LPDFMLPAFFVRIDSLPLSANGKLDRRQLPAP 942
Cdd:PRK12406  469 LAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 445-939 1.10e-29

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 126.67  E-value: 1.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   445 ATLPTLFAEQVARTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVargPHLLP---AILGVQRAGG 521
Cdd:PRK07059   23 PSLADLLEESFRQYADRPAF-ICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMM---PNVLQypvAIAAVLRAGY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   522 AYVPINPDHPLERVRLLLEDCGARVVLVDER-AATLGESLGETRVLHLerLPQSTGDL-------------------PA- 580
Cdd:PRK07059   99 VVVNVNPLYTPRELEHQLKDSGAEAIVVLENfATTVQQVLAKTAVKHV--VVASMGDLlgfkghivnfvvrrvkkmvPAw 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   581 ----------------------ANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVV-NRLN---WMQ---RRYPIGERDVLL 631
Cdd:PRK07059  177 slpghvrfndalaegarqtfkpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQmeaWLQpafEKKPRPDQLNFV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   632 QKTPV--TFDVSVWELFWWSfTGARLSLLPpgaekDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARAAASSLR 709
Cdd:PRK07059  257 CALPLyhIFALTVCGLLGMR-TGGRNILIP-----NPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLI 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   710 LVFCSGEALAPLQVARFRRLFGDAVrlVNLYGPTEATvdvsdhECASDNPTRVP-----IGRPIDNLRLYVLDRALRPQP 784
Cdd:PRK07059  331 VANGGGMAVQRPVAERWLEMTGCPI--TEGYGLSETS------PVATCNPVDATefsgtIGLPLPSTEVSIRDDDGNDLP 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   785 LGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDR 864
Cdd:PRK07059  403 LGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEV 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   865 LAALPGVRDAAVVardsAVRGTH---LVGYYVAAAelDPG----QLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRR 937
Cdd:PRK07059  477 VASHPGVLEVAAV----GVPDEHsgeAVKLFVVKK--DPAlteeDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRR 550


                  ..
gi 15598523   938 QL 939
Cdd:PRK07059  551 EL 552
PRK08315 PRK08315
AMP-binding domain protein; Validated
 432-933 1.89e-29

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 126.08  E-value: 1.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   432 HTRNATDQAFPEQaTLPTLFAEQVARTPQRTALLEADGGT-LSYAELDAKVQAVADALRAAGVRTDERVALLvargPHLL 510
Cdd:PRK08315    4 YVRGPTDVPLLEQ-TIGQLLDRTAARYPDREALVYRDQGLrWTYREFNEEVDALAKGLLALGIEKGDRVGIW----APNV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   511 PAILGVQ----RAGGAYVPINPDHPLERVRLLLEDCGARVVLVDER------AATLGESLGETRV-----LHLERLPQ-- 573
Cdd:PRK08315   79 PEWVLTQfataKIGAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyVAMLYELAPELATcepgqLQSARLPElr 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   574 --------------STGDLPAANVAPGDLAY-----------VI---YTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIG 625
Cdd:PRK08315  159 rviflgdekhpgmlNFDELLALGRAVDDAELaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   626 ERDVLLqkTPVTF------------DVSVwelfwwsftGArlSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMltpFLD 693
Cdd:PRK08315  239 EEDRLC--IPVPLyhcfgmvlgnlaCVTH---------GA--TMVYPGEGFDPLATLAAVEEERCTALYGVPTM---FIA 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   694 LLDGDPTARAAASSLRLVFCSGeALAPLQVARfrrlfgDAVRLVNL------YGPTEaTVDVSdHECASDNPT--RV-PI 764
Cdd:PRK08315  303 ELDHPDFARFDLSSLRTGIMAG-SPCPIEVMK------RVIDKMHMsevtiaYGMTE-TSPVS-TQTRTDDPLekRVtTV 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   765 GRPIDNLRLYVLDRAL-RPQPLGAVGELYIGGVGVARGYLNRPELNAErfLVDpfvAGGRLyRTGDLARWLADGNLEYLG 843
Cdd:PRK08315  374 GRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AID---ADGWM-HTGDLAVMDEEGYVNIVG 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   844 RADDQVkIRG--NrVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV--AAAELDPGQLRAGLSATLPDFMLPAF 919
Cdd:PRK08315  448 RIKDMI-IRGgeN-IYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIlrPGATLTEEDVRDFCRGKIAHYKIPRY 525

                         570
                  ....*....|....
gi 15598523   920 FVRIDSLPLSANGK 933
Cdd:PRK08315  526 IRFVDEFPMTVTGK 539
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 587-936 1.94e-29

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: 121.98  E-value: 1.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  587 DLAYVIYTSGSTGMPKGVMVEHRSVVNRL-NWMQRRYPIGERDVLLQKTPVTFDV-SVWELFWWSFTGARLSLlppGAEK 664
Cdd:cd17635    2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPdILQKEGLNWVVGDVTYLPLPATHIGgLWWILTCLIHGGLCVTG---GENT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  665 DPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDgdpTARAAASSLRLVFCSGEALAPLQVaRFRRLFGDaVRLVNLYGPTE 744
Cdd:cd17635   79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELK---SANATVPSLRLIGYGGSRAIAADV-RFIEATGL-TNTAQVYGLSE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  745 -ATVDVSDHECASDNPTRVpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLvdpfvaGGR 823
Cdd:cd17635  154 tGTALCLPTDDDSIEINAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI------DGW 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  824 LYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQL 903
Cdd:cd17635  226 VN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAI 304

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 15598523  904 RA---GLSATLPDFMLPAFFVRIDSLPLSANGKLDR 936
Cdd:cd17635  305 RAlkhTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1477-1963 3.05e-29

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 125.98  E-value: 3.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1477 VVSLFERQVEALPGSAALAF----EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVC 1552
Cdd:COG1022   13 LPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1553 VPLDVSYPAQRLALILETAQP-FRVVAHPEHAHVAAA----------------------ERVLPVEELVAD----IEPET 1605
Cdd:COG1022   93 VPIYPTSSAEEVAYILNDSGAkVLFVEDQEQLDKLLEvrdelpslrhivvldprglrddPRLLSLDELLALgrevADPAE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1606 F----AAPQLDELAMLLFTSGSTGRPKGVELSHRmwaNYTqWQLRVASGV----PGLRTLQFAPLS-------------- 1663
Cdd:COG1022  173 LearrAAVKPDDLATIIYTSGTTGRPKGVMLTHR---NLL-SNARALLERlplgPGDRTLSFLPLAhvfertvsyyalaa 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1664 -FDMAFQEIFSTLcgGGELQLI-----------------SNRERMDPS--------------ALLHVLERRQVQRVLLPF 1711
Cdd:COG1022  249 gATVAFAESPDTL--AEDLREVkptfmlavprvwekvyaGIQAKAEEAgglkrklfrwalavGRRYARARLAGKSPSLLL 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1712 VALQRLAEA------SNALGvrpGALRVVVSSGEQLRitEDVRAFCAAMpGLLLENQYGPTETHQVTyhslSGDPAHYPD 1785
Cdd:COG1022  327 RLKHALADKlvfsklREALG---GRLRFAVSGGAALG--PELARFFRAL-GIPVLEGYGLTETSPVI----TVNRPGDNR 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1786 LPPIGRPLDGVEVQvldaalrpvpVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIV 1865
Cdd:COG1022  397 IGTVGPPLPGVEVK----------IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDEDGFLR 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1866 WLGRA-DTQVKVRGFRIEPAEVELAIMR-----QA----ERQPGLrGAAVV--------ARERQGNDAFLAAFLLGEPEA 1927
Cdd:COG1022  461 ITGRKkDLIVTSGGKNVAPQPIENALKAsplieQAvvvgDGRPFL-AALIVpdfealgeWAEENGLPYTSYAELAQDPEV 539

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....
gi 15598523 1928 VDL--AELKQAlRSELPEHMVPAHFA-----W-VDGFALTPSGK 1963
Cdd:COG1022  540 RALiqEEVDRA-NAGLSRAEQIKRFRllpkeFtIENGELTPTLK 582
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 1497-1928 3.67e-29

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: 123.47  E-value: 3.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1497 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL-DVSYPAQrLALILETAQPfr 1575
Cdd:cd05907    2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIyPTSSAEQ-IAYILNDSEA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1576 vvahpehahvaaaeRVLPVEELvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGvPGL 1654
Cdd:cd05907   79 --------------KALFVEDP--------------DDLATIIYTSGTTGRPKGVMLSHRnILSNALALAERLPAT-EGD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1655 RTLQFAPLS--FDMAFQEIFSTLCGG------GELQLISNRERMDPSALLhvlerrQVQRVLLPFVALQRLAEASNALG- 1725
Cdd:cd05907  130 RHLSFLPLAhvFERRAGLYVPLLAGAriyfasSAETLLDDLSEVRPTVFL------AVPRVWEKVYAAIKVKAVPGLKRk 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1726 ----VRPGALRVVVSSGEqlRITEDVRAFCAAMpGLLLENQYGPTETHQVTyhslSGDPAHYPDLPPIGRPLDGVEVQvl 1801
Cdd:cd05907  204 lfdlAVGGRLRFAASGGA--PLPAELLHFFRAL-GIPVYEGYGLTETSAVV----TLNPPGDNRIGTVGKPLPGVEVR-- 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1802 daalrpvpVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRA-DTQVKVRGFR 1880
Cdd:cd05907  275 --------IADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKN 340

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 15598523 1881 IEPAEVELAIMrqaeRQPGLRGAAVVARERqgndAFLAAFLLGEPEAV 1928
Cdd:cd05907  341 ISPEPIENALK----ASPLISQAVVIGDGR----PFLVALIVPDPEAL 380
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 7-410 4.11e-29

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: 122.70  E-value: 4.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    7 LPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLR-LGETDGTPYQWLDTDAEFEARH 85
Cdd:cd19543    2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSfVWEGLGEPLQVVLKDRKLPWRE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   86 VDLR--ADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGEL-G 161
Cdd:cd19543   82 LDLShlSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSfHHILLDGWSLPILLKELFAIYAALGeG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  162 EPQAQMPTASL---LAQLETDDYSGSEqyrgdrAYFAEALEGLE--PAL--FTRRRPAGLRRTARHRLTLERTLLDAIRD 234
Cdd:cd19543  162 QPPSLPPVRPYrdyIAWLQRQDKEAAE------AYWREYLAGFEepTPLpkELPADADGSYEPGEVSFELSAELTARLQE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  235 RGESPFLFLS----AAVALYLARIHQNDDVVLGVPVLNR-ADRA-AKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREAT 308
Cdd:cd19543  236 LARQHGVTLNtvvqGAWALLLSRYSGRDDVVFGTTVSGRpAELPgIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQ 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  309 RTLLRHQKMPLGDLLRGAS---PLFDTTLSYMRWPAAQAIPNA---------SVETVAQTHAHdpdaLAIWVSEFDGHSd 376
Cdd:cd19543  316 LELREHEYVPLYEIQAWSEgkqALFDHLLVFENYPVDESLEEEqdedglritDVSAEEQTNYP----LTVVAIPGEELT- 390

                        410       420       430
                 ....*....|....*....|....*....|....
gi 15598523  377 aqVDFEYACDVFDADFpMDAAARHIETFLRALVE 410
Cdd:cd19543  391 --IKLSYDAEVFDEAT-IERLLGHLRRVLEQVAA 421
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 458-936 4.30e-29

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: 124.92  E-value: 4.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  458 TPQRTALLEADGGT----LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVP-------- 525
Cdd:cd05970   30 YPDKLALVWCDDAGeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqltak 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  526 ----------------INPDHPLERVRLLLEDCGARVVLVderaaTLGESLGETRVLHLERLPQSTGDL--PAANVAPG- 586
Cdd:cd05970  110 divyriesadikmivaIAEDNIPEEIEKAAPECPSKPKLV-----WVGDPVPEGWIDFRKLIKNASPDFerPTANSYPCg 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  587 -DLAYVIYTSGSTGMPKgvMVEHRSVvnrlnwmqrrYPIG------------ERDVLLQKTPVTFDVSVWELFWWSFTGA 653
Cdd:cd05970  185 eDILLVYFSSGTTGMPK--MVEHDFT----------YPLGhivtakywqnvrEGGLHLTVADTGWGKAVWGKIYGQWIAG 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  654 RLSLLPPGAEKDPREMLRSIQRDAVTVIhFVPSMLTPFL---DLLDGDptaraaASSLRLVFCSGEALAPLQVARFRRLF 730
Cdd:cd05970  253 AAVFVYDYDKFDPKALLEKLSKYGVTTF-CAPPTIYRFLireDLSRYD------LSSLRYCTTAGEALNPEVFNTFKEKT 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  731 GdaVRLVNLYGPTEATVDVSDHECASDNPTRvpIGRPIDNLRLYVLDRALRPQPLGAVGELYIG-----GVGVARGYLNR 805
Cdd:cd05970  326 G--IKLMEGFGQTETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKD 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  806 PELNAERFLvDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRG 885
Cdd:cd05970  402 AEKTAEVWH-DGY------YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRG 474

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523  886 THLVGYYVAAAELDPGQlraGLSATLPDFM----LPAFFVRI----DSLPLSANGKLDR 936
Cdd:cd05970  475 QVVKATIVLAKGYEPSE---ELKKELQDHVkkvtAPYKYPRIvefvDELPKTISGKIRR 530
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 7-408 7.59e-29

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: 121.64  E-value: 7.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    7 LPLSPYQRDIWVAAAQFPelDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGET--DGTPYQWLDTDAEFEAR 84
Cdd:cd19542    2 YPCTPMQEGMLLSQLRSP--GLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESsaEGTFLQVVLKSLDPPIE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   85 HVdlradRDPEAAVRSWLRDAFrhAYP-LDGRSLVDLALLH-SDQALYVYVRTHHIVSDAWGLQLFLSRVRAGYLGELGE 162
Cdd:cd19542   80 EV-----ETDEDSLDALTRDLL--DDPtLFGQPPHRLTLLEtSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  163 PQAQMptASLLAQLETDDYSGSEQYRgdRAYFAEALEGLEPALFTRRRPAG-LRRTARHRLTLERTLldaiRDRGESPFL 241
Cdd:cd19542  153 PAPPF--SDYISYLQSQSQEESLQYW--RKYLQGASPCAFPSLSPKRPAERsLSSTRRSLAKLEAFC----ASLGVTLAS 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  242 FLSAAVALYLARIHQNDDVVLG-------VPVLNradraAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTLLRH 314
Cdd:cd19542  225 LFQAAWALVLARYTGSRDVVFGyvvsgrdLPVPG-----IDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPH 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  315 QKMPLGDLLR-----GASPLFDTTLSYMRWPAAQAIPNASVETVAQTHAHDPDALAIWVSEFDGHSDAQVDFEYACDVFD 389
Cdd:cd19542  300 QHLSLREIQRalglwPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLS 379

                        410
                 ....*....|....*....
gi 15598523  390 ADFpmdaAARHIETFLRAL 408
Cdd:cd19542  380 EEQ----AEELLEQFDDIL 394
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1483-1963 7.63e-29

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 124.09  E-value: 7.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1483 RQVEALPGSAALAFEE-QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPA 1561
Cdd:PRK06087   31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1562 QRLALILETAQP--------FRVVAH-----------PEHAHVAAAERVLP------VEELVADIEPETFAAP-QLDELA 1615
Cdd:PRK06087  111 AELVWVLNKCQAkmffaptlFKQTRPvdlilplqnqlPQLQQIVGVDKLAPatsslsLSQIIADYEPLTTAITtHGDELA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1616 MLLFTSGSTGRPKGVELSHrmwaNYTQWQLRVASGVPGLRTLQF----APLSFDMAF-QEIFSTLCGGGELQLIsnrERM 1690
Cdd:PRK06087  191 AVLFTSGTEGLPKGVMLTH----NNILASERAYCARLNLTWQDVfmmpAPLGHATGFlHGVTAPFLIGARSVLL---DIF 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1691 DPSALLHVLERRQVQRVL--LPFV--ALQRLAEAsnalGVRPGALRVVVSSGEQlrITEDVrAFCAAMPGLLLENQYGPT 1766
Cdd:PRK06087  264 TPDACLALLEQQRCTCMLgaTPFIydLLNLLEKQ----PADLSALRFFLCGGTT--IPKKV-ARECQQRGIKLLSVYGST 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1767 ETHQVTYHSLsGDPAHYpDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpg 1846
Cdd:PRK06087  337 ESSPHAVVNL-DDPLSR-FMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW--- 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1847 arlYRTGDLGRILGNGEIVWLGRaDTQVKVRGFR-IEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGNDAFLAAFLLG 1923
Cdd:PRK06087  412 ---YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILL----QHPKIHDACVVAMpdERLGERSCAYVVLKA 483

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 15598523  1924 EPEAVDLAELKQAL-RSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK06087  484 PHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGK 524
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 471-880 1.32e-28

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: 122.08  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD 550
Cdd:cd17640    5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 ERaatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVL 630
Cdd:cd17640   85 ND--------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRF 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  631 LQKTPVtfdvsvwelfWWSFTgaRLS---LLPPGAEK---DPREMLRSIQRDAVTVIHFVP----SMLTPFLD-LLDGDP 699
Cdd:cd17640  133 LSILPI----------WHSYE--RSAeyfIFACGCSQaytSIRTLKDDLKRVKPHYIVSVPrlweSLYSGIQKqVSKSSP 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  700 TARAAASSL------RLVFCSGEALAPlQVARFRRLFGdaVRLVNLYGPTEATVDVSDHEcaSDNPTRVPIGRPIDNLRL 773
Cdd:cd17640  201 IKQFLFLFFlsggifKFGISGGGALPP-HVDTFFEAIG--IEVLNGYGLTETSPVVSARR--LKCNVRGSVGRPLPGTEI 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  774 YVLDRALR-PQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKIR 852
Cdd:cd17640  276 KIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAKDTIVLS 349

                        410       420
                 ....*....|....*....|....*....
gi 15598523  853 -GNRVEPDEVRDRLAALPGVRDAAVVARD 880
Cdd:cd17640  350 nGENVEPQPIEEALMRSPFIEQIMVVGQD 378
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 1501-1974 3.14e-28

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: 120.68  E-value: 3.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1501 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHP 1580
Cdd:cd05969    1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1581 EhahvaaaervlpveeLVADIEPETfaapqldeLAMLLFTSGSTGRPKGVELSHR-MWANY--TQWQLRV-------ASG 1650
Cdd:cd05969   81 E---------------LYERTDPED--------PTLLHYTSGTTGTPKGVLHVHDaMIFYYftGKYVLDLhpddiywCTA 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1651 VPGLRTLQFAPlsfdmafqeIFSTLCGGgeLQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVR--P 1728
Cdd:cd05969  138 DPGWVTGTVYG---------IWAPWLNG--VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKydL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1729 GALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTYhslsgdpAHYPDLP----PIGRPLDGVEVQVLDAA 1804
Cdd:cd05969  207 SSLRFIHSVGEPL--NPEAIRWGMEVFGVPIHDTWWQTETGSIMI-------ANYPCMPikpgSMGKPLPGVKAAVVDEN 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1805 LRPVPVGVTGELYFGGD--CLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIE 1882
Cdd:cd05969  278 GNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-W------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1883 PAEVELAIMrqaeRQPGLRGAAVVARE----RQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFAL 1958
Cdd:cd05969  351 PFEVESALM----EHPAVAEAGVIGKPdplrGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426

                        490
                 ....*....|....*.
gi 15598523 1959 TPSGKRDDAALRALPL 1974
Cdd:cd05969  427 TRSGKIMRRVLKAKEL 442
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 1489-1971 3.29e-28

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 122.02  E-value: 3.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGV-ALNRsPEMIATIWGILRAGLVCVPL----------DV 1557
Cdd:PRK06188   26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlSLNR-PEVLMAIGAAQLAGLRRTALhplgslddhaYV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1558 SYPAQRLALILEtAQPFRVVAHPEHAHVAAAERVL---PVEELV------ADIEPETFAAPQL-DELAMLLFTSGSTGRP 1627
Cdd:PRK06188  105 LEDAGISTLIVD-PAPFVERALALLARVPSLKHVLtlgPVPDGVdllaaaAKFGPAPLVAAALpPDIAGLAYTGGTTGKP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1628 KGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSfDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRV 1707
Cdd:PRK06188  184 KGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVL---AKFDPAEVLRAIEEQRITAT 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1708 LLPFVALQRLAEAsnalgvrPGALRVVVSSGEQL----------RITEDVRAFcaampGLLLENQYGPTETHQVTYHSLS 1777
Cdd:PRK06188  260 FLVPTMIYALLDH-------PDLRTRDLSSLETVyygaspmspvRLAEAIERF-----GPIFAQYYGQTEAPMVITYLRK 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1778 GDpaHYPDLPPI----GRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFvEHPWrpgarlYRTG 1853
Cdd:PRK06188  328 RD--HDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGW------LHTG 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1854 DLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGnDAFLAAFLLGEPEAVDLA 1931
Cdd:PRK06188  399 DVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLA----EHPAVAQVAVigVPDEKWG-EAVTAVVVLRPGAAVDAA 473

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 15598523  1932 ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 1971
Cdd:PRK06188  474 ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 1613-1972 4.21e-28

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: 117.43  E-value: 4.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1613 ELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPG--LRTLqfaPLSFDMAFQEIFSTLCGGGELQLISNRer 1689
Cdd:cd17630    1 RLATVILTSGSTGTPKAVVHTAAnLLASAAGLHSRLGFGGGDswLLSL---PLYHVGGLAILVRSLLAGAELVLLERN-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1690 mdpSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLlenQYGPTET- 1768
Cdd:cd17630   76 ---QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAADRGIPLYT---TYGMTETa 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1769 HQVTYHSLSGdpahyPDLPPIGRPLDGVEVQVLDaalrpvpvgvTGELYFGGDCLARGYHRApkltaerfVEHPWRPGAR 1848
Cdd:cd17630  149 SQVATKRPDG-----FGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRG--------QLVPEFNEDG 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1849 LYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVArerQGNDAF---LAAFLLGEP 1925
Cdd:cd17630  206 WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAAL----AAHPAVRDAFVVG---VPDEELgqrPVAVIVGRG 278

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 15598523 1926 EaVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:cd17630  279 P-ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 451-939 4.43e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 122.06  E-value: 4.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   451 FAEQVA-RTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD 529
Cdd:PRK06710   29 YVEQMAsRYPEKKAL-HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   530 HPLERVRLLLEDCGARVVL----------------------------------------VDERAATLGESLGETRVLHL- 568
Cdd:PRK06710  108 YTERELEYQLHDSGAKVILcldlvfprvtnvqsatkiehvivtriadflpfpknllypfVQKKQSNLVVKVSESETIHLw 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   569 ---ERLPQSTGDLPAAnvAPGDLAYVIYTSGSTGMPKGVMVEHRSVV-NRLNWMQRRYPIGE-RDVLLQKTPVTFDVSVW 643
Cdd:PRK06710  188 nsvEKEVNTGVEVPCD--PENDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMT 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   644 ELFWWS-FTGARLSLLPpgaEKDPREMLRSIQRDAVTVIhfvPSMLTPFLDLLDGDPTARAAASSLRLVFcSGEALAPLQ 722
Cdd:PRK06710  266 AVMNLSiMQGYKMVLIP---KFDMKMVFEAIKKHKVTLF---PGAPTIYIALLNSPLLKEYDISSIRACI-SGSAPLPVE 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   723 VA-RFRRLFGDavRLVNLYGPTEAT-VDVSDHECASDNPTRVPIGRPIDNLRLYVLD--RALRPqplGAVGELYIGGVGV 798
Cdd:PRK06710  339 VQeKFETVTGG--KLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLEtgEALPP---GEIGEIVVKGPQI 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   799 ARGYLNRPELNAerflvdPFVAGGRLYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVA 878
Cdd:PRK06710  414 MKGYWNKPEETA------AVLQDGWLH-TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598523   879 RDSAVRGTHLVGYYV--AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK06710  487 VPDPYRGETVKAFVVlkEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 443-939 5.15e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 121.79  E-value: 5.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   443 EQATLPTLFAEQVARTPQRTALlEADGGTLSYAELDAKVQAVADALRA-AGVRTDERVALLVargPHLLP---AILGVQR 518
Cdd:PRK05677   22 EYPNIQAVLKQSCQRFADKPAF-SNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQL---PNVLQypvAVFGAMR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   519 AGGAYVPINPDHPLERVRLLLEDCGARVVLVDERAATLGES-LGETRVLH------------LER--------------- 570
Cdd:PRK05677   98 AGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKvLPKTGVKHvivtevadmlppLKRllinavvkhvkkmvp 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   571 ---LPQSTG-----------DLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNrlNWMQRRYPIGER-----DVLL 631
Cdd:PRK05677  178 ayhLPQAVKfndalakgagqPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVA--NMLQCRALMGSNlnegcEILI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   632 QKTPV------TFDVSVWELfwwsfTGARLSLLPpgaekDPRE---MLRSIQRDAVTviHFVpSMLTPFLDLLDGDPTAR 702
Cdd:PRK05677  256 APLPLyhiyafTFHCMAMML-----IGNHNILIS-----NPRDlpaMVKELGKWKFS--GFV-GLNTLFVALCNNEAFRK 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   703 AAASSLRLVFCSGEALAPLQVARFRRLFGDAVrlVNLYGPTEATvdvsdhECASDNPTRV----PIGRPIDNLRLYVLDR 778
Cdd:PRK05677  323 LDFSALKLTLSGGMALQLATAERWKEVTGCAI--CEGYGMTETS------PVVSVNPSQAiqvgTIGIPVPSTLCKVIDD 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   779 ALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVaggrlyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEP 858
Cdd:PRK05677  395 DGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYP 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   859 DEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVA--AAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDR 936
Cdd:PRK05677  469 NELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVkpGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILR 548


                  ...
gi 15598523   937 RQL 939
Cdd:PRK05677  549 REL 551
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 2077-2341 5.16e-28

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 114.02  E-value: 5.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2077 PPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAY 2156
Cdd:pfam00975    1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2157 EMARQLRALDPQaVAQLIVLDsitvdrnhaGSASdealllffywELVWFERSDKeveplpegASLEQKLDHIveRAIEAG 2236
Cdd:pfam00975   81 EVARRLERQGEA-VRSLFLSD---------ASAP----------HTVRYEASRA--------PDDDEVVAEF--TDEGGT 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2237 VLPAGTPRATVQRLYELFRASWQALIGYRPEVSDQDMTLLRADGPLPLALKPMHDAagthygdpknGWQHWTSGRLDVID 2316
Cdd:pfam00975  131 PEELLEDEELLSMLLPALRADYRALESYSCPPLDAQSATLFYGSDDPLHDADDLAE----------WVRDHTPGEFDVHV 200

                          250       260
                   ....*....|....*....|....*
gi 15598523   2317 VPGDHLVLMKEPyvETVAAEIAALL 2341
Cdd:pfam00975  201 FDGDHFYLIEHL--EAVLEIIEAKL 223
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
442-939 6.41e-28

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 121.31  E-value: 6.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   442 PEQ-ATLPTLFAEQVARTPQRTALLEAdGGTLSYAELDAKVQAVADALRAA-GVRTDERVALLVargPHLL--P-AILGV 516
Cdd:PRK08974   19 PDRyQSLVDMFEQAVARYADQPAFINM-GEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMM---PNLLqyPiALFGI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   517 QRAGGAYVPINPDHPLERVRLLLEDCGAR-VVLVDERAATLGESLGETRVLH--LERLPQ--STG--------------- 576
Cdd:PRK08974   95 LRAGMIVVNVNPLYTPRELEHQLNDSGAKaIVIVSNFAHTLEKVVFKTPVKHviLTRMGDqlSTAkgtlvnfvvkyikrl 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   577 ----DLPAA------------------NVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNrlNWMQRR---YPI---GERD 628
Cdd:PRK08974  175 vpkyHLPDAisfrsalhkgrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLA--NLEQAKaayGPLlhpGKEL 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   629 VLLqKTPV--TFDVSVWELFWWSFTGARLSLLPPgaeKDPREMLRSIQRDAVTVIHFVPsmlTPFLDLLDGDPTARAAAS 706
Cdd:PRK08974  253 VVT-ALPLyhIFALTVNCLLFIELGGQNLLITNP---RDIPGFVKELKKYPFTAITGVN---TLFNALLNNEEFQELDFS 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   707 SLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEAT--VDVSDHECASDNPTrvpIGRPIDNLRLYVLDRALRPQP 784
Cdd:PRK08974  326 SLKLSVGGGMAVQQAVAERWVKLTG--QYLLEGYGLTECSplVSVNPYDLDYYSGS---IGLPVPSTEIKLVDDDGNEVP 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   785 LGAVGELYIGGVGVARGYLNRPELNAErFLVDPFVAggrlyrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDR 864
Cdd:PRK08974  401 PGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523   865 LAALPGVRDAAVVARDSAVRGtHLVGYYVAA--AELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK08974  474 VMLHPKVLEVAAVGVPSEVSG-EAVKIFVVKkdPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 1499-1970 7.11e-28

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 120.30  E-value: 7.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1499 QRWTYRDLDH-VARCVATrLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPfRVV 1577
Cdd:PRK09088   21 RRWTYAELDAlVGRLAAV-LRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEP-RLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1578 AHpeHAHVAAAE-RVLPVEELVADI---EPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRmwanyTQWQLRVASGVPG 1653
Cdd:PRK09088   99 LG--DDAVAAGRtDVEDLAAFIASAdalEPADTPSIPPERVSLILFTSGTSGQPKGVMLSER-----NLQQTAHNFGVLG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1654 L-----RTLQFAPLSFDMAF-QEIFSTLCGGGELQlISNRerMDPSALLHVLERRQVQrVLLPFVALQRLAEASNALGVR 1727
Cdd:PRK09088  172 RvdahsSFLCDAPMFHIIGLiTSVRPVLAVGGSIL-VSNG--FEPKRTLGRLGDPALG-ITHYFCVPQMAQAFRAQPGFD 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1728 PGALR--VVVSSGEQLRITEDVRAFCAAmpGLLLENQYGPTETHQVtyHSLSGDPAHYPD-LPPIGRPLDGVEVQVLDAA 1804
Cdd:PRK09088  248 AAALRhlTALFTGGAPHAAEDILGWLDD--GIPMVDGFGMSEAGTV--FGMSVDCDVIRAkAGAAGIPTPTVQTRVVDDQ 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1805 LRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPA 1884
Cdd:PRK09088  324 GNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPA 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1885 EVELAIMrqaeRQPGLRGAAVV--ARERQGNDAFLAAfLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 1962
Cdd:PRK09088  398 EIEAVLA----DHPGIRECAVVgmADAQWGEVGYLAI-VPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASG 472


                  ....*...
gi 15598523  1963 KRDDAALR 1970
Cdd:PRK09088  473 KLQKARLR 480
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 1498-1892 7.94e-28

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: 119.77  E-value: 7.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1498 EQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPfrvv 1577
Cdd:cd17640    3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1578 ahpehahVAaaervlpveeLVADIEPetfaapqlDELAMLLFTSGSTGRPKGVELSHRmwaNYTqWQLR----VASGVPG 1653
Cdd:cd17640   79 -------VA----------LVVENDS--------DDLATIIYTSGTTGNPKGVMLTHA---NLL-HQIRslsdIVPPQPG 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1654 LRTLQFAPL--SFDMAFqEIFSTLCGGGEL-----QLISNRERMDPSALLHV-------LERRQVQRVLLPFVAlQRLAE 1719
Cdd:cd17640  130 DRFLSILPIwhSYERSA-EYFIFACGCSQAytsirTLKDDLKRVKPHYIVSVprlweslYSGIQKQVSKSSPIK-QFLFL 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1720 ASnalgVRPGALRVVVSSGEQLRITEDvRAFCAAmpGLLLENQYGPTETHQVTYHSLSGDPAhypdLPPIGRPLDGVEVQ 1799
Cdd:cd17640  208 FF----LSGGIFKFGISGGGALPPHVD-TFFEAI--GIEVLNGYGLTETSPVVSARRLKCNV----RGSVGRPLPGTEIK 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1800 VLDAALR-PVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRA-DTQVKVR 1877
Cdd:cd17640  277 IVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAkDTIVLSN 350

                        410
                 ....*....|....*
gi 15598523 1878 GFRIEPAEVELAIMR 1892
Cdd:cd17640  351 GENVEPQPIEEALMR 365
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 585-939 8.42e-28

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: 117.58  E-value: 8.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  585 PGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtFDV--SVWELFWWSFTGARLSLLPPGA 662
Cdd:cd05944    1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVngSVVTLLTPLASGAHVVLAGPAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  663 EKDP---REMLRSIQRDAVTVIHFVPSMLTPFLDLLDGdptarAAASSLRLVFCSGealAPLQVARFRRlFGDA--VRLV 737
Cdd:cd05944   80 YRNPglfDNFWKLVERYRITSLSTVPTVYAALLQVPVN-----ADISSLRFAMSGA---APLPVELRAR-FEDAtgLPVV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  738 NLYGPTEATvdvSDHECA-SDNPTR---VPIGRPIDNLRLYVLD---RALRPQPLGAVGELYIGGVGVARGYLNRpELNA 810
Cdd:cd05944  151 EGYGLTEAT---CLVAVNpPDGPKRpgsVGLRLPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYT-EGNK 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  811 ERFlvdpfvAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVG 890
Cdd:cd05944  227 NAF------VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVA 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15598523  891 Y--YVAAAELDPGQLRAGLSATLPD-FMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05944  301 YvqLKPGAVVEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK09274 PRK09274
peptide synthase; Provisional
 456-877 1.03e-27

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 120.77  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   456 ARTPQRTALLEADGG---------TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGayVPI 526
Cdd:PRK09274   17 QERPDQLAVAVPGGRgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA--VPV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   527 ------------------NPD----HPLERV-RLLL---EDCGARVVLVDERAATLGESLGETRvlhlerLPQSTGDLPA 580
Cdd:PRK09274   95 lvdpgmgiknlkqclaeaQPDafigIPKAHLaRRLFgwgKPSVRRLVTVGGRLLWGGTTLATLL------RDGAAAPFPM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   581 ANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPI--GERDVllqktpVTFDVSVweLFwwsftGARL--- 655
Cdd:PRK09274  169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIepGEIDL------PTFPLFA--LF-----GPALgmt 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   656 SLLPP-----GAEKDPREMLRSIQRDAVTVIHFVPSMLTPfldLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLF 730
Cdd:PRK09274  236 SVIPDmdptrPATVDPAKLFAAIERYGVTNLFGSPALLER---LGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAML 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   731 GDAVRLVNLYGPTEA----TVDVSDHECASDNPTR----VPIGRPIDNLRLYVLDRALRPQ---------PLGAVGELYI 793
Cdd:PRK09274  313 PPDAEILTPYGATEAlpisSIESREILFATRAATDngagICVGRPVDGVEVRIIAISDAPIpewddalrlATGEIGEIVV 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   794 GGVGVARGYLNRPELNAERFLVDPfvAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRD 873
Cdd:PRK09274  393 AGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKR 470


                  ....
gi 15598523   874 AAVV 877
Cdd:PRK09274  471 SALV 474
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 587-936 3.51e-27

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: 114.81  E-value: 3.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  587 DLAYVIYTSGSTGMPKGVMVEHRSvvnrlnWMQRrYPIGER-------DVLLQKTPVTFDVSVWELFWWSFTGARLSLLp 659
Cdd:cd17633    1 NPFYIGFTSGTTGLPKAYYRSERS------WIES-FVCNEDlfnisgeDAILAPGPLSHSLFLYGAISALYLGGTFIGQ- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  660 pgAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDptaraaaSSLRLVFCSGEALAPLQVARFRRLFGDAVrLVNL 739
Cdd:cd17633   73 --RKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE-------SKIKSIFSSGQKLFESTKKKLKNIFPKAN-LIEF 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  740 YGPTEATVdVSdHECASDNPTRVPIGRPIDNLRLYVLDralrpQPLGAVGELYIGGVGVARGYLNRPELNAERFlvdpfv 819
Cdd:cd17633  143 YGTSELSF-IT-YNFNQESRPPNSVGRPFPNVEIEIRN-----ADGGEIGKIFVKSEMVFSGYVRGGFSNPDGW------ 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  820 aggrlYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVaAAELD 899
Cdd:cd17633  210 -----MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS-GDKLT 283

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 15598523  900 PGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDR 936
Cdd:cd17633  284 YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 9-233 6.05e-27

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 111.67  E-value: 6.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    9 LSPYQRDIWVAaaqFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEARHVDL 88
Cdd:COG4908    1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   89 RA--DRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLH-SDQALYVYVRTHHIVSDAWGLQLFLSRVRAGYLGELGEPQA 165
Cdd:COG4908   78 SAlpEPEREAELEELVAEEASRPFDLARGPLLRAALIRlGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523  166 QMPT-----ASLLAQLetDDYSGSEQYRGDRAYFAEALEGLEPAL---FTRRRPAGL-RRTARHRLTLERTLLDAIR 233
Cdd:COG4908  158 PLPElpiqyADYAAWQ--RAWLQSEALEKQLEYWRQQLAGAPPVLelpTDRPRPAVQtFRGATLSFTLPAELTEALK 232
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 1451-1970 6.15e-27

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 118.34  E-value: 6.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1451 HPDEAADFAFLAPRRDAASQpeplvdvvslFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGV 1530
Cdd:PRK07786    3 ALTLAQEQPYLARRQNWVNQ----------LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1531 -ALNRsPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAAAER------------------- 1590
Cdd:PRK07786   73 lMLNR-TEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRdivpllstvvvaggssdds 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1591 VLPVEELVAdiepETFAAPQL-----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRvASGVPGLRTLQF--APLS 1663
Cdd:PRK07786  152 VLGYEDLLA----EAGPAHAPvdipnDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLR-TNGADINSDVGFvgVPLF 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1664 FDMAFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPGALRVVvSSGEQLRI 1743
Cdd:PRK07786  227 HIAGIGSMLPGLLLGAPT-VIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVL-SWGAAPAS 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1744 TEDVRAFCAAMPGLLLENQYGPTETHQVTYhSLSGDPAhYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCL 1823
Cdd:PRK07786  304 DTLLRQMAATFPEAQILAAFGQTEMSPVTC-MLLGEDA-IRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTL 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1824 ARGYHRAPKLTAERFvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGA 1903
Cdd:PRK07786  382 MSGYWNNPEATAEAF-AGGW------FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLA----SHPDIVEV 450

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523  1904 AVVAR--ERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:PRK07786  451 AVIGRadEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 6-408 6.26e-27

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: 116.37  E-value: 6.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    6 RLPLSPYQRDIWVAAaQF-PELDQYTI-FSYdRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQW-LDTD-AEF 81
Cdd:cd19540    1 RIPLSFAQQRLWFLN-RLdGPSAAYNIpLAL-RLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVvLPAAeARP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   82 EARHVDLRADRDPEAavrswLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGEL 160
Cdd:cd19540   79 DLTVVDVTEDELAAR-----LAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVvHHIAADGWSMAPLARDLATAYAARR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  161 --GEPQ-AQMP------TASLLAQLETDDYSGSEQYRgDRAYFAEALEGL--EPAL-FTRRRPAGL-RRTARHRLTLERT 227
Cdd:cd19540  154 agRAPDwAPLPvqyadyALWQRELLGDEDDPDSLAAR-QLAYWRETLAGLpeELELpTDRPRPAVAsYRGGTVEFTIDAE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  228 LLDAI----RDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQ 303
Cdd:cd19540  233 LHARLaalaREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLAR 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  304 LREATRTLLRHQKMP---LGDLL-----RGASPLFDTTLSY-MRWPAAQAIPNASVEtvaqthAHDPDA------LAIWV 368
Cdd:cd19540  313 VRETDLAAFAHQDVPferLVEALnpprsTARHPLFQVMLAFqNTAAATLELPGLTVE------PVPVDTgvakfdLSFTL 386

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 15598523  369 SE-FDGHSDAQ---VDFEYACDVFDAdfpmDAAARHIETFLRAL 408
Cdd:cd19540  387 TErRDADGAPAgltGELEYATDLFDR----STAERLADRFVRVL 426
PRK05691 PRK05691
peptide synthase; Validated
 1466-2052 7.21e-27

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 121.04  E-value: 7.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1466 DAASQPEPLVDVVslfERQVEALPGSAALAF-----EEQR-WTYRDLDHVARCVATRLvRAGARRGDAIGVALNRSPEMI 1539
Cdd:PRK05691    3 DAFELPLTLVQAL---QRRAAQTPDRLALRFladdpGEGVvLSYRDLDLRARTIAAAL-QARASFGDRAVLLFPSGPDYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1540 ATIWGILRAGLVCVPldvSYPAQ--------RLALILETAQPFRVV---------AHPEHAHVAAAERVLPVEELVADIe 1602
Cdd:PRK05691   79 AAFFGCLYAGVIAVP---AYPPEsarrhhqeRLLSIIADAEPRLLLtvadlrdslLQMEELAAANAPELLCVDTLDPAL- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1603 PETFAAPQL--DELAMLLFTSGSTGRPKGVELSH-RMWANytQWQLRVASGV---PGLRTLQFAPLSFDMAF-----QEI 1671
Cdd:PRK05691  155 AEAWQEPALqpDDIAFLQYTSGSTALPKGVQVSHgNLVAN--EQLIRHGFGIdlnPDDVIVSWLPLYHDMGLiggllQPI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1672 FS----------------------------TLCGGGELQLISNRERMDPSALlhvlERRQVQRVLLPFV--------ALQ 1715
Cdd:PRK05691  233 FSgvpcvlmspayflerplrwleaiseyggTISGGPDFAYRLCSERVSESAL----ERLDLSRWRVAYSgsepirqdSLE 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1716 RLAEASNALGVRPGALRVVVSSGE-QLRITEDVRAfcAAMPGLLLENQygptethqvtyhSLSGDPAHYPDLPPI---GR 1791
Cdd:PRK05691  309 RFAEKFAACGFDPDSFFASYGLAEaTLFVSGGRRG--QGIPALELDAE------------ALARNRAEPGTGSVLmscGR 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1792 PLDGVEVQVLDAA-LRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPwrpGARLYRTGDLGrILGNGEIVWLGRA 1870
Cdd:PRK05691  375 SQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLG-FLRDGELFVTGRL 450

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1871 DTQVKVRGFRIEPAEVELAIMRQAERQPGLRgAAVVARERQGNDAFLAAFLLGE--PEAVDLAELKQALRSELPE--HMV 1946
Cdd:PRK05691  451 KDMLIVRGHNLYPQDIEKTVEREVEVVRKGR-VAAFAVNHQGEEGIGIAAEISRsvQKILPPQALIKSIRQAVAEacQEA 529

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1947 PAHFAWVDGFAL--TPSGKRDDAALRaLPLEHGTNIEY--------------LAPRDDYERTLAGLLGELLDRPRVGIRD 2010
Cdd:PRK05691  530 PSVVLLLNPGALpkTSSGKLQRSACR-LRLADGSLDSYalfpalqaveaaqtAASGDELQARIAAIWCEQLKVEQVAADD 608

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 15598523  2011 SFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLA 2052
Cdd:PRK05691  609 HFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFS 650
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 1489-1963 8.91e-27

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 117.40  E-value: 8.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:PRK13383   49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1569 ETAQPFRVVAHPEHAhvaaaERVLPVEELVADIEPETFAA------PQLDELA-MLLFTSGSTGRPKGVELSHRMWANYT 1641
Cdd:PRK13383  129 RAHHISTVVADNEFA-----ERIAGADDAVAVIDPATAGAeesggrPAVAAPGrIVLLTSGTTGKPKGVPRAPQLRSAVG 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1642 QW-------QLRVASGVpGLRTLQFAPLSFDMafqeIFSTLCGGGElqlISNRERMDPSALLHVLERRQVQRVLLPFVAL 1714
Cdd:PRK13383  204 VWvtildrtRLRTGSRI-SVAMPMFHGLGLGM----LMLTIALGGT---VLTHRHFDAEAALAQASLHRADAFTAVPVVL 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1715 QRLAEASNALGVRPG--ALRVVVSSGEQLRITEDVRAFCAAmpGLLLENQYGPTEthqVTYHSLSgDPAHYPDLP-PIGR 1791
Cdd:PRK13383  276 ARILELPPRVRARNPlpQLRVVMSSGDRLDPTLGQRFMDTY--GDILYNGYGSTE---VGIGALA-TPADLRDAPeTVGK 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1792 PLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRApklTAERFVEHpwrpgarLYRTGDLGRILGNGEIVWLGRAD 1871
Cdd:PRK13383  350 PVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG---GGKAVVDG-------MTSTGDMGYLDNAGRLFIVGRED 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1872 TQVKVRGFRIEPAEVELAImrqaERQPGLRGAAV--VARERQGNDafLAAFLLGEPEA-VDLAELKQALRSELPEHMVPA 1948
Cdd:PRK13383  420 DMIISGGENVYPRAVENAL----AAHPAVADNAVigVPDERFGHR--LAAFVVLHPGSgVDAAQLRDYLKDRVSRFEQPR 493

                         490
                  ....*....|....*
gi 15598523  1949 HFAWVDGFALTPSGK 1963
Cdd:PRK13383  494 DINIVSSIPRNPTGK 508
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 1494-1890 9.09e-27

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: 116.39  E-value: 9.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1494 LAFEEQRWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ 1572
Cdd:cd05914    1 LYYGGEPLTYKDLaDNIAK-FALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1573 PFRVVAHPEhahvaaaervlpveelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHR-MWANYTqWQLRVASGV 1651
Cdd:cd05914   80 AKAIFVSDE------------------------------DDVALINYTSGTTGNSKGVMLTYRnIVSNVD-GVKEVVLLG 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1652 PGLRTLQFAPLS--FDMAFQEIFSTLCGGGELQLisnrERMdPSALLHVLERRQVQ----------------RVLLPFVA 1713
Cdd:cd05914  129 KGDKILSILPLHhiYPLTFTLLLPLLNGAHVVFL----DKI-PSAKIIALAFAQVTptlgvpvplviekifkMDIIPKLT 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1714 L----QRLAEASNALGVRP-----------GALRVVVSSGEQL--RITEDVR--AFCAAMpglllenQYGPTETHQVtyh 1774
Cdd:cd05914  204 LkkfkFKLAKKINNRKIRKlafkkvheafgGNIKEFVIGGAKInpDVEEFLRtiGFPYTI-------GYGMTETAPI--- 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1775 sLSGDPAHYPDLPPIGRPLDGVEVQVLDaalrPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGD 1854
Cdd:cd05914  274 -ISYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGD 342

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 15598523 1855 LGRILGNGEIVWLGRADTQ-VKVRGFRIEPAEVELAI 1890
Cdd:cd05914  343 LGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKI 379
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 1500-1970 1.20e-26

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: 116.96  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1500 RWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI------------ 1567
Cdd:cd12119   25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIinhaedrvvfvd 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1568 -------------LETAQPFRVVAHPEHAHVAAAERVLPVEELVADiEPETFAAPQLDE--LAMLLFTSGSTGRPKGVEL 1632
Cdd:cd12119  105 rdflplleaiaprLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAA-ESPEYDWPDFDEntAAAICYTSGTTGNPKGVVY 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1633 SHRmwANYTQWQLRVASGVPGLRT----LQFAPLSFDMAFQEIFSTLCGGGELQLISnrERMDPSALLHVLERRQVQRVL 1708
Cdd:cd12119  184 SHR--SLVLHAMAALLTDGLGLSEsdvvLPVVPMFHVNAWGLPYAAAMVGAKLVLPG--PYLDPASLAELIEREGVTFAA 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1709 -LPFVALQRLAEASnALGVRPGALRVVVSSGeqlritedvrafcAAMPGLLLE----------NQYGPTETHQVTyhSLS 1777
Cdd:cd12119  260 gVPTVWQGLLDHLE-ANGRDLSSLRRVVIGG-------------SAVPRSLIEafeergvrviHAWGMTETSPLG--TVA 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1778 GDPAHYPDLPP---------IGRPLDGVEVQVLDAALRPVPV-GVT-GELYFGGDCLARGYHRAPKlTAERFVEHPWrpg 1846
Cdd:cd12119  324 RPPSEHSNLSEdeqlalrakQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW--- 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1847 arlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR------ERQgndafLAAF 1920
Cdd:cd12119  400 ---LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIM----AHPAVAEAAVIGVphpkwgERP-----LAVV 467

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 15598523 1921 LLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd12119  468 VLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 456-941 2.47e-26

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: 117.21  E-value: 2.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  456 ARTPQRTALL-EADGG---TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHP 531
Cdd:cd05968   72 ADTRTRPALRwEGEDGtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  532 LERVRLLLEDCGARVVLVDE------RAATLGESLGET-------------RVLHLERLPQSTGDL-----------PAA 581
Cdd:cd05968  152 KEAAATRLQDAEAKALITADgftrrgREVNLKEEADKAcaqcptvekvvvvRHLGNDFTPAKGRDLsydeeketagdGAE 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  582 NVAPGDLAYVIYTSGSTGMPKGVMVEHRSV-VNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLP- 659
Cdd:cd05968  232 RTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDg 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  660 -PGaEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDgDPTARAAASSLRLVFCSGEALAPLQVAR-FRRLFGDAVRLV 737
Cdd:cd05968  312 aPD-HPKADRLWRMVEDHEITHLGLSPTLIRALKPRGD-APVNAHDLSSLRVLGSTGEPWNPEPWNWlFETVGKGRNPII 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  738 NLYGPTEATVDVsdhecASDNPTRvPI-----GRPIDNLRLYVLDRALRPQPlGAVGELYIGG--VGVARGYLNRPElna 810
Cdd:cd05968  390 NYSGGTEISGGI-----LGNVLIK-PIkpssfNGPVPGMKADVLDESGKPAR-PEVGELVLLApwPGMTRGFWRDED--- 459

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  811 eRFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVG 890
Cdd:cd05968  460 -RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVC 538

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  891 YYVAAAELDPG-----QLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLPA 941
Cdd:cd05968  539 FVVLKPGVTPTealaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 1497-1907 2.67e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 116.25  E-value: 2.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1497 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG--LVCVPldvsYPAQRLALILETAQPF 1574
Cdd:PRK07768   26 APVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGasLTMLH----QPTPRTDLAVWAEDTL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1575 RVVAHPEHAHV-------AAAE-------RVLPVEELVADIEPETFAAPQlDELAMLLFTSGSTGRPKGVELSHR-MWAN 1639
Cdd:PRK07768  102 RVIGMIGAKAVvvgepflAAAPvleekgiRVLTVADLLAADPIDPVETGE-DDLALMQLTSGSTGSPKAVQITHGnLYAN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1640 ----YTQWQLRVASGVpglrTLQFAPLSFDMAFQEIFST-LCGGGELQLISNRERM-DPSALLHVLERRQVQRVLLP-F- 1711
Cdd:PRK07768  181 aeamFVAAEFDVETDV----MVSWLPLFHDMGMVGFLTVpMYFGAELVKVTPMDFLrDPLLWAELISKYRGTMTAAPnFa 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1712 --VALQRLAEASNALGVRPGALRVVVSSGEQLRITeDVRAFCAA-----MPGLLLENQYGPTET----------HQVTYH 1774
Cdd:PRK07768  257 yaLLARRLRRQAKPGAFDLSSLRFALNGAEPIDPA-DVEDLLDAgarfgLRPEAILPAYGMAEAtlavsfspcgAGLVVD 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1775 SLSGD---------PAHYPD---LPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYhrapkLTAERFV--- 1839
Cdd:PRK07768  336 EVDADllaalrravPATKGNtrrLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIpaq 410

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523  1840 -EHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVA 1907
Cdd:PRK07768  411 dADGW------LDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE----RAAARVEGVRPGNAVA 469
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1058-1281 3.29e-26

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 109.74  E-value: 3.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1058 GLLFHsrqRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGaSEPLQLVHTQARSEPLILDLRGNPE 1137
Cdd:COG4908    7 RFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVDLSALPE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1138 AG--TVLDEHIRQRRFHRYSLQQPGLFLFAAFVREDGLD-LVFSFHHAILDGWSVANLIVALVAAYRGE------PLPGP 1208
Cdd:COG4908   83 PEreAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAALYAALlegeppPLPEL 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523 1209 APALACHVREELAALASPA---AVGYWTGLLEGARMTRLDGFGAHEPQAAQG-PASHREALPDGLLERLKATAAQRG 1281
Cdd:COG4908  163 PIQYADYAAWQRAWLQSEAlekQLEYWRQQLAGAPPVLELPTDRPRPAVQTFrGATLSFTLPAELTEALKALAKAHG 239
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 1481-1977 4.94e-26

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 115.14  E-value: 4.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1481 FERQVEA-LPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:PRK07470   12 FLRQAARrFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1560 PAQRLALILETAQPFRVVAH---PEHAhvAAAERVLPVEELVADIEPETF------------------AAPQLDELAMLL 1618
Cdd:PRK07470   92 TPDEVAYLAEASGARAMICHadfPEHA--AAVRAASPDLTHVVAIGGARAgldyealvarhlgarvanAAVDHDDPCWFF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1619 FTSGSTGRPKGVELSHRMWA----NytqwqlRVASGVPGL----RTLQFAPLSFDMAFQEIFSTLCGGGELQLISnrERM 1690
Cdd:PRK07470  170 FTSGTTGRPKAAVLTHGQMAfvitN------HLADLMPGTteqdASLVVAPLSHGAGIHQLCQVARGAATVLLPS--ERF 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1691 DPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITEDVRAFcaAMPGLLLENQYGPTE-TH 1769
Cdd:PRK07470  242 DPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRAL--AKLGKVLVQYFGLGEvTG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1770 QVT-----YHSLSGDPAhyPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVeHPWr 1844
Cdd:PRK07470  320 NITvlppaLHDAEDGPD--ARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR-DGW- 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1845 pgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGnDAFLAAFLL 1922
Cdd:PRK07470  396 -----FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLL----THPAVSEVAVlgVPDPVWG-EVGVAVCVA 465

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15598523  1923 GEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRALPLEHG 1977
Cdd:PRK07470  466 RDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEERG 520
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 1489-1907 1.65e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 113.90  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD----------- 1556
Cdd:PRK08314   24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNpmnreeelahy 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1557 -------VSYPAQRLALILETAQPFRVVAH----------PEHAHVAAAERVLPVEELVADIEP------ETFAAPQL-- 1611
Cdd:PRK08314  104 vtdsgarVAIVGSELAPKVAPAVGNLRLRHvivaqysdylPAEPEIAVPAWLRAEPPLQALAPGgvvawkEALAAGLApp 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1612 ------DELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVaSGVPGLRTLQFAPLSFDMAFQE-IFSTLCGGGELQL 1683
Cdd:PRK08314  184 phtagpDDLAVLPYTSGTTGVPKGCMHTHRtVMANAVGSVLWS-NSTPESVVLAVLPLFHVTGMVHsMNAPIYAGATVVL 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1684 ISnreRMDPSALLHVLERRQVQR------VLLPFVALQRLAEASNAlgvrpgALRVVVSSGeqlritedvrafcAAMP-- 1755
Cdd:PRK08314  263 MP---RWDREAAARLIERYRVTHwtniptMVVDFLASPGLAERDLS------SLRYIGGGG-------------AAMPea 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1756 ---------GLLLENQYGPTETHQVTyHSlsgDPAHYPDLPPIGRPLDGVEVQVLDAA-LRPVPVGVTGELYFGGDCLAR 1825
Cdd:PRK08314  321 vaerlkeltGLDYVEGYGLTETMAQT-HS---NPPDRPKLQCLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFK 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1826 GYHRAPKLTAERFVEhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRqaeRQPGLRGAAV 1905
Cdd:PRK08314  397 GYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE-NLLY---KHPAIQEACV 469


                  ..
gi 15598523  1906 VA 1907
Cdd:PRK08314  470 IA 471
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 8-381 1.85e-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: 111.78  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    8 PLSPYQRDIWVAAAQFPELDQYTI-FSYdRFTGEVDTQALERALLQAARDTEAFRLR--LGETDGTPYQ--WLDTDAEFE 82
Cdd:cd19532    3 PMSFGQSRFWFLQQYLEDPTTFNVtFSY-RLTGPLDVARLERAVRAVGQRHEALRTCffTDPEDGEPMQgvLASSPLRLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   83 ARHVDlradrdPEAAVRSWLRDAFRHAYPLDGRSLVDLALL-HSDQALYVYVRTHHIVSDAWGLQLFLSRVRAGYLGE-L 160
Cdd:cd19532   82 HVQIS------DEAEVEEEFERLKNHVYDLESGETMRIVLLsLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQpL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  161 GEPQAQMPTaslLAQLETDDYSgSEQYRGDRAYFAEALEGLEPAL----FTRR--RPAgLRRTARHR--LTLERTLLDAI 232
Cdd:cd19532  156 LPPPLQYLD---FAARQRQDYE-SGALDEDLAYWKSEFSTLPEPLpllpFAKVksRPP-LTRYDTHTaeRRLDAALAARI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  233 RDR----GESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREAT 308
Cdd:cd19532  231 KEAsrklRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKA 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  309 RTLLRHQKMPLGDLLR--------GASPLFDTTLSY-MRWPAAQAIPNASVETVAQTHAHDPDALAIWVSEFDGHsDAQV 379
Cdd:cd19532  311 YAALAHSRVPFDVLLDelgvprsaTHSPLFQVFINYrQGVAESRPFGDCELEGEEFEDARTPYDLSLDIIDNPDG-DCLL 389


                 ..
gi 15598523  380 DF 381
Cdd:cd19532  390 TL 391
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1059-1374 2.04e-25

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: 111.70  E-value: 2.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1059 LLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQ--LVHTQARSEPLILDlRGNP 1136
Cdd:cd19539   11 LWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQeiLPPGPAPLEVRDLS-DPDS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1137 EAGTVLDEHIRQRRFHRYSLQQPGLFLFAAF-VREDGLDLVFSFHHAILDGWSVANLIVALVAAYRG------EPLPGPA 1209
Cdd:cd19539   90 DRERRLEELLRERESRGFDLDEEPPIRAVLGrFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAArrkgpaAPLPELR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1210 PALACHVREELAALASPAA---VGYWTGLLEGARMTRLdgfGAHEPQAAQGP---ASHREALPDGLLERLKATAAQRGLP 1283
Cdd:cd19539  170 QQYKEYAAWQREALAAPRAaelLDFWRRRLRGAEPTAL---PTDRPRPAGFPypgADLRFELDAELVAALRELAKRARSS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1284 LKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIAGCSwiEVADALFRQER---DGHAHR 1360
Cdd:cd19539  247 LFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH-PRFESTVGFFVNLLPLRVDVSDCA--TFRDLIARVRKalvDAQRHQ 323

                        330
                 ....*....|....
gi 15598523 1361 RYPLSAIQQIVGDE 1374
Cdd:cd19539  324 ELPFQQLVAELPVD 337
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 469-939 2.30e-25

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 113.38  E-value: 2.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   469 GGTLSYAELDAKVQAVADALRAagvRTD----ERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGA 544
Cdd:PRK12492   47 GVTLSYAELERHSAAFAAYLQQ---HTDlvpgDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   545 R-VVLVDERAATLGESLGETRVLHL------------------------------ERLPQSTG-----------DLPAAN 582
Cdd:PRK12492  124 RaLVYLNMFGKLVQEVLPDTGIEYLieakmgdllpaakgwlvntvvdkvkkmvpaYHLPQAVPfkqalrqgrglSLKPVP 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   583 VAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNW----MQRRYPIGE------RDVLLQKTPVtfdvsvweLFWWSFTG 652
Cdd:PRK12492  204 VGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQvracLSQLGPDGQplmkegQEVMIAPLPL--------YHIYAFTA 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   653 ARLSLLPPGAEK----DPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRR 728
Cdd:PRK12492  276 NCMCMMVSGNHNvlitNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQ 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   729 LFGdaVRLVNLYGPTEATvdvsdhECASDNP----TRV-PIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYL 803
Cdd:PRK12492  356 LTG--CTIVEGYGLTETS------PVASTNPygelARLgTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYW 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   804 NRPELNAERFLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAv 883
Cdd:PRK12492  428 QQPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDE- 500

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523   884 RGTHLVGYYVAAAE--LDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK12492  501 RSGEAVKLFVVARDpgLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PLN02246 PLN02246
4-coumarate--CoA ligase
 423-941 2.45e-25

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 113.15  E-value: 2.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   423 SAAEREELIHTRNATDQAFPEQATLPTLFAEQVARTPQRTALLE-ADGGTLSYAELDAKVQAVADALRAAGVRTDERVAL 501
Cdd:PLN02246    1 EASASEEFIFRSKLPDIYIPNHLPLHDYCFERLSEFSDRPCLIDgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   502 LVARGPHLLPAILGVQRAGGAYVPINPDHP----------------------LERVRLLLEDCGARVVLVDERAAtlges 559
Cdd:PLN02246   81 LLPNCPEFVLAFLGASRRGAVTTTANPFYTpaeiakqakasgakliitqscyVDKLKGLAEDDGVTVVTIDDPPE----- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   560 lgetRVLHLERLPQS-TGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVN-----------RLNWmqrrypiGER 627
Cdd:PLN02246  156 ----GCLHFSELTQAdENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTsvaqqvdgenpNLYF-------HSD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   628 DVLLQKTPVtFDV----SVweLFWWSFTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSMLtpfLDLLDGDPTARA 703
Cdd:PLN02246  225 DVILCVLPM-FHIyslnSV--LLCGLRVGAAILIMP---KFEIGALLELIQRHKVTIAPFVPPIV---LAIAKSPVVEKY 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   704 AASSLRLVFcSGEalAP----LQVArFRRLFGDAVrLVNLYGPTEATVDVSDHECASDNPTRV---PIGRPIDNLRLYVL 776
Cdd:PLN02246  296 DLSSIRMVL-SGA--APlgkeLEDA-FRAKLPNAV-LGQGYGMTEAGPVLAMCLAFAKEPFPVksgSCGTVVRNAELKIV 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   777 D----RAL-RPQPlgavGELYIGGVGVARGYLNRPELNAERFLVDpfvagGRLYrTGDLARWLADGNLEYLGRADDQVKI 851
Cdd:PLN02246  371 DpetgASLpRNQP----GEICIRGPQIMKGYLNDPEATANTIDKD-----GWLH-TGDIGYIDDDDELFIVDRLKELIKY 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   852 RGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAA--ELDPGQLRAGLSATLpdfmlpAFFVRI------ 923
Cdd:PLN02246  441 KGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNgsEITEDEIKQFVAKQV------VFYKRIhkvffv 514

                         570
                  ....*....|....*...
gi 15598523   924 DSLPLSANGKLDRRQLPA 941
Cdd:PLN02246  515 DSIPKAPSGKILRKDLRA 532
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 472-939 2.80e-25

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: 111.51  E-value: 2.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDE 551
Cdd:cd05974    1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  552 raatlgeslgetrvlhlerlpqstgdlpaaNVAPGDLAYVIYTSGSTGMPKgvMVEHrsvvnrlnwMQRRYPIGERDVL- 630
Cdd:cd05974   81 ------------------------------NTHADDPMLLYFTSGTTSKPK--LVEH---------THRSYPVGHLSTMy 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  631 ---LQKTPVTFDVS-------VWELFWWSFTGARLSLLPPGAEKDPREMLRSIQRDAVTVIHFVPSMLTpfldLLDGDPT 700
Cdd:cd05974  120 wigLKPGDVHWNISspgwakhAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWR----MLIQQDL 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  701 ARAAASsLRLVFCSGEALAPLQVARFRRLFGDAVRlvNLYGPTEATVDVSDhecASDNPTRV-PIGRPIDNLRLYVLDRA 779
Cdd:cd05974  196 ASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIR--DGYGQTETTALVGN---SPGQPVKAgSMGRPLPGYRVALLDPD 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  780 LRPQPLGAVGeLYIGG---VGVARGYLNRPELNAErflvdpfVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRV 856
Cdd:cd05974  270 GAPATEGEVA-LDLGDtrpVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRI 341

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  857 EPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRA-GLSATLPDFMLPAFFVR---IDSLPLSANG 932
Cdd:cd05974  342 SPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETAlEIFRFSRERLAPYKRIRrleFAELPKTISG 421


                 ....*..
gi 15598523  933 KLDRRQL 939
Cdd:cd05974  422 KIRRVEL 428
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 1615-1963 3.45e-25

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: 109.27  E-value: 3.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1615 AMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGelQLISNRERMDPS 1693
Cdd:cd17635    4 LAVIFTSGTTGEPKAVLLANKtFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG--LCVTGGENTTYK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1694 ALLHVLERRQVQRVLLPFVALQRLA-EASNALGVRPgALRVVVSSGEqlRITEDVRAFCAAMPGLLLENQYGPTETHQVT 1772
Cdd:cd17635   82 SLFKILTTNAVTTTCLVPTLLSKLVsELKSANATVP-SLRLIGYGGS--RAIAADVRFIEATGLTNTAQVYGLSETGTAL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1773 YHSLSGDPAhypDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRT 1852
Cdd:cd17635  159 CLPTDDDSI---EINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG-W------VNT 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1853 GDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAV--VARERQGNDAFLAAFLLGEPEAVDL 1930
Cdd:cd17635  229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVE----RIAEGVSGVQECACyeISDEEFGELVGLAVVASAELDENAI 304

                        330       340       350
                 ....*....|....*....|....*....|...
gi 15598523 1931 AELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd17635  305 RALKHTIRRELEPYARPSTIVIVTDIPRTQSGK 337
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 461-941 4.31e-25

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 112.68  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   461 RTALLEADGG---TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRL 537
Cdd:PRK04319   60 KVALRYLDASrkeKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRD 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   538 LLEDCGARVV----------------------LVDEraatLGESLGETRVLHlERLPQSTGDLPAANVAPGDLAYVIYTS 595
Cdd:PRK04319  140 RLEDSEAKVLittpallerkpaddlpslkhvlLVGE----DVEEGPGTLDFN-ALMEQASDEFDIEWTDREDGAILHYTS 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   596 GSTGMPKGVMVEHRSVVnrLNWMQRRYpigerdVL-LQKTpvtfDVsvwelFW------WsFTGARLSLLPP-------- 660
Cdd:PRK04319  215 GSTGKPKGVLHVHNAML--QHYQTGKY------VLdLHED----DV-----YWctadpgW-VTGTSYGIFAPwlngatnv 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   661 --GAEKDPREMLRSIQRDAVTVIHFVPsmlTPFLDLL--DGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRL 736
Cdd:PRK04319  277 idGGRFSPERWYRILEDYKVTVWYTAP---TAIRMLMgaGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFG--LPI 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   737 VNLYGPTE---------ATVDVSdhecasdnptrvP--IGRPIDNLRLYVLDRALRPQPLGAVGELYI--GGVGVARGYL 803
Cdd:PRK04319  352 HDNWWMTEtggimianyPAMDIK------------PgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIW 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   804 NRPELNAERFlvdpfvAGGrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAV 883
Cdd:PRK04319  420 NNPEKYESYF------AGD-WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPV 492

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523   884 RGtHLVGYYVAaaeLDPG-----QLRAGLSAtlpdfmlpafFVR--------------IDSLPLSANGKLDRRQLPA 941
Cdd:PRK04319  493 RG-EIIKAFVA---LRPGyepseELKEEIRG----------FVKkglgahaapreiefKDKLPKTRSGKIMRRVLKA 555
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 465-961 5.04e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 112.08  E-value: 5.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   465 LEADGGTLSYAELDAKVQAVADALRAAGVRTDER-VALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVR--LLLED 541
Cdd:PRK07867   22 LYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALArdIAHAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   542 CgaRVVLVD-ERAATLGESLGETRVLHLERL-------PQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVN 613
Cdd:PRK07867  102 C--QLVLTEsAHAELLDGLDPGVRVINVDSPawadelaAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   614 RLNWMQRRYPIGERDVLLQKTPVTFDVSVweLFWWSF---TGARLSLlppgaekdPRE-----MLRSIQRDAVTVIHFVP 685
Cdd:PRK07867  180 AGVMLAQRFGLGPDDVCYVSMPLFHSNAV--MAGWAValaAGASIAL--------RRKfsasgFLPDVRRYGATYANYVG 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   686 SmltPFLDLLDGDPTARAAASSLRLVFcsGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVsdhecasdnpTRVP-- 763
Cdd:PRK07867  250 K---PLSYVLATPERPDDADNPLRIVY--GNEGAPGDIARFARRFG--CVVVDGFGSTEGGVAI----------TRTPdt 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   764 ----IGRPIDNLRLY-----------VLDRALRPQPLGAVGELY-IGGVGVARGYLNRPELNAERflvdpfVAGGRlYRT 827
Cdd:PRK07867  313 ppgaLGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAER------MRGGV-YWS 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   828 GDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDPGQLRA 905
Cdd:PRK07867  386 GDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLApgAKFDPDAFAE 465

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523   906 GLSATlPDF---MLPAfFVRI-DSLPLSANGKLDRRQLPAP----PEQVAAVAPRTATEAELAA 961
Cdd:PRK07867  466 FLAAQ-PDLgpkQWPS-YVRVcAELPRTATFKVLKRQLSAEgvdcADPVWWIRRLTPSDYAALA 527
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 1463-1962 5.29e-25

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 112.14  E-value: 5.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1463 PRRDAASQPEPLVdvvSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATI 1542
Cdd:PRK06164    1 TPHDAAPRADTLA---SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1543 WGILRAGLVCVPLDVSYPAQRLALILETAQP--------------FRVVAHPEHAHVAAAERVLPVEELVADIEPETFAA 1608
Cdd:PRK06164   78 LACARLGATVIAVNTRYRSHEVAHILGRGRArwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVDDAADATPAPAPGA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1609 P--------------------QLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAF 1668
Cdd:PRK06164  158 RvqlfalpdpappaaageraaDPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1669 QEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPgALRVVVSSGEQLRITEDVR 1748
Cdd:PRK06164  238 STLLGALAGGAPLVCE---PVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFP-SARLFGFASFAPALGELAA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1749 AFCAAmpGLLLENQYGPTETHQ-VTYHSLSGDPAHYPDlpPIGRPLDG-VEVQVLDAALRPV-PVGVTGELYFGGDCLAR 1825
Cdd:PRK06164  314 LARAR--GVPLTGLYGSSEVQAlVALQPATDPVSVRIE--GGGRPASPeARVRARDPQDGALlPDGESGEIEIRAPSLMR 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1826 GYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAV 1905
Cdd:PRK06164  390 GYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL----EALPGVAAAQV 459

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523  1906 VARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 1962
Cdd:PRK06164  460 VGATRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1617-1965 5.94e-25

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: 109.01  E-value: 5.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1617 LLFTSGSTGRPKGVELSH----RMWAN----------YTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQ 1682
Cdd:cd05924    8 ILYTGGTTGMPKGVMWRQedifRMLMGgadfgtgeftPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1683 LIsnRERMDPSALLHVLERRQVQRVLLPFVALQR-LAEASNALGVRP-GALRVVVSSGEQLriTEDVR-AFCAAMPGLLL 1759
Cdd:cd05924   88 LP--DDRFDPEEVWRTIEKHKVTSMTIVGDAMARpLIDALRDAGPYDlSSLFAISSGGALL--SPEVKqGLLELVPNITL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1760 ENQYGPTET-HQVTYHSLSGDPAHYPdlppigRPLDGVEVQVLDAALRPVPVGVTGELYFG-GDCLARGYHRAPKLTAER 1837
Cdd:cd05924  164 VDAFGSSETgFTGSGHSAGSGPETGP------FTRANPDTVVLDDDGRVVPPGSGGVGWIArRGHIPLGYYGDEAKTAET 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1838 FVEhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVAR--ERQGNDa 1915
Cdd:cd05924  238 FPE---VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEAL----KSHPAVYDVLVVGRpdERWGQE- 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15598523 1916 fLAAFL-LGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 1965
Cdd:cd05924  310 -VVAVVqLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 442-939 7.60e-25

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 111.86  E-value: 7.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   442 PEQATLPTLFAEqvARTPQRTALLEADGG-TLSYAELDAKVQAVADAL-RAAGVRTDERVALLVARGPHLLPAILGVQRA 519
Cdd:PLN02574   38 PNLDAVSFIFSH--HNHNGDTALIDSSTGfSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   520 GGAYVPINPDHPLERVRLLLEDC------------------GARVVLVDErAATLGESLGETRVLHlERLPQSTGDLPAA 581
Cdd:PLN02574  116 GGIVTTMNPSSSLGEIKKRVVDCsvglaftspenveklsplGVPVIGVPE-NYDFDSKRIEFPKFY-ELIKEDFDFVPKP 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   582 NVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVN------RLNWMQRRYPiGERDVLLQKTPVtFDVSVWELFwwsftgaRL 655
Cdd:PLN02574  194 VIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAmvelfvRFEASQYEYP-GSDNVYLAALPM-FHIYGLSLF-------VV 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   656 SLLPPGA------EKDPREMLRSIQRDAVTVIHFVPSMLTPFLDlldgdpTARAAAS----SLRLVFCSGealAPLqvar 725
Cdd:PLN02574  265 GLLSLGStivvmrRFDASDMVKVIDRFKVTHFPVVPPILMALTK------KAKGVCGevlkSLKQVSCGA---APL---- 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   726 FRRLFGDAVR------LVNLYGPTEATVdVSDHECASDNPTR-VPIGRPIDNLRLYVLDRALRP-QPLGAVGELYIGGVG 797
Cdd:PLN02574  332 SGKFIQDFVQtlphvdFIQGYGMTESTA-VGTRGFNTEKLSKySSVGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPG 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   798 VARGYLNRPELNAERFLVDPFVaggrlyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVV 877
Cdd:PLN02574  411 VMKGYLNNPKATQSTIDKDGWL------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVT 484

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523   878 ARDSAVRGTHLVGYYVAAAEldpgqlrAGLSAT-----LPDFMLPAFFVR----IDSLPLSANGKLDRRQL 939
Cdd:PLN02574  485 AVPDKECGEIPVAFVVRRQG-------STLSQEavinyVAKQVAPYKKVRkvvfVQSIPKSPAGKILRREL 548
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 1489-1963 1.05e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 111.17  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:PRK07788   63 PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1569 ETAQPFRVVAHPEHAHVAAA-----ERVLPVEELVADIEPETFAAPQLDELA----------------MLLFTSGSTGRP 1627
Cdd:PRK07788  143 AREGVKALVYDDEFTDLLSAlppdlGRLRAWGGNPDDDEPSGSTDETLDDLIagsstaplpkppkpggIVILTSGTTGTP 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1628 KGVELSHrmwanytqwqlrvasgVPGLRTL-QF---APLSFDMAFQ---EIFSTLcGGGELQLISN-------RERMDPS 1693
Cdd:PRK07788  223 KGAPRPE----------------PSPLAPLaGLlsrVPFRAGETTLlpaPMFHAT-GWAHLTLAMAlgstvvlRRRFDPE 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1694 ALLHVLERRQVQRVLLPFVALQRLAEASNALGVRP--GALRVVVSSGEQLRiTEDVRAFCAAMpGLLLENQYGPTETHQV 1771
Cdd:PRK07788  286 ATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYdtSSLKIIFVSGSALS-PELATRALEAF-GPVLYNLYGSTEVAFA 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1772 TY---HSLSGDPAhypdlpPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYhrapklTAERfveHPWRPGAr 1848
Cdd:PRK07788  364 TIatpEDLAEAPG------TVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR---DKQIIDG- 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1849 LYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEP-EA 1927
Cdd:PRK07788  428 LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLL----AGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPgAA 503

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 15598523  1928 VDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK07788  504 LDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGK 539
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 448-933 1.10e-24

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: 110.47  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  448 PTLFAEQVART-PQRTALLEadGGT-LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVP 525
Cdd:cd12118    6 PLSFLERAAAVyPDRTSIVY--GDRrYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  526 INPDHPLERVRLLLEDCGARVVLVDEraatlgESLGETRVlhlerlpqSTGDLPAANVAPGDLAYVI---YTSGSTGMPK 602
Cdd:cd12118   84 LNTRLDAEEIAFILRHSEAKVLFVDR------EFEYEDLL--------AEGDPDFEWIPPADEWDPIalnYTSGTTGRPK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  603 GVMVEHR-----SVVNRLNWMQRRYPigerdVLLQKTPVtFDVSVWeLFWWSFT--GARLSLLPpgaEKDPREMLRSIQR 675
Cdd:cd12118  150 GVVYHHRgaylnALANILEWEMKQHP-----VYLWTLPM-FHCNGW-CFPWTVAavGGTNVCLR---KVDAKAIYDLIEK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  676 DAVTviHF--VPSMLTpflDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGDavrLVNLYGPTE----ATV-- 747
Cdd:cd12118  220 HKVT--HFcgAPTVLN---MLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFD---VTHVYGLTEtygpATVca 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  748 --DVSDHECASDNP-------TRVPIGRPIDnlrlyVLD-RALRPQPLGA--VGELYIGGVGVARGYLNRPELNAERFlv 815
Cdd:cd12118  292 wkPEWDELPTEERArlkarqgVRYVGLEEVD-----VLDpETMKPVPRDGktIGEIVFRGNIVMKGYLKNPEATAEAF-- 364

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  816 dpfvAGGrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVAR-DSavrgtHLVGYYVA 894
Cdd:cd12118  365 ----RGG-WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpDE-----KWGEVPCA 434

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 15598523  895 AAELDPG------QLRAGLSATLPDFMLPAFFVrIDSLPLSANGK 933
Cdd:cd12118  435 FVELKEGakvteeEIIAFCREHLAGFMVPKTVV-FGELPKTSTGK 478
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 445-939 1.20e-24

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 110.93  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   445 ATLPTLFAEQVARTPQRTALL-EADGG---TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAG 520
Cdd:PRK08008    7 QHLRQMWDDLADVYGHKTALIfESSGGvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   521 GAYVPINPDHPLERVRLLLEDCGARVVLVDERAATLGESL---GETRVLHL----ERLPQSTG-----DLPAANVA---- 584
Cdd:PRK08008   87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIqqeDATPLRHIcltrVALPADDGvssftQLKAQQPAtlcy 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   585 -----PGDLAYVIYTSGSTGMPKGVMVEHrsvVNRL------NWMQRrypIGERDVLLQKTP---VTFDVSVwelFWWSF 650
Cdd:PRK08008  167 applsTDDTAEILFTSGTTSRPKGVVITH---YNLRfagyysAWQCA---LRDDDVYLTVMPafhIDCQCTA---AMAAF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   651 T-GARLSLLppgaEK-DPREMLRSIQRDAVTVIHFVPSMLTpflDLLDGDPTARAAASSLRLVF-----CSGEALAplqv 723
Cdd:PRK08008  238 SaGATFVLL----EKySARAFWGQVCKYRATITECIPMMIR---TLMVQPPSANDRQHCLREVMfylnlSDQEKDA---- 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   724 arFRRLFGdaVRLVNLYGPTEATVDVsdhecASDNPT---RVP-IGRPIDNLRLYVLDRALRPQPLGAVGELYIGGV--- 796
Cdd:PRK08008  307 --FEERFG--VRLLTSYGMTETIVGI-----IGDRPGdkrRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgk 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   797 GVARGYLNRPELNAErflvdPFVAGGRLYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAV 876
Cdd:PRK08008  378 TIFKEYYLDPKATAK-----VLEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523   877 VA-----RDSAVRGTHLvgyYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK08008  452 VGikdsiRDEAIKAFVV---LNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 1499-1887 1.22e-24

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: 110.79  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1499 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVA 1578
Cdd:cd05904   31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1579 HPEHAH--VAAAERVLPVEELVAD---IEPETFAAPQL---------DELAMLLFTSGSTGRPKGVELSHR-MWANYTQW 1643
Cdd:cd05904  111 TAELAEklASLALPVVLLDSAEFDslsFSDLLFEADEAeppvvvikqDDVAALLYSSGTTGRSKGVMLTHRnLIAMVAQF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1644 QLRVASGVPGL-RTLQFAPLSFDMAFQEIFSTLCGGGELQLIsnRERMDPSALLHVLERRQVQRvlLPFVALQRLAEASN 1722
Cdd:cd05904  191 VAGEGSNSDSEdVFLCVLPMFHIYGLSSFALGLLRLGATVVV--MPRFDLEELLAAIERYKVTH--LPVVPPIVLALVKS 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1723 ALGV--RPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTE-THQVTYHSL-SGDPAHYPDlppIGRPLDGVEV 1798
Cdd:cd05904  267 PIVDkyDLSSLRQIMSGAAPLGK-ELIEAFRAKFPNVDLGQGYGMTEsTGVVAMCFApEKDRAKYGS---VGRLVPNVEA 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1799 QVLD-AALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVR 1877
Cdd:cd05904  343 KIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW------LHTGDLCYIDEDGYLFIVDRLKELIKYK 416

                        410
                 ....*....|
gi 15598523 1878 GFRIEPAEVE 1887
Cdd:cd05904  417 GFQVAPAELE 426
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 1493-1970 2.03e-24

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: 109.10  E-value: 2.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1493 ALAFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETA 1571
Cdd:cd05958    3 CLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1572 QPfrvvahpehAHVAAAERVLPVeelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASG 1650
Cdd:cd05958   83 RI---------TVALCAHALTAS-----------------DDICILAFTSGTTGAPKATMHFHRdPLASADRYAVNVLRL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1651 VPGLRTLQFAPLSFDMAF--QEIFSTLCGGGELQLisnrERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRP 1728
Cdd:cd05958  137 REDDRFVGSPPLAFTFGLggVLLFPFGVGASGVLL----EEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDL 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1729 GALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTyhsLSGDPAhypDLPP--IGRPLDGVEVQVLDAALR 1806
Cdd:cd05958  213 SSLRKCVSAGEAL--PAALHRAWKEATGIPIIDGIGSTEMFHIF---ISARPG---DARPgaTGKPVPGYEAKVVDDEGN 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1807 PVPVGVTGELYFGGDClarGYHRAPKLTAERFVEHPWRPgarlyrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEV 1886
Cdd:cd05958  285 PVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNI------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEV 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1887 ELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPE----AVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 1962
Cdd:cd05958  356 EDVLL----QHPAVAECAVVGHPDESRGVVVKAFVVLRPGvipgPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATG 431


                 ....*...
gi 15598523 1963 KRDDAALR 1970
Cdd:cd05958  432 KLQRFALR 439
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 1460-1970 3.32e-24

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 109.76  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1460 FLAPRRDAAS-----QPEPLVDvvsLFERQVEALPGSAALA------FEEQRWTYRDLDHVARCVATRLVRAGARRGDAI 1528
Cdd:PRK13295    7 LLPPRRAASIaaghwHDRTIND---DLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1529 GVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQP--------FRVVAHPEHA-----------HVAAA- 1588
Cdd:PRK13295   84 SCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESkvlvvpktFRGFDHAAMArrlrpelpalrHVVVVg 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1589 -------ERVL--PVEELVADIePETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVasgvpGLRT 1656
Cdd:PRK13295  164 gdgadsfEALLitPAWEQEPDA-PAILARLRPgpDDVTQLIYTSGTTGEPKGVMHTANtLMANIVPYAERL-----GLGA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1657 LQFAPLSFDMAFQEIFstlcGGGELQLISNRERM------DPSALLHVLERRQVQRVL--LPFvaLQRLAEASNALGVRP 1728
Cdd:PRK13295  238 DDVILMASPMAHQTGF----MYGLMMPVMLGATAvlqdiwDPARAAELIRTEGVTFTMasTPF--LTDLTRAVKESGRPV 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1729 GALRVVVSSGEQL--RITEDVRAFCaampGLLLENQYGPTETHQVTYHSLSGDP--AHYPDlppiGRPLDGVEVQVLDAA 1804
Cdd:PRK13295  312 SSLRTFLCAGAPIpgALVERARAAL----GAKIVSAWGMTENGAVTLTKLDDPDerASTTD----GCPLPGVEVRVVDAD 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1805 LRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFveHPWrpgarlYRTGDLGRILGNGEIVWLGRAdTQVKVRGFR-IEP 1883
Cdd:PRK13295  384 GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGW------FDTGDLARIDADGYIRISGRS-KDVIIRGGEnIPV 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1884 AEVELAIMrqaeRQPGLRGAAVVA--RERQGNDAflAAFLLGEP-EAVDLAELKQALRSE-LPEHMVPAHFAWVDGFALT 1959
Cdd:PRK13295  455 VEIEALLY----RHPAIAQVAIVAypDERLGERA--CAFVVPRPgQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRT 528

                         570
                  ....*....|.
gi 15598523  1960 PSGKRDDAALR 1970
Cdd:PRK13295  529 PSGKIQKFRLR 539
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 471-939 3.61e-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: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 108.70  E-value: 3.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVArgphllpailgvqraggayvpinPDHPLERVRLLLEDCGARVVLVD 550
Cdd:cd05910    2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVP-----------------------PGPDFFALTFALFKAGAVPVLID 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 ERA--ATLGESLGETRvlhlerlPQSTGDLPAAnvapGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERD 628
Cdd:cd05910   59 PGMgrKNLKQCLQEAE-------PDAFIGIPKA----DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  629 VLLQKTPvtfdvsvweLFwwSFTGARL---SLLPP-----GAEKDPREMLRSIQRDAVTVIHFVPSMLtpfldlldgDPT 700
Cdd:cd05910  128 VDLATFP---------LF--ALFGPALgltSVIPDmdptrPARADPQKLVGAIRQYGVSIVFGSPALL---------ERV 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  701 ARAAA------SSLRLVFCSGEALAPLQVARFRRLFGDAVRLVNLYGPTEA--TVDVSDHE------CASDNPTRVPIGR 766
Cdd:cd05910  188 ARYCAqhgitlPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlpVSSIGSREllatttAATSGGAGTCVGR 267

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  767 PIDNLRLYVL----------DRALRpQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPfvAGGRLYRTGDLARWLAD 836
Cdd:cd05910  268 PIPGVRVRIIeiddepiaewDDTLE-LPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN--SEGFWHRMGDLGYLDDE 344

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  837 GNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYY-VAAAELDPGQLRAGLSATLPDFM 915
Cdd:cd05910  345 GRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEpLPGTITPRARLEQELRALAKDYP 424

                        490       500
                 ....*....|....*....|....*....
gi 15598523  916 LPAFFVRI---DSLPLSA--NGKLDRRQL 939
Cdd:cd05910  425 HTQRIGRFlihPSFPVDIrhNAKIFREKL 453
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1477-1969 3.62e-24

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 109.59  E-value: 3.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1477 VVSLFERQVEALPGSAALAFEEQRW--TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVP 1554
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1555 LDVSYPA--QRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQLD-------------------E 1613
Cdd:PRK05852   98 LDPALPIaeQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHldaateptpatstpeglrpD 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1614 LAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAF-QEIFSTLCGGGELqLISNRER--- 1689
Cdd:PRK05852  178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLiAALLATLASGGAV-LLPARGRfsa 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1690 ------MDPSALLHVLERRQVQRVLLPFVALQRLAEASNALG-VRPGALRVVVSSGEQLRITEDVRAFCAampglllenq 1762
Cdd:PRK05852  257 htfwddIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRfIRSCSAPLTAETAQALQTEFAAPVVCA---------- 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1763 YGPTE-THQVTYHSLSG-DPAHYPDLP--PIGRPlDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERF 1838
Cdd:PRK05852  327 FGMTEaTHQVTTTQIEGiGQTENPVVStgLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1839 VeHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQG-NDAFL 1917
Cdd:PRK05852  406 T-DGW------LRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVL----ASHPNVMEAAVFGVPDQLyGEAVA 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15598523  1918 AAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAAL 1969
Cdd:PRK05852  475 AVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 442-935 3.85e-24

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 111.55  E-value: 3.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   442 PEQATLPTLFAEQVARTPQRTALLEADGGTLSYAELDAKVQAVADALRAaGVRTDERVALLvargphlLPAilgvqRAGG 521
Cdd:PRK08633  612 EALPPLAEAWIDTAKRNWSRLAVADSTGGELSYGKALTGALALARLLKR-ELKDEENVGIL-------LPP-----SVAG 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   522 AY----------VPINPDHPLER--VRLLLEDCGARVVLVDER-------AATLGESLGETRVLHLERLPQ--STGD--- 577
Cdd:PRK08633  679 ALanlalllagkVPVNLNYTASEaaLKSAIEQAQIKTVITSRKfleklknKGFDLELPENVKVIYLEDLKAkiSKVDklt 758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   578 -------LPA--------ANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPvtfdvsv 642
Cdd:PRK08633  759 allaarlLPArllkrlygPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLP------- 831

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   643 welFWWSFtGARLSLLPPGAE-------KDPREML---RSIQRDAVTVIHFVPSMLTPFLDLLDGDPtarAAASSLRLVF 712
Cdd:PRK08633  832 ---FFHSF-GLTVTLWLPLLEgikvvyhPDPTDALgiaKLVAKHRATILLGTPTFLRLYLRNKKLHP---LMFASLRLVV 904

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   713 CSGEALAPLQVARFRRLFGdaVRLVNLYGPTE----ATVDVSDHECASDNPTRV----PIGRPIDNLRLYVLD-RALRPQ 783
Cdd:PRK08633  905 AGAEKLKPEVADAFEEKFG--IRILEGYGATEtspvASVNLPDVLAADFKRQTGskegSVGMPLPGVAVRIVDpETFEEL 982

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   784 PLGAVGELYIGGVGVARGYLNRPELNAErFLVDpfVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRD 863
Cdd:PRK08633  983 PPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKD--IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEE 1059

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598523   864 RLAALPGVRDA--AVVARDSAVRGTHLVgYYVAAAELDPGQLRAGLSAT-LPDFMLPAFFVRIDSLPLSANGKLD 935
Cdd:PRK08633 1060 ELAKALGGEEVvfAVTAVPDEKKGEKLV-VLHTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLD 1133
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 1462-1975 6.00e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 109.09  E-value: 6.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1462 APRRDAASQPEPLVD--VVSLFERQVEALPGSAALAFEEQ--RWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSP 1536
Cdd:PRK12583    3 QPSYYQGGGDKPLLTqtIGDAFDATVARFPDREALVVRHQalRYTWRQLaDAVDR-LARGLLALGVQPGDRVGIWAPNCA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1537 EMIATIWGILRAGLVCVPLDVSYPAQRLALILE--------TAQPFR---------------------VVAHPEHAH--- 1584
Cdd:PRK12583   82 EWLLTQFATARIGAILVNINPAYRASELEYALGqsgvrwviCADAFKtsdyhamlqellpglaegqpgALACERLPElrg 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1585 -----VAAAERVLPVEELVAdiEPETFAAPQLDELAM---------LLFTSGSTGRPKGVELSHRMWANyTQWQLRVASG 1650
Cdd:PRK12583  162 vvslaPAPPPGFLAWHELQA--RGETVSREALAERQAsldrddpinIQYTSGTTGFPKGATLSHHNILN-NGYFVAESLG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1651 VPGLRTLqFAPLSFDMAFQEIFSTL-CGGGELQLISNRERMDPSALLHVLERRQ---VQRVLLPFVAL----QRLAEASN 1722
Cdd:PRK12583  239 LTEHDRL-CVPVPLYHCFGMVLANLgCMTVGACLVYPNEAFDPLATLQAVEEERctaLYGVPTMFIAEldhpQRGNFDLS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1723 AL--GVRPGA--LRVVVSsgeqlRITEDVRafcaaMPGLLLenQYGPTETHQVTYHSLSGDPAHYpDLPPIGRPLDGVEV 1798
Cdd:PRK12583  318 SLrtGIMAGApcPIEVMR-----RVMDEMH-----MAEVQI--AYGMTETSPVSLQTTAADDLER-RVETVGRTQPHLEV 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1799 QVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRG 1878
Cdd:PRK12583  385 KVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW------MHTGDLATMDEQGYVRIVGRSKDMIIRGG 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1879 FRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDafLAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVDG 1955
Cdd:PRK12583  459 ENIYPREIEEFLF----THPAVADVQVfgVPDEKYGEE--IVAWVRLHPgHAASEEELREFCKARIAHFKVPRYFRFVDE 532

                         570       580
                  ....*....|....*....|
gi 15598523  1956 FALTPSGKRDDAALRALPLE 1975
Cdd:PRK12583  533 FPMTVTGKVQKFRMREISIE 552
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 754-1028 7.26e-24

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 104.45  E-value: 7.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  754 CASDNPTRVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVA-RGYLNRPELNAERFLVDPFVAGGRLYRTGDLAR 832
Cdd:COG3433   10 PPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLlRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  833 WLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLP 912
Cdd:COG3433   90 RRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  913 DFMLPAFFVRIDSLPLSANGKLDRRQLPAPP--------EQVAAVAPRTATEAELAAVWADVLGV--AEVGVHDDFYALG 982
Cdd:COG3433  170 PDVVAASAVVALDALLLLALKVVARAAPALAaaeallaaASPAPALETALTEEELRADVAELLGVdpEEIDPDDNLFDLG 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15598523  983 GDSILMLRIRAAAQRRGLGFELADLMRNPTVAGLAERLVRPLAERS 1028
Cdd:COG3433  250 LDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 1489-1971 7.63e-24

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 108.05  E-value: 7.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:PRK06145   16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1569 ETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQL----------DELAMLLFTSGSTGRPKGVELSHR--M 1636
Cdd:PRK06145   96 GDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLeippqaavapTDLVRLMYTSGTTDRPKGVMHSYGnlH 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1637 WANYTQwqlRVASGVPG-LRTLQFAPLSFDMAFQ-EIFSTLCGGGELQLISNrerMDPSALLHVLERRQVQRVLLPFVAL 1714
Cdd:PRK06145  176 WKSIDH---VIALGLTAsERLLVVGPLYHVGAFDlPGIAVLWVGGTLRIHRE---FDPEAVLAAIERHRLTCAWMAPVML 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1715 QRLAEASNALGVRPGALRVVVSSGE---QLRItedvRAFCAAMPGLLLENQYGPTEThqVTYHSLSGDPAHYPDLPPIGR 1791
Cdd:PRK06145  250 SRVLTVPDRDRFDLDSLAWCIGGGEktpESRI----RDFTRVFTRARYIDAYGLTET--CSGDTLMEAGREIEKIGSTGR 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1792 PLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRAD 1871
Cdd:PRK06145  324 ALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-W------FRSGDVGYLDEEGFLYLTDRKK 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1872 TQVKVRGFRIEPAEVELAIMRQAErqpgLRGAAVV-ARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHF 1950
Cdd:PRK06145  397 DMIISGGENIASSEVERVIYELPE----VAEAAVIgVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQL 472

                         490       500
                  ....*....|....*....|.
gi 15598523  1951 AWVDGFALTPSGKRDDAALRA 1971
Cdd:PRK06145  473 KVRDELPRNPSGKVLKRVLRD 493
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 1492-1963 8.09e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 108.07  E-value: 8.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1492 AALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETA 1571
Cdd:PRK08276    3 VIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1572 QPFRVVAHP---EHAHVAAAERVLPVEELVADIEPETFAAPQLDELA--------------MLLFTSGSTGRPKGV--EL 1632
Cdd:PRK08276   83 GAKVLIVSAalaDTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAaqpdtpiadetagaDMLYSSGTTGRPKGIkrPL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1633 SHR---MWANYTQWQL-RVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQV---Q 1705
Cdd:PRK08276  163 PGLdpdEAPGMMLALLgFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVM---EKFDAEEALALIERYRVthsQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1706 RVLLPFVALQRLAEAsnalgVRPgalRVVVSSgeqLRitedvRAFCAAMP-------------GLLLENQYGPTETHQVT 1772
Cdd:PRK08276  240 LVPTMFVRMLKLPEE-----VRA---RYDVSS---LR-----VAIHAAAPcpvevkramidwwGPIIHEYYASSEGGGVT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1773 YHSlSGDPAHYPDlpPIGRPLDGvEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRT 1852
Cdd:PRK08276  304 VIT-SEDWLAHPG--SVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW------VTV 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1853 GDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGND--AFLAAFLLGEPEAV 1928
Cdd:PRK08276  374 GDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLV----THPKVADVAVfgVPDEEMGERvkAVVQPADGADAGDA 449

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 15598523  1929 DLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK08276  450 LAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGK 484
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 587-934 9.27e-24

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: 104.89  E-value: 9.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  587 DLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPvtfdvsvwelFWWSF---TGARLSLLP---- 659
Cdd:cd17638    1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINP----------FFHTFgykAGIVACLLTgatv 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  660 -PGAEKDPREMLRSIQRDAVTVihfVPSMLTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFG-DAVrlV 737
Cdd:cd17638   71 vPVAVFDVDAILEAIERERITV---LPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfETV--L 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  738 NLYGPTEATVDVSdheC-ASDNPTRVP--IGRPIDNLRLYVLDRalrpqplgavGELYIGGVGVARGYLNRPELNAERfl 814
Cdd:cd17638  146 TAYGLTEAGVATM---CrPGDDAETVAttCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEA-- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  815 VDpfvAGGRLYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGThlVG-YYV 893
Cdd:cd17638  211 ID---ADGWLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGE--VGkAFV 284

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 15598523  894 AAAE---LDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKL 934
Cdd:cd17638  285 VARPgvtLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK05857 PRK05857
fatty acid--CoA ligase;
453-941 3.02e-23

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 106.63  E-value: 3.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   453 EQVARTPQRTALLEADGGT-LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHP 531
Cdd:PRK05857   22 EQARQQPEAIALRRCDGTSaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   532 LERVRLLLEDCGARVVLVDER----AATLGESLGETRVLHLERLPQSTG-------DLPAANVAPG--DLAYVIYTSGST 598
Cdd:PRK05857  102 IAAIERFCQITDPAAALVAPGskmaSSAVPEALHSIPVIAVDIAAVTREsehsldaASLAGNADQGseDPLAMIFTSGTT 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   599 GMPKGVMVEHRSVV--------NRLNWMQrrYPIGErdVLLQKTPVTFDVSVwelfWWSFTG-ARLSLLPPGAEKDP--R 667
Cdd:PRK05857  182 GEPKAVLLANRTFFavpdilqkEGLNWVT--WVVGE--TTYSPLPATHIGGL----WWILTClMHGGLCVTGGENTTslL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   668 EMLRSiqrDAVTVIHFVPSMLTPFLDLLDgdpTARAAASSLRLVFCSG-EALAplqvARFRRLFGDAVRLVNLYGPTEAT 746
Cdd:PRK05857  254 EILTT---NAVATTCLVPTLLSKLVSELK---SANATVPSLRLVGYGGsRAIA----ADVRFIEATGVRTAQVYGLSETG 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   747 VDVSDHECASDNPTRV---PIGRPIDNLRLYVLD------RALRPQPLGAVGELYIGGVGVARGYLNRPELNAErFLVDP 817
Cdd:PRK05857  324 CTALCLPTDDGSIVKIeagAVGRPYPGVDVYLAAtdgigpTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAE-VLIDG 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   818 FVaggrlyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVrDRLA-ALPGVRDAAVVARDSAVRGThLVGYYV-AA 895
Cdd:PRK05857  403 WV------NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEV-DRIAeGVSGVREAACYEIPDEEFGA-LVGLAVvAS 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15598523   896 AELDPGQLRAgLSATLP--------DFMLPAFFVRIDSLPLSANGKLDRRQLPA 941
Cdd:PRK05857  475 AELDESAARA-LKHTIAarfrresePMARPSTIVIVTDIPRTQSGKVMRASLAA 527
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 6-336 3.04e-23

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: 105.42  E-value: 3.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    6 RLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEARH 85
Cdd:cd20483    1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   86 VDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVR-THHIVSDAWGLQLFLSRVRAGYLGELgepq 164
Cdd:cd20483   81 IDLSEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLaSHHIAWDRGSSKSIFEQFTALYDALR---- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  165 AQMPTASLLAQ-LETDDYS-------GSEQYRGDRAYFAEALEGLEPAL----F--TRRRPAGLRRTARHRLTLERTLLD 230
Cdd:cd20483  157 AGRDLATVPPPpVQYIDFTlwhnallQSPLVQPLLDFWKEKLEGIPDASkllpFakAERPPVKDYERSTVEATLDKELLA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  231 AIRD----RGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLRE 306
Cdd:cd20483  237 RMKRicaqHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKT 316

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 15598523  307 ATRTLLRHQKMPLGDLL--------RGASPLFDTTLSY 336
Cdd:cd20483  317 TCLEAYEHSAVPFDYIVdaldvprsTSHFPIGQIAVNY 354
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 1476-1970 3.29e-23

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: 106.43  E-value: 3.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1476 DVVslfERQVEALPGSAALAF-----EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGL 1550
Cdd:cd05970   21 DVV---DAMAKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1551 VCVPLDVSYPAQRLALILETAQPFRVVAH-----PEHAHVAAAE-RVLPVEELVADIEPETF---------AAPQL---- 1611
Cdd:cd05970   98 IAIPATHQLTAKDIVYRIESADIKMIVAIaedniPEEIEKAAPEcPSKPKLVWVGDPVPEGWidfrkliknASPDFerpt 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1612 -------DELAMLLFTSGSTGRPKGVE------LSHRMWANYtqWQ-LRvasgvPGLRTLQFAPLSFDMA-FQEIFSTLC 1676
Cdd:cd05970  178 ansypcgEDILLVYFSSGTTGMPKMVEhdftypLGHIVTAKY--WQnVR-----EGGLHLTVADTGWGKAvWGKIYGQWI 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1677 GGGELqLISNRERMDPSALLHVLERRQVQRVLLP-----FVALQRLAEASNAlgvrpgALRVVVSSGEQLriTEDVRAFC 1751
Cdd:cd05970  251 AGAAV-FVYDYDKFDPKALLEKLSKYGVTTFCAPptiyrFLIREDLSRYDLS------SLRYCTTAGEAL--NPEVFNTF 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1752 AAMPGLLLENQYGPTEThQVTYHSLsgdPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELY--------FGgdcL 1823
Cdd:cd05970  322 KEKTGIKLMEGFGQTET-TLTIATF---PWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVirtskgkpVG---L 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1824 ARGYHRAPKLTAErfvehPWRPGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGA 1903
Cdd:cd05970  395 FGGYYKDAEKTAE-----VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALI----QHPAVLEC 463

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523 1904 AV--VARERQGNdAFLAAFLLGEPeavdlAELKQALRSELPEHM--------VPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd05970  464 AVtgVPDPIRGQ-VVKATIVLAKG-----YEPSEELKKELQDHVkkvtapykYPRIVEFVDELPKTISGKIRRVEIR 534
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 455-939 3.86e-23

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 105.93  E-value: 3.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   455 VARTPQRTALLEA-DGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLE 533
Cdd:PRK13391    7 AQTTPDKPAVIMAsTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   534 RVRLLLEDCGARVVLVDERAATLGESLGET--RVLH------------LERLPQSTGDLPAANVAP---GDLayVIYTSG 596
Cdd:PRK13391   87 EAAYIVDDSGARALITSAAKLDVARALLKQcpGVRHrlvldgdgelegFVGYAEAVAGLPATPIADeslGTD--MLYSSG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   597 STGMPKGVMVE--HRSVVNRLN---WMQRRYPIGERDVLLQKTPVTFDVSVwelfWWSFTGARLSLLPPGAEK-DPREML 670
Cdd:PRK13391  165 TTGRPKGIKRPlpEQPPDTPLPltaFLQRLWGFRSDMVYLSPAPLYHSAPQ----RAVMLVIRLGGTVIVMEHfDAEQYL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   671 RSIQRDAVTVIHFVPSMLTPFLDLLDgDPTARAAASSLRLVFcSGEALAPLQVAR-FRRLFGDAVRlvNLYGPTEAT-VD 748
Cdd:PRK13391  241 ALIEEYGVTHTQLVPTMFSRMLKLPE-EVRDKYDLSSLEVAI-HAAAPCPPQVKEqMIDWWGPIIH--EYYAATEGLgFT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   749 VSDHECASDNPTRVpiGRPIDNlRLYVLDRALRPQPLGAVGELYIGGvGVARGYLNRPELNAERFLVDPfvaggRLYRTG 828
Cdd:PRK13391  317 ACDSEEWLAHPGTV--GRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----TWSTVG 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   829 DLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAV--VARDSAVRGTHLVGYYVAAAELDP---GQL 903
Cdd:PRK13391  388 DIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfgVPNEDLGEEVKAVVQPVDGVDPGPalaAEL 467

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 15598523   904 RAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK13391  468 IAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 1479-1963 4.21e-23

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: 105.46  E-value: 4.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1479 SLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVS 1558
Cdd:cd12118    8 SFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1559 YPAQRLALILETAQPFRVVAHPEHAHvaaaervlpvEELVADIEPETFAAPQLDELAM--LLFTSGSTGRPKGVELSHR- 1635
Cdd:cd12118   88 LDAEEIAFILRHSEAKVLFVDREFEY----------EDLLAEGDPDFEWIPPADEWDPiaLNYTSGTTGRPKGVVYHHRg 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1636 ----MWANYTQWQLRVAS------------------GVPG-------LRTLQfAPLSFDMAFQEIFSTLCGGGE-LQLIS 1685
Cdd:cd12118  158 aylnALANILEWEMKQHPvylwtlpmfhcngwcfpwTVAAvggtnvcLRKVD-AKAIYDLIEKHKVTHFCGAPTvLNMLA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1686 NrerMDPSALLHVLERRQVQR--VLLPFVALQRLaeasNALGvrpgaLRVVVSSGeqLRITEDVRAFCAAMP---GLLLE 1760
Cdd:cd12118  237 N---APPSDARPLPHRVHVMTagAPPPAAVLAKM----EELG-----FDVTHVYG--LTETYGPATVCAWKPewdELPTE 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1761 NQYGPTETHQVTYHSLSgdpahypdlppigrpldgvEVQVLDAA-LRPVPV-GVT-GELYFGGDCLARGYHRAPKLTAER 1837
Cdd:cd12118  303 ERARLKARQGVRYVGLE-------------------EVDVLDPEtMKPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEA 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1838 FvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGND- 1914
Cdd:cd12118  364 F-RGGW------FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLY----KHPAVLEAAVVARpdEKWGEVp 432

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 15598523 1915 -AFLAaflLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDgFALTPSGK 1963
Cdd:cd12118  433 cAFVE---LKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 1493-1970 5.93e-23

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 105.53  E-value: 5.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1493 ALAFEE-----QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI 1567
Cdd:PRK08008   25 ALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1568 LETAQPFRVVAHPEHA---------------HVAAAERVLPVEELVADIE-------PETFAAPQL--DELAMLLFTSGS 1623
Cdd:PRK08008  105 LQNSQASLLVTSAQFYpmyrqiqqedatplrHICLTRVALPADDGVSSFTqlkaqqpATLCYAPPLstDDTAEILFTSGT 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1624 TGRPKGVELSH---RMWANYTQWQ--LRVASgvpglRTLQFAPlSFDMAFQ-----EIFSTlcgGGELQLIsnrERMDPS 1693
Cdd:PRK08008  185 TSRPKGVVITHynlRFAGYYSAWQcaLRDDD-----VYLTVMP-AFHIDCQctaamAAFSA---GATFVLL---EKYSAR 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1694 ALLhvlerRQVQR----------VLLPFVALQRLAEASnalgvRPGALRVV-----VSSGEQLritedvrAFCAAMpGLL 1758
Cdd:PRK08008  253 AFW-----GQVCKyratitecipMMIRTLMVQPPSAND-----RQHCLREVmfylnLSDQEKD-------AFEERF-GVR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1759 LENQYGPTETHQVTYHSLSGDPAHYPDlppIGRPLDGVEVQVLDAALRPVPVGVTGELYFG---GDCLARGYHRAPKLTA 1835
Cdd:PRK08008  315 LLTSYGMTETIVGIIGDRPGDKRRWPS---IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATA 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1836 ERFVEHPWrpgarLYrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDA 1915
Cdd:PRK08008  392 KVLEADGW-----LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIA----THPKIQDIVVVGIKDSIRDE 461

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  1916 FLAAF-LLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:PRK08008  462 AIKAFvVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 1483-1963 6.36e-23

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 105.40  E-value: 6.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1483 RQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQ 1562
Cdd:PRK08316   19 RSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1563 RLALILETAQPFRVVAHPEHA-HVAAAERVLPVEELVADI--------------------EPETFAAPQLDE--LAMLLF 1619
Cdd:PRK08316   99 ELAYILDHSGARAFLVDPALApTAEAALALLPVDTLILSLvlggreapggwldfadwaeaGSVAEPDVELADddLAQILY 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1620 TSGSTGRPKGVELSHR--MWanytQWQLRVASG--VPGLRTLQFAPLsFDMAFQEIF---STLCGGGELQLisnrERMDP 1692
Cdd:PRK08316  179 TSGTESLPKGAMLTHRalIA----EYVSCIVAGdmSADDIPLHALPL-YHCAQLDVFlgpYLYVGATNVIL----DAPDP 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1693 SALLHVLERRQVQRVLLP---FVALQRlaeasnalgvRPGALRVVVSSgeqLR------------ITEDVRafcAAMPGL 1757
Cdd:PRK08316  250 ELILRTIEAERITSFFAPptvWISLLR----------HPDFDTRDLSS---LRkgyygasimpveVLKELR---ERLPGL 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1758 LLENQYGPTEThqVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAER 1837
Cdd:PRK08316  314 RFYNCYGQTEI--APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEA 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1838 FvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA--RERQGnDA 1915
Cdd:PRK08316  392 F-RGGW------FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALY----THPAVAEVAVIGlpDPKWI-EA 459

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 15598523  1916 FLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK08316  460 VTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGK 507
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 1501-1963 7.20e-23

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: 103.97  E-value: 7.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1501 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDvsypaqrlaliletaqpfrvvahp 1580
Cdd:cd05912    2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN------------------------ 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1581 ehAHVAAAERVLPVEElvadiepetfAAPQLDELAMLLFTSGSTGRPKGVELSHRM-WANYTQWQLRVasgvpGL----R 1655
Cdd:cd05912   58 --TRLTPNELAFQLKD----------SDVKLDDIATIMYTSGTTGKPKGVQQTFGNhWWSAIGSALNL-----GLteddN 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1656 TLQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNalGVRPGALRVVV 1735
Cdd:cd05912  121 WLCALPLFHISGLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILG--EGYPNNLRCIL 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1736 SSGEQlrITEDVRAFCAAMpGLLLENQYGPTET-HQVTyhSLSGDPAHyPDLPPIGRPLDGVEVQVLDAALRPVPVgvtG 1814
Cdd:cd05912  196 LGGGP--APKPLLEQCKEK-GIPVYQSYGMTETcSQIV--TLSPEDAL-NKIGSAGKPLFPVELKIEDDGQPPYEV---G 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1815 ELYFGGDCLARGYHRAPKLTAERFvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRQa 1894
Cdd:cd05912  267 EILLKGPNVTKGYLNRPDATEESF-ENGW------FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE-EVLLS- 337

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523 1895 erQPGLRGAAVVARERQGNDAFLAAFLLGEPEaVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd05912  338 --HPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1050-1379 1.83e-22

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: 102.87  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1050 FPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFdLSGASEPLQLV--HTqARSEP 1127
Cdd:cd19066    2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQVVldKT-VRFRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1128 LILDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAF-VREDGLDLVFSFHHAILDGWSVANLIVALVAAYRG---- 1202
Cdd:cd19066   80 EIIDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFrLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerq 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1203 ----EPLPGPAPALACHVREELAALASPAAVGYWTGLLEGAR---MTRLDGFGAHEPQAAQGPAShrEALPDGLLERLKA 1275
Cdd:cd19066  160 kptlPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPpplPLPKAKRPSQVASYEVLTLE--FFLRSEETKRLRE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1276 TAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIA-GCSWIEVADALFRQER 1354
Cdd:cd19066  238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD-EAVEDTIGLFLNLLPLRIDTSpDATFPELLKRTKEQSR 316

                        330       340
                 ....*....|....*....|....*
gi 15598523 1355 DGHAHRRYPLSAIQQIVGDELSSAF 1379
Cdd:cd19066  317 EAIEHQRVPFIELVRHLGVVPEAPK 341
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
484-981 2.48e-22

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 104.73  E-value: 2.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   484 VADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDeraATLGESLGET 563
Cdd:PRK06060   43 LGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTS---DALRDRFQPS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   564 RVLHLERLPQSTGDLPAANVAP--GD-LAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRR-YPIGERDVLLQKTPVTFD 639
Cdd:PRK06060  120 RVAEAAELMSEAARVAPGGYEPmgGDaLAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFA 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   640 VSVWELFWWSF-TG--ARLSLLPPGAEKdpREMLRSiqRDAVTVIHFVPSMLTPFLDLLDGDptaraAASSLRLVFCSGE 716
Cdd:PRK06060  200 YGLGNSVWFPLaTGgsAVINSAPVTPEA--AAILSA--RFGPSVLYGVPNFFARVIDSCSPD-----SFRSLRCVVSAGE 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   717 ALAPLQVARFRRLFGdAVRLVNLYGPTEATvdvsdhecasdnptRVPIGRPIDNLRLYVLDRALRP------QPLGAV-- 788
Cdd:PRK06060  271 ALELGLAERLMEFFG-GIPILDGIGSTEVG--------------QTFVSNRVDEWRLGTLGRVLPPyeirvvAPDGTTag 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   789 ----GELYIGGVGVARGYLNRPelnaerflvDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDR 864
Cdd:PRK06060  336 pgveGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERL 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   865 LAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDPGQLR---AGLSATLPDFMLPAFFVRIDSLPLSANGKLDRR-- 937
Cdd:PRK06060  407 IIEDEAVAEAAVVAVRESTGASTLQAFLVATsgATIDGSVMRdlhRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGal 486

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15598523   938 --QLPAPP-EQVAAVAPRTATEAEL-----AAVWADVLGVAEVGVHDDFYAL 981
Cdd:PRK06060  487 rkQSPTKPiWELSLTEPGSGVRAQRddlsaSNMTIAGGNDGGATLRERLVAL 538
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 469-880 2.80e-22

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: 102.91  E-value: 2.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  469 GGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVL 548
Cdd:cd05914    5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  549 VDEraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERD 628
Cdd:cd05914   85 VSD---------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGD 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  629 VLLQKTPV--TFDVsVWELFWWSFTGARLSLLppgaEKDPREMLRSIQRDAVTVIHFVP----------------SMLTP 690
Cdd:cd05914  132 KILSILPLhhIYPL-TFTLLLPLLNGAHVVFL----DKIPSAKIIALAFAQVTPTLGVPvplviekifkmdiipkLTLKK 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  691 FLDLLDGDPTARAAASSLRL-----------VFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVSdhecaSDNP 759
Cdd:cd05914  207 FKFKLAKKINNRKIRKLAFKkvheafggnikEFVIGGAKINPDVEEFLRTIG--FPYTIGYGMTETAPIIS-----YSPP 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  760 TRVPI---GRPIDNLRLYVLDralrPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLAD 836
Cdd:cd05914  280 NRIRLgsaGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAE 349

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 15598523  837 GNLEYLGRADDQ-VKIRGNRVEPDEVRDRLAALPGVRDAAVVARD 880
Cdd:cd05914  350 GYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQE 394
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 591-936 3.36e-22

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: 100.42  E-value: 3.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  591 VIYTSGSTGMPKGVMVEHRSVVnrLNWMQRRYPIG--ERDVLLQKTPvtfdvsvweLFWWSFTGARLSLLPPGA-----E 663
Cdd:cd17637    5 IIHTAAVAGRPRGAVLSHGNLI--AANLQLIHAMGltEADVYLNMLP---------LFHIAGLNLALATFHAGGanvvmE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  664 K-DPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPtarAAASSLRLVFcsgeAL-APLQVARFRRLFGdaVRLVNLYG 741
Cdd:cd17637   74 KfDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSG---VDLSSLRHVL----GLdAPETIQRFEETTG--ATFWSLYG 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  742 PTEATVDVSDHEcASDNPTRVpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlvdpfvAG 821
Cdd:cd17637  145 QTETSGLVTLSP-YRERPGSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF------RN 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  822 GrLYRTGDLARWLADGNLEYLGR--ADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVArdsavrgthlvgyyVAAAELD 899
Cdd:cd17637  216 G-WHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIG--------------VPDPKWG 280

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15598523  900 PG-----QLRAGLSAT---LPDFM--------LPAFFVRIDSLPLSANGKLDR 936
Cdd:cd17637  281 EGikavcVLKPGATLTadeLIEFVgsriarykKPRYVVFVEALPKTADGSIDR 333
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 1502-1972 3.55e-22

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: 102.79  E-value: 3.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1502 TYRDLdHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD--VSYPAQRLAL-------ILeTAQ 1572
Cdd:cd05909    9 TYRKL-LTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNytAGLRELRACIklagiktVL-TSK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1573 PF-RVVAHPEHAHVAAAERVLPVEELVADIE--------------PET-----FAAP-QLDELAMLLFTSGSTGRPKGVE 1631
Cdd:cd05909   87 QFiEKLKLHHLFDVEYDARIVYLEDLRAKISkadkckaflagkfpPKWllrifGVAPvQPDDPAVILFTSGSEGLPKGVV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1632 LSHR-MWANYTQwQLRVASGVPGLRTLQFAPL--SFDMAFQeIFSTLCGGGELQLISNRerMDPSALLHVLERRQVQRVL 1708
Cdd:cd05909  167 LSHKnLLANVEQ-ITAIFDPNPEDVVFGALPFfhSFGLTGC-LWLPLLSGIKVVFHPNP--LDYKKIPELIYDKKATILL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1709 LPFVALQRLAEASNALGVRpgALRVVVSSGEQLRitEDVRAFCAAMPGLLLENQYGPTETHQVtyhsLSGDPAHYPDLP- 1787
Cdd:cd05909  243 GTPTFLRGYARAAHPEDFS--SLRLVVAGAEKLK--DTLRQEFQEKFGIRILEGYGTTECSPV----ISVNTPQSPNKEg 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1788 PIGRPLDGVEVQVLD-AALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFvEHPWrpgarlYRTGDLGRILGNGEIVW 1866
Cdd:cd05909  315 TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGW------YDTGDIGKIDGEGFLTI 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1867 LGRADTQVKVRGFRIEPAEVELAIMrqaERQPGLRGAAVVAR--ERQGNdaflAAFLLGEPEAVDLAELKQALR-SELPE 1943
Cdd:cd05909  388 TGRLSRFAKIAGEMVSLEAIEDILS---EILPEDNEVAVVSVpdGRKGE----KIVLLTTTTDTDPSSLNDILKnAGISN 460

                        490       500
                 ....*....|....*....|....*....
gi 15598523 1944 HMVPAHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:cd05909  461 LAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 459-936 3.56e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 102.94  E-value: 3.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   459 PQRTALLEADGgTLSYAELDAKVQAVADALRAAGVRtDERVALLVARGPHLLPAILGVQRAGGAYVPINPD-HPLERV-R 536
Cdd:PRK07638   15 PNKIAIKENDR-VLTYKDWFESVCKVANWLNEKESK-NKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKwKQDELKeR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   537 LLLEDCGarvVLVDERAATLGESLGETRVLHLERLPQSTgDLPAANVAPG-----DLAYVIYTSGSTGMPKGVMVEHRSV 611
Cdd:PRK07638   93 LAISNAD---MIVTERYKLNDLPDEEGRVIEIDEWKRMI-EKYLPTYAPIenvqnAPFYMGFTSGSTGKPKAFLRAQQSW 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   612 VNRLNWMQRRYPIGERD-VLLQKTPVTfdvsvwELFWWS-----FTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVP 685
Cdd:PRK07638  169 LHSFDCNVHDFHMKREDsVLIAGTLVH------SLFLYGaistlYVGQTVHLMR---KFIPNQVLDKLETENISVMYTVP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   686 SMLTPFLDlldgdptARAAASSLRLVFCSGEALAPLQVARFRRLFGDAvRLVNLYGPTEAT-VDVSDHECASDNPTRVpi 764
Cdd:PRK07638  240 TMLESLYK-------ENRVIENKMKIISSGAKWEAEAKEKIKNIFPYA-KLYEFYGASELSfVTALVDEESERRPNSV-- 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   765 GRPIDNLRLYVLDRA-LRPQPlGAVGELYIGGVGVARGYLNrpelnaerflvdpfvaGGRLYRTGDLARWLADGNLEYL- 842
Cdd:PRK07638  310 GRPFHNVQVRICNEAgEEVQK-GEIGTVYVKSPQFFMGYII----------------GGVLARELNADGWMTVRDVGYEd 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   843 --------GRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAelDPGQLRAGLSATLPDF 914
Cdd:PRK07638  373 eegfiyivGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSA--TKQQLKSFCLQRLSSF 450

                         490       500
                  ....*....|....*....|..
gi 15598523   915 MLPAFFVRIDSLPLSANGKLDR 936
Cdd:PRK07638  451 KIPKEWHFVDEIPYTNSGKIAR 472
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 456-939 4.98e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 102.39  E-value: 4.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   456 ART-PQRTALLEADGG-TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLE 533
Cdd:PRK13390    7 AQIaPDRPAVIVAETGeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   534 RVRLLLEDCGARVVL----VDERAATLGESLgETRVLHLERLpQSTGDLPAANVAPGDL-------AYVIYTSGSTGMPK 602
Cdd:PRK13390   87 EADYIVGDSGARVLVasaaLDGLAAKVGADL-PLRLSFGGEI-DGFGSFEAALAGAGPRlteqpcgAVMLYSSGTTGFPK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   603 GVM--VEHRSVVNR----LNWMQRRYPIGERDVLLQKTPVTFDVSvweLFWWSFTGARLSLLPPGAEKDPREMLRSIQRD 676
Cdd:PRK13390  165 GIQpdLPGRDVDAPgdpiVAIARAFYDISESDIYYSSAPIYHAAP---LRWCSMVHALGGTVVLAKRFDAQATLGHVERY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   677 AVTVIHFVPSMLTPFLDlLDGDPTARAAASSLRLVFcsgEALAPLQVARFRRLFGDAVRLV-NLYGPTEA----TVDVSD 751
Cdd:PRK13390  242 RITVTQMVPTMFVRLLK-LDADVRTRYDVSSLRAVI---HAAAPCPVDVKHAMIDWLGPIVyEYYSSTEAhgmtFIDSPD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   752 HECASDNPTRVPIGrpidnlRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAE-RFLVDPFVAggrlyRTGDL 830
Cdd:PRK13390  318 WLAHPGSVGRSVLG------DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWT-----TVGDL 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   831 ARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPG-----QLRA 905
Cdd:PRK13390  387 GSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSdelarELID 466

                         490       500       510
                  ....*....|....*....|....*....|....
gi 15598523   906 GLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK13390  467 YTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1059-1339 5.10e-22

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: 101.66  E-value: 5.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1059 LLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGAsEPLQLVHTQARSEPLILDLRGNPEA 1138
Cdd:cd19531   11 LWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG-EPVQVILPPLPLPLPVVDLSGLPEA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1139 G--TVLDEHIRQRRFHRYSLQQPGLfLFAAFVREDGLD--LVFSFHHAILDGWSVANLIVALVAAYR----GEPLPGPAP 1210
Cdd:cd19531   90 EreAEAQRLAREEARRPFDLARGPL-LRATLLRLGEDEhvLLLTMHHIVSDGWSMGVLLRELAALYAaflaGRPSPLPPL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1211 AL-----ACHVREELAALASPAAVGYWTGLLEGArmtrldgfgaHEP------------QAAQGpASHREALPDGLLERL 1273
Cdd:cd19531  169 PIqyadyAVWQREWLQGEVLERQLAYWREQLAGA----------PPVlelptdrprpavQSFRG-ARVRFTLPAELTAAL 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523 1274 KATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTG-AISN-GRPELpdaDRMVGLFLNTVPVRSEIAG 1339
Cdd:cd19531  238 RALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGtPVAGrNRAEL---EGLIGFFVNTLVLRTDLSG 302
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 1471-1963 1.06e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 102.15  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1471 PEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVR-AGARRGDAIGVALNRSPEMIATIWGILRAG 1549
Cdd:PRK05677   20 PDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1550 LVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAaaERVLP--------VEElVADIEP------------------ 1603
Cdd:PRK05677  100 LIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLA--EKVLPktgvkhviVTE-VADMLPplkrllinavvkhvkkmv 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1604 --------------------ETF--AAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPGLRTLQFA 1660
Cdd:PRK05677  177 payhlpqavkfndalakgagQPVteANPQADDVAVLQYTGGTTGVAKGAMLTHRnLVANMLQCRALMGSNLNEGCEILIA 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1661 PLS----FDMAFQEIFSTLCGGGELqLISNRErmDPSALLHVLERRQVQrvllPFVALQRLAEA-SNALGVRP---GALR 1732
Cdd:PRK05677  257 PLPlyhiYAFTFHCMAMMLIGNHNI-LISNPR--DLPAMVKELGKWKFS----GFVGLNTLFVAlCNNEAFRKldfSALK 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1733 VVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTyhslSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGV 1812
Cdd:PRK05677  330 LTLSGGMAL--QLATAERWKEVTGCAICEGYGMTETSPVV----SVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGE 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1813 TGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE--LAI 1890
Cdd:PRK05677  404 VGELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEdvLAA 477

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  1891 MrqaerqPG-LRGAAV-VARERQGNDafLAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK05677  478 L------PGvLQCAAIgVPDEKSGEA--IKVFVVVKPgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1489-1963 2.08e-21

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 100.42  E-value: 2.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 1568
Cdd:PRK03640   16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1569 ETAQPFRVVAHPEHAHVAAAERVLPVEELVA----DIEP-ETFaapQLDELAMLLFTSGSTGRPKGVELShrmWANYtqW 1643
Cdd:PRK03640   96 DDAEVKCLITDDDFEAKLIPGISVKFAELMNgpkeEAEIqEEF---DLDEVATIMYTSGTTGKPKGVIQT---YGNH--W 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1644 QLRVASGVP-GLRT----LQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQRLA 1718
Cdd:PRK03640  168 WSAVGSALNlGLTEddcwLAAVPIFHISGLSILMRSVIYGMRVVLV---EKFDAEKINKLLQTGGVTIISVVSTMLQRLL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1719 EasnALGVR--PGALRVVVSSGEQlrITEDVRAFCAAMpGLLLENQYGPTET-HQVTyhSLSGDPAHyPDLPPIGRPLDG 1795
Cdd:PRK03640  245 E---RLGEGtyPSSFRCMLLGGGP--APKPLLEQCKEK-GIPVYQSYGMTETaSQIV--TLSPEDAL-TKLGSAGKPLFP 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1796 VEVQVLDaALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVK 1875
Cdd:PRK03640  316 CELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG-W------FKTGDIGYLDEEGFLYVLDRRSDLII 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1876 VRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEpEAVDLAELKQALRSELPEHMVPAHFAWVDG 1955
Cdd:PRK03640  388 SGGENIYPAEIEEVLL----SHPGVAEAGVVGVPDDKWGQVPVAFVVKS-GEVTEEELRHFCEEKLAKYKVPKRFYFVEE 462


                  ....*...
gi 15598523  1956 FALTPSGK 1963
Cdd:PRK03640  463 LPRNASGK 470
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 442-923 2.08e-21

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 101.49  E-value: 2.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   442 PEQA-TLPTLFAEQVARTPQRTALLEaDGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAG 520
Cdd:PRK08279   33 PDSKrSLGDVFEEAAARHPDRPALLF-EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   521 GAYVPINP---DHPLE--------RVRLLLEDCGARV------VLVDERAATLGESLGETRVLHLErLPQSTGDLPAAN- 582
Cdd:PRK08279  112 AVVALLNTqqrGAVLAhslnlvdaKHLIVGEELVEAFeearadLARPPRLWVAGGDTLDDPEGYED-LAAAAAGAPTTNp 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   583 -----VAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTP----VTFDVSvwelfwWS---F 650
Cdd:PRK08279  191 asrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPlyhnTGGTVA------WSsvlA 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   651 TGARLSLlppgAEK-DPREMLRSIQRDAVTVIHFVPSMLTPfldLLDGDPTARAAASSLRLVFCSG---EALAPLQvARF 726
Cdd:PRK08279  265 AGATLAL----RRKfSASRFWDDVRRYRATAFQYIGELCRY---LLNQPPKPTDRDHRLRLMIGNGlrpDIWDEFQ-QRF 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   727 rrlfgdAV-RLVNLYGPTEAT-----VDVSDHECAsdnptRVPiGRPIDNLRL--YVLDRA---------LRPQPLGAVG 789
Cdd:PRK08279  337 ------GIpRILEFYAASEGNvgfinVFNFDGTVG-----RVP-LWLAHPYAIvkYDVDTGepvrdadgrCIKVKPGEVG 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   790 ELyIGGVGVAR---GYlNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLA 866
Cdd:PRK08279  405 LL-IGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALS 482

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523   867 ALPGVRD-----------------AAVVARDsavrgthlvgyyvaAAELDPGQLRAGLSATLPDFMLPAfFVRI 923
Cdd:PRK08279  483 GFPGVEEavvygvevpgtdgragmAAIVLAD--------------GAEFDLAALAAHLYERLPAYAVPL-FVRL 541
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
457-939 2.13e-21

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 100.83  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   457 RTPQRTALLeaDGG-TLSYAELDAKVQAVADALRAAGVRTDERV---------------ALLVArGPHLLPAILGVQRAG 520
Cdd:PRK10946   35 AASDAIAVI--CGErQFSYRELNQASDNLACSLRRQGIKPGDTAlvqlgnvaefyitffALLKL-GVAPVNALFSHQRSE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   521 -GAYV-PINP-------DHPL----ERVRLLLEDCGA-RVVLVderaatLGESlGETRVLHLerLPQSTGDLPAANVAPG 586
Cdd:PRK10946  112 lNAYAsQIEPalliadrQHALfsddDFLNTLVAEHSSlRVVLL------LNDD-GEHSLDDA--INHPAEDFTATPSPAD 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   587 DLAYVIYTSGSTGMPKGVMVEH--------RSV-VNRLNwMQRRY----PIGERDVLlqKTPVTFDVsvwelFwwsFTGA 653
Cdd:PRK10946  183 EVAFFQLSGGSTGTPKLIPRTHndyyysvrRSVeICGFT-PQTRYlcalPAAHNYPM--SSPGALGV-----F---LAGG 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   654 RLSLLPpgaekDPREML--RSIQRDAVTVIHFVPSMLTPFLDLLDgDPTARAAASSLRLVFCSGEALAPLQVARFRRLFG 731
Cdd:PRK10946  252 TVVLAP-----DPSATLcfPLIEKHQVNVTALVPPAVSLWLQAIA-EGGSRAQLASLKLLQVGGARLSETLARRIPAELG 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   732 daVRLVNLYGPTEATVDVSDHEcasDNPTRV--PIGRPI-DNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPEL 808
Cdd:PRK10946  326 --CQLQQVFGMAEGLVNYTRLD---DSDERIftTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQH 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   809 NAERFLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHL 888
Cdd:PRK10946  401 NASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKS 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15598523   889 VGYYVAAAELDPGQLRAGLSAT-LPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK10946  475 CAFLVVKEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 7-409 2.61e-21

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: 99.06  E-value: 2.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    7 LPLSPYQRDIWVAAAQFPELDQYtifsYDRFTGEVDTQALERALLQAARDTEA----FRLRLGETD-GTPYQWLDTDAEF 81
Cdd:cd19536    2 YPLSSLQEGMLFHSLLNPGGSVY----LHNYTYTVGRRLNLDLLLEALQVLIDrhdiLRTSFIEDGlGQPVQVVHRQAQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   82 EARHVDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVY--VRTHHIVSDAWGLQLFLSRVRAGYLGE 159
Cdd:cd19536   78 PVTELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLlvISDHHSILDGWSLYLLVKEILAVYNQL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  160 LGEPQAQMPTAS----LLAQLETddysgSEQYRGDRAYFAEALEGLEpalfTRRRPAGLR-RTARHRLTLERTLLDAI-- 232
Cdd:cd19536  158 LEYKPLSLPPAQpyrdFVAHERA-----SIQQAASERYWREYLAGAT----LATLPALSEaVGGGPEQDSELLVSVPLpv 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  233 ------RDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNR--ADRAAKQVVGHFANTLPLRIrTAPEQTVDEFLAQL 304
Cdd:cd19536  229 rsrslaKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRV-TLSEETVEDLLKRA 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  305 REATRTLLRHQKMPLGDLLRGAS--PLFDTTLSYMRWPAAQAIP----NASVETVAQTHAHDPDaLAIWVSEFDGHSDAQ 378
Cdd:cd19536  308 QEQELESLSHEQVPLADIQRCSEgePLFDSIVNFRHFDLDFGLPewgsDEGMRRGLLFSEFKSN-YDVNLSVLPKQDRLE 386

                        410       420       430
                 ....*....|....*....|....*....|.
gi 15598523  379 VDFEYACDVFDADFPMDAAArHIETFLRALV 409
Cdd:cd19536  387 LKLAYNSQVLDEEQAQRLAA-YYKSAIAELA 416
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 471-876 3.75e-21

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: 99.35  E-value: 3.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD 550
Cdd:cd05940    3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 eraatlgeslgetrvlhlerlpqstgdlpaanvapgdLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVL 630
Cdd:cd05940   83 -------------------------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVL 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  631 LQKTPVTFDVSVweLFWWS---FTGARLSLlppgAEK-DPREMLRSIQRDAVTVIHFVPSMLTPfldLLDGDPTARAAAS 706
Cdd:cd05940  126 YTCLPLYHSTAL--IVGWSaclASGATLVI----RKKfSASNFWDDIRKYQATIFQYIGELCRY---LLNQPPKPTERKH 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  707 SLRLVFcsGEALAPLQVARFRRLFGDAvRLVNLYGPTEATvdvsdheCASDNPTRVP--IGR------PIDNLRLYVLD- 777
Cdd:cd05940  197 KVRMIF--GNGLRPDIWEEFKERFGVP-RIAEFYAATEGN-------SGFINFFGKPgaIGRnpsllrKVAPLALVKYDl 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  778 ---RALRPQ-------PLGAVGEL--YIGGVGVARGYLNRPELNaERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRA 845
Cdd:cd05940  267 esgEPIRDAegrcikvPRGEPGLLisRINPLEPFDGYTDPAATE-KKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRL 345

                        410       420       430
                 ....*....|....*....|....*....|.
gi 15598523  846 DDQVKIRGNRVEPDEVRDRLAALPGVRDAAV 876
Cdd:cd05940  346 GDTFRWKGENVSTTEVAAVLGAFPGVEEANV 376
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 1482-1963 4.89e-21

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: 99.96  E-value: 4.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1482 ERQVEALPGSAALAFE------EQRWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVP 1554
Cdd:cd17634   60 DRHLRENGDRTAIIYEgddtsqSRTISYRELhREVCR-FAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1555 LDVSYPAQRLA--------LILETA----QPFRVVAHPEHAHVAAAERVLPVE-----------------------ELVA 1599
Cdd:cd17634  139 IFGGFAPEAVAgriidsssRLLITAdggvRAGRSVPLKKNVDDALNPNVTSVEhvivlkrtgsdidwqegrdlwwrDLIA 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1600 DIEPETFAAP-QLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGV-PGLRTLQFAPLSFDMAFQEIF--STL 1675
Cdd:cd17634  219 KASPEHQPEAmNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYgPGDIYWCTADVGWVTGHSYLLygPLA 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1676 CGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNAL--GVRPGALRVVVSSGEQLRiTEDVRAFCAA 1753
Cdd:cd17634  299 CGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAieGTDRSSLRILGSVGEPIN-PEAYEWYWKK 377

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1754 MPGLL--LENQYGPTETHQVTYHSLSGDPAHYPDLPPigRPLDGVEVQVLDAALRPVPVGVTGELYFGGDC--LARGYHR 1829
Cdd:cd17634  378 IGKEKcpVVDTWWQTETGGFMITPLPGAIELKAGSAT--RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWpgQTRTLFG 455

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1830 APkltaERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARE 1909
Cdd:cd17634  456 DH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLV----AHPKVAEAAVVGIP 527

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523 1910 RQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHM----VPAHFAWVDGFALTPSGK 1963
Cdd:cd17634  528 HAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGK 585
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1067-1382 5.95e-21

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: 98.16  E-value: 5.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1067 PDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDlSGASEPLQLVHtqaRSEPLILdlrgNPEAGTVLDE-- 1144
Cdd:cd20484   19 PEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIE-EEDGVPFQKIE---PSKPLSF----QEEDISSLKEse 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1145 ---HIRQRRFHRYSLQQPGLFLFAAFVR-EDGLDLVFSFHHAILDGWSVANLIVALVAAYR-----GEPLPGPAPAlACH 1215
Cdd:cd20484   91 iiaYLREKAKEPFVLENGPLMRVHLFSRsEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqgKQPTLASSPA-SYY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1216 --VREELAALASP---AAVGYWTGLLEGArMTRLDGFGAHEPQAAQG--PASHREALPDGLLERLKATAAQRGLPLKSLL 1288
Cdd:cd20484  170 dfVAWEQDMLAGAegeEHRAYWKQQLSGT-LPILELPADRPRSSAPSfeGQTYTRRLPSELSNQIKSFARSQSINLSTVF 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1289 LAAHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIAGC-SWIEVADALFRQERDGHAHRRYPLSAI 1367
Cdd:cd20484  249 LGIFKLLLHRYTGQEDIIVGMPTMGRPE-ERFDSLIGYFINMLPIRSRILGEeTFSDFIRKLQLTVLDGLDHAAYPFPAM 327

                        330
                 ....*....|....*
gi 15598523 1368 QQIVGDELSSAFNYV 1382
Cdd:cd20484  328 VRDLNIPRSQANSPV 342
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1499-1906 6.12e-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: 98.69  E-value: 6.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1499 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDvsypaqrlaliletaqPFRVVA 1578
Cdd:cd05910    1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLID----------------PGMGRK 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1579 HpehahvaaaervlpVEELVADIEPETF-AAPQLDELAMLLFTSGSTGRPKGVELSHRMWanytqwqlrvASGVPGLRTL 1657
Cdd:cd05910   65 N--------------LKQCLQEAEPDAFiGIPKADEPAAILFTSGSTGTPKGVVYRHGTF----------AAQIDALRQL 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1658 -QFAPLSFDMAFQEIFSTLcgGGELQLISNRERMDPSA--------LLHVLERRQVQRVLLPFVALQRLAEASNALGVRP 1728
Cdd:cd05910  121 yGIRPGEVDLATFPLFALF--GPALGLTSVIPDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1729 GALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQVTY---HSLSGDPAHYPDLPP---IGRPLDGVEVQVLD 1802
Cdd:cd05910  199 PSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEALPVSSigsRELLATTTAATSGGAgtcVGRPIPGVRVRIIE 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1803 AALRP---------VPVGVTGELYFGGDCLARGYHRAPKLTAerfVEHPWRPGAR-LYRTGDLGRILGNGEIVWLGRADT 1872
Cdd:cd05910  279 IDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATA---LAKIDDNSEGfWHRMGDLGYLDDEGRLWFCGRKAH 355

                        410       420       430
                 ....*....|....*....|....*....|....
gi 15598523 1873 QVKVRGFRIEPAEVElaimRQAERQPGLRGAAVV 1906
Cdd:cd05910  356 RVITTGGTLYTEPVE----RVFNTHPGVRRSALV 385
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 473-941 7.02e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 97.80  E-value: 7.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   473 SYAELDAKVQAVADALR---AAGvrtdERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLV 549
Cdd:PRK08308   10 SKSDFDLRLQRYEEMEQfqeAAG----NRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   550 DEraatlgeslGETRVLHLErlPQSTGdlpaanvaPGDLayVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDV 629
Cdd:PRK08308   86 GE---------SDFTKLEAV--NYLAE--------EPSL--LQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDET 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   630 LLQKTPVTFDvsvwelfwWSFTGARLSLLPPGAE------KDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARA 703
Cdd:PRK08308  145 PIVACPVTHS--------YGLICGVLAALTRGSKpviitnKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGTFQFHA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   704 aasslrlVFCSGealAPLQVARFRRLFGDAVRLVNLYGPTEATvdvsdheCASDNP---TRVPIGRPIDNLRLyvldral 780
Cdd:PRK08308  217 -------VMTSG---TPLPEAWFYKLRERTTYMMQQYGCSEAG-------CVSICPdmkSHLDLGNPLPHVSV------- 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   781 rpqplgavgelyigGVGVARGylnrpelNAERFLVDpfvAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDE 860
Cdd:PRK08308  273 --------------SAGSDEN-------APEEIVVK---MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIE 328

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   861 VRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLP 940
Cdd:PRK08308  329 VEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408


                  .
gi 15598523   941 A 941
Cdd:PRK08308  409 L 409
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 1489-1970 8.46e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 98.54  E-value: 8.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAFEE--QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY-PAQRLA 1565
Cdd:PRK13390   11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLtAPEADY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1566 LILETAQPFRVVAHPEHAHVAAAERVLPVE-------ELVADIEPETFAA-PQLDEL---AMLLFTSGSTGRPKGV--EL 1632
Cdd:PRK13390   91 IVGDSGARVLVASAALDGLAAKVGADLPLRlsfggeiDGFGSFEAALAGAgPRLTEQpcgAVMLYSSGTTGFPKGIqpDL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1633 SHRmwanytqwqlrvASGVPGLRTLQFAPLSFDMAFQEIFST-----------LCG-----GGELQLIsnrERMDPSALL 1696
Cdd:PRK13390  171 PGR------------DVDAPGDPIVAIARAFYDISESDIYYSsapiyhaaplrWCSmvhalGGTVVLA---KRFDAQATL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1697 HVLERRQV---QRVLLPFVALQRL-AEASNALGVrpGALRVVVSSGEQLRIteDVRAFCAAMPGLLLENQYGPTETHQVT 1772
Cdd:PRK13390  236 GHVERYRItvtQMVPTMFVRLLKLdADVRTRYDV--SSLRAVIHAAAPCPV--DVKHAMIDWLGPIVYEYYSSTEAHGMT 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1773 YHSlSGDPAHYPDlpPIGRPLDGvEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAErfVEHPWRPgarLYRT 1852
Cdd:PRK13390  312 FID-SPDWLAHPG--SVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP---FWTT 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1853 -GDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDAFLAAFLL-GEPEAV 1928
Cdd:PRK13390  383 vGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALT----MHPAVHDVAVigVPDPEMGEQVKAVIQLVeGIRGSD 458

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 15598523  1929 DLA-ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:PRK13390  459 ELArELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 6-351 9.56e-21

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: 97.72  E-value: 9.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    6 RLPLSPYQRDIWVaaaqfpeLDQ-------YTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTD 78
Cdd:cd19538    1 EIPLSFAQRRLWF-------LHQlegpsatYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   79 AEfeaRHVDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYL 157
Cdd:cd19538   74 DE---ATPKLEIKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLlHHIAADGWSLAPLTRDLSKAYR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  158 GELgepQAQMPTASLLA---------QLETDDYSGSEQYRGDR--AYFAEALEGLEPAL---FTRRRPAGlRRTARHRLT 223
Cdd:cd19538  151 ARC---KGEAPELAPLPvqyadyalwQQELLGDESDPDSLIARqlAYWKKQLAGLPDEIelpTDYPRPAE-SSYEGGTLT 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  224 LE------RTLLDAIRDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTV 297
Cdd:cd19538  227 FEidselhQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSF 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598523  298 DEFLAQLREATRTLLRHQKMPLGDLL------RGAS--PLFDTTLsymrwpAAQAIPNASVE 351
Cdd:cd19538  307 RELLERVKETNLEAYEHQDIPFERLVealnptRSRSrhPLFQIML------ALQNTPQPSLD 362
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1619-1963 1.07e-20

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: 96.19  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1619 FTSGSTGRPKGVELSHRMWAN---YTQWQLRVASG----VPglrtlqfAPL--SFDMAFQeIFSTLCGGGELQLISnrER 1689
Cdd:cd05917    9 FTSGTTGSPKGATLTHHNIVNngyFIGERLGLTEQdrlcIP-------VPLfhCFGSVLG-VLACLTHGATMVFPS--PS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1690 MDPSALLHVLERRQ---VQRVLLPFVALQRLAEASNalgVRPGALRVVVSSG------------EQLRITEDVRAfcaam 1754
Cdd:cd05917   79 FDPLAVLEAIEKEKctaLHGVPTMFIAELEHPDFDK---FDLSSLRTGIMAGapcppelmkrviEVMNMKDVTIA----- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1755 pglllenqYGPTETHQVTYHSLSGDPAHyPDLPPIGRPLDGVEVQVLDAALRPVP-VGVTGELYFGGDCLARGYHRAPKL 1833
Cdd:cd05917  151 --------YGMTETSPVSTQTRTDDSIE-KRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEK 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1834 TAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVkVRGFR-IEPAEVELAIMrqaeRQPGLRGAAV--VARER 1910
Cdd:cd05917  222 TAEAIDGDGW------LHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLH----THPKVSDVQVvgVPDER 290

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15598523 1911 QGNDafLAAFLLGEPEA-VDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd05917  291 YGEE--VCAWIRLKEGAeLTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGK 342
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 1486-1970 2.36e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 97.16  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1486 EALPGSAALAFEEQRWTYRDLDHVARCVATRLvRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA 1565
Cdd:PRK07638   12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1566 LILETAQPFRVVAHPEHAHVAAAE--RVLPVEELVADIEPETFAAPQLDELAM----LLFTSGSTGRPKGVELSHRMW-- 1637
Cdd:PRK07638   91 ERLAISNADMIVTERYKLNDLPDEegRVIEIDEWKRMIEKYLPTYAPIENVQNapfyMGFTSGSTGKPKAFLRAQQSWlh 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1638 ---ANYTQWQLRVASGV--PGlrTLqfapLSFDMAFQEIfSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFV 1712
Cdd:PRK07638  171 sfdCNVHDFHMKREDSVliAG--TL----VHSLFLYGAI-STLYVGQTVHLM---RKFIPNQVLDKLETENISVMYTVPT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1713 ALQRLAEASnalGVRPGALRVVvSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETHQVTYHSlSGDPAHYPDlpPIGRP 1792
Cdd:PRK07638  241 MLESLYKEN---RVIENKMKII-SSGAKWEA-EAKEKIKNIFPYAKLYEFYGASELSFVTALV-DEESERRPN--SVGRP 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1793 LDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWRPgarlyrTGDLGRILGNGEIVWLGRADT 1872
Cdd:PRK07638  313 FHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADG-WMT------VRDVGYEDEEGFIYIVGREKN 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1873 QVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARErqgnDAFLaafllGE-PEAV-----DLAELKQALRSELPEHMV 1946
Cdd:PRK07638  386 MILFGGINIFPEEIE----SVLHEHPAVDEIVVIGVP----DSYW-----GEkPVAIikgsaTKQQLKSFCLQRLSSFKI 452

                         490       500
                  ....*....|....*....|....
gi 15598523  1947 PAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:PRK07638  453 PKEWHFVDEIPYTNSGKIARMEAK 476
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
587-939 2.76e-20

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 95.11  E-value: 2.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   587 DLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRR-------------YPIGERDVLLQK-----TPVTFDVSvwelfww 648
Cdd:PRK07824   36 DVALVVATSGTTGTPKGAMLTAAALTASADATHDRlggpgqwllalpaHHIAGLQVLVRSviagsEPVELDVS------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   649 sftgarlsllppgAEKDPREMLRSIQRDAV--TVIHFVPSMLTPFLDlldgDPTARAAASSLRLVFCSGEALaPLQVARF 726
Cdd:PRK07824  109 -------------AGFDPTALPRAVAELGGgrRYTSLVPMQLAKALD----DPAATAALAELDAVLVGGGPA-PAPVLDA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   727 RRLFGdaVRLVNLYGPTEATvdvsdHECASDnptrvpiGRPIDNLRLYVLDralrpqplgavGELYIGGVGVARGYLNRP 806
Cdd:PRK07824  171 AAAAG--INVVRTYGMSETS-----GGCVYD-------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   807 ELnaerflvDPFVAGGrLYRTGDLARwLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGT 886
Cdd:PRK07824  226 DP-------DPFAEPG-WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQ 296

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15598523   887 HLVGYYVAAAELDP--GQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK07824  297 RVVAAVVGDGGPAPtlEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 6-390 2.83e-20

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: 96.23  E-value: 2.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    6 RLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAEFEARH 85
Cdd:cd20484    1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   86 VDLRADRdpEAAVRSWLRDAFRHAYPLDGRSLVDLALLH-SDQALYVYVRTHHIVSDAWGLQLFLSRVRAGY--LGELGE 162
Cdd:cd20484   81 EDISSLK--ESEIIAYLREKAKEPFVLENGPLMRVHLFSrSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqaLLQGKQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  163 PQAQMPTASL--LAQLETDDYSGSEqyrGD--RAYFAEALEGLEPAL---FTRRRPAGLRRTAR-HRLTLERTLLDAIR- 233
Cdd:cd20484  159 PTLASSPASYydFVAWEQDMLAGAE---GEehRAYWKQQLSGTLPILelpADRPRSSAPSFEGQtYTRRLPSELSNQIKs 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  234 ----DRGESPFLFLSAAVALyLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATR 309
Cdd:cd20484  236 farsQSINLSTVFLGIFKLL-LHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVL 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  310 TLLRHQKMPLGDLLR--------GASPLFDTTLSY--------MRWPAAQAIPNASVETVAQTHAHDPDALAIWVseFDG 373
Cdd:cd20484  315 DGLDHAAYPFPAMVRdlniprsqANSPVFQVAFFYqnflqstsLQQFLAEYQDVLSIEFVEGIHQEGEYELVLEV--YEQ 392

                        410
                 ....*....|....*..
gi 15598523  374 HSDAQVDFEYACDVFDA 390
Cdd:cd20484  393 EDRFTLNIKYNPDLFDA 409
PRK09192 PRK09192
fatty acyl-AMP ligase;
461-936 3.11e-20

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 97.38  E-value: 3.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   461 RTALLEAdggtLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPL-------E 533
Cdd:PRK09192   43 RGQLEEA----LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFggresyiA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   534 RVRLLLEDCGARVVLV-DERAATLGESLGETRVLH------LERLPQSTGDLPAanVAPGDLAYVIYTSGSTGMPKGVMV 606
Cdd:PRK09192  119 QLRGMLASAQPAAIITpDELLPWVNEATHGNPLLHvlshawFKALPEADVALPR--PTPDDIAYLQYSSGSTRFPRGVII 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   607 EHRSVVNRLN-----------------WMQRRYPIGERDVLLqkTPVTFDVSVwelfwwsftgarlSLLPPGA-EKDPRE 668
Cdd:PRK09192  197 THRALMANLRaishdglkvrpgdrcvsWLPFYHDMGLVGFLL--TPVATQLSV-------------DYLPTRDfARRPLQ 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   669 MLRSIQRDAVTvIHFVPsmltPF-LDL----LDGDPTARAAASSLRLVFCSGEALAP--LQ--VARFRRLFGDAVRLVNL 739
Cdd:PRK09192  262 WLDLISRNRGT-ISYSP----PFgYELcarrVNSKDLAELDLSCWRVAGIGADMIRPdvLHqfAEAFAPAGFDDKAFMPS 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   740 YGPTEATVDVS---------------------DHECASDNPTR-----VPIGRPIDNLRLYVLDRALRPQPLGAVGELYI 793
Cdd:PRK09192  337 YGLAEATLAVSfsplgsgivveevdrdrleyqGKAVAPGAETRrvrtfVNCGKALPGHEIEIRNEAGMPLPERVVGHICV 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   794 GGVGVARGYLNRPElnAERFLvdpfVAGGRLyRTGDLArWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVR- 872
Cdd:PRK09192  417 RGPSLMSGYFRDEE--SQDVL----AADGWL-DTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRs 488

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523   873 -DAAV--VARDSAVRGTHLVGYYVAAAElDPGQLRAGLSATLpdfmLPAFFVRID-------SLPLSANGKLDR 936
Cdd:PRK09192  489 gDAAAfsIAQENGEKIVLLVQCRISDEE-RRGQLIHALAALV----RSEFGVEAAvelvpphSLPRTSSGKLSR 557
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 1616-1965 3.83e-20

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: 94.29  E-value: 3.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1616 MLLFTSGSTGRPKGVELSHR--MWANYTQWQLRVASgvPGLRTLQFAPLsFDMAFQ-EIFSTLCGGGELQLISnreRMDP 1692
Cdd:cd17636    4 LAIYTAAFSGRPNGALLSHQalLAQALVLAVLQAID--EGTVFLNSGPL-FHIGTLmFTLATFHAGGTNVFVR---RVDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1693 SALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGE-QLRITEDVRAFCAAMPGlllenqYGPTE-THQ 1770
Cdd:cd17636   78 EEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwNDMATVDTSPWGRKPGG------YGQTEvMGL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1771 VTYHSLSGdpahyPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVehpwrpgARLY 1850
Cdd:cd17636  152 ATFAALGG-----GAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GGWH 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1851 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAV--VARERQGNDAfLAAFLLGEPEAV 1928
Cdd:cd17636  220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCL----RQHPAVADAAVigVPDPRWAQSV-KAIVVLKPGASV 294

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 15598523 1929 DLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 1965
Cdd:cd17636  295 TEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 446-882 4.04e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 97.42  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   446 TLPTLFAEQVARTPQRTALLEADGGT-----LSYAELDAKVQAVADALRAAGVRTDERVALLVARG-PHLLPAiLGVQRA 519
Cdd:PRK12582   50 SIPHLLAKWAAEAPDRPWLAQREPGHgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSiEHALMT-LAAMQA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   520 GGAYVPINP-----DHPLERVRLLLEDCGARVVLVDERA------ATLGesLGETRVLHLERLPQSTGDLPAANVA---- 584
Cdd:PRK12582  129 GVPAAPVSPayslmSHDHAKLKHLFDLVKPRVVFAQSGApfaralAALD--LLDVTVVHVTGPGEGIASIAFADLAatpp 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   585 ------------PGDLAYVIYTSGSTGMPKGVMVEHRSV-VNRLNWMQ--RRYPIGERDVLLQKTP--------VTFDVS 641
Cdd:PRK12582  207 taavaaaiaaitPDTVAKYLFTSGSTGMPKAVINTQRMMcANIAMQEQlrPREPDPPPPVSLDWMPwnhtmggnANFNGL 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   642 VWElfwwsftGARLSL-----LPPGAEkdprEMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARAAA-SSLRLVFCSG 715
Cdd:PRK12582  287 LWG-------GGTLYIddgkpLPGMFE----ETIRNLREISPTVYGNVPAGYAMLAEAMEKDDALRRSFfKNLRLMAYGG 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   716 EALAPLQVARFRRL----FGDAVRLVNLYGPTE-ATVDVSDHEcasdNPTRVP-IGRPIDNLRLYVLdralrpqPLGAVG 789
Cdd:PRK12582  356 ATLSDDLYERMQALavrtTGHRIPFYTGYGATEtAPTTTGTHW----DTERVGlIGLPLPGVELKLA-------PVGDKY 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   790 ELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLADGNLE----YLGRADDQVKI-RGNRVEPDEVR-D 863
Cdd:PRK12582  425 EVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVDPDDPEkgliFDGRVAEDFKLsTGTWVSVGTLRpD 498

                         490       500
                  ....*....|....*....|
gi 15598523   864 RLAAL-PGVRDAAVVARDSA 882
Cdd:PRK12582  499 AVAACsPVIHDAVVAGQDRA 518
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 1507-1949 1.58e-19

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 94.77  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1507 DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAH------- 1579
Cdd:PRK12406   19 QRAAR-AAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHadllhgl 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1580 -------------PEHAHVAAAERVLPV-----------EELVADIEPetFAAPQLDELAMLLFTSGSTGRPKGV----- 1630
Cdd:PRK12406   98 asalpagvtvlsvPTPPEIAAAYRISPAlltppagaidwEGWLAQQEP--YDGPPVPQPQSMIYTSGTTGHPKGVrraap 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1631 --ELShrmwANYTQWQLRVASGVPGLRTLQFAPL--SFDMAFQEIFSTLcgGGELQLISnreRMDPSALLHVLERRQVQR 1706
Cdd:PRK12406  176 tpEQA----AAAEQMRALIYGLKPGIRALLTGPLyhSAPNAYGLRAGRL--GGVLVLQP---RFDPEELLQLIERHRITH 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1707 V-LLP--FVALQRLAEASNAlgvrpgalRVVVSSgeqLRITEDVRAFCA-----AMP---GLLLENQYGPTETHQVTYHS 1775
Cdd:PRK12406  247 MhMVPtmFIRLLKLPEEVRA--------KYDVSS---LRHVIHAAAPCPadvkrAMIewwGPVIYEYYGSTESGAVTFAT 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1776 lSGDPAHYPDlpPIGRPLDGVEVQVLDAALRPVPVGVTGELYfggdCLARG-----YHRAPKLTAErfVEhpwRPGarLY 1850
Cdd:PRK12406  316 -SEDALSHPG--TVGKAAPGAELRFVDEDGRPLPQGEIGEIY----SRIAGnpdftYHNKPEKRAE--ID---RGG--FI 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1851 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDafLAAFLLGEPEA- 1927
Cdd:PRK12406  382 TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLH----AVPGVHDCAVfgIPDAEFGEA--LMAVVEPQPGAt 455

                         490       500
                  ....*....|....*....|..
gi 15598523  1928 VDLAELKQALRSELPEHMVPAH 1949
Cdd:PRK12406  456 LDEADIRAQLKARLAGYKVPKH 477
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1058-1349 3.82e-19

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: 92.50  E-value: 3.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1058 GLLFHSRQRPDSSVYHDVFHYRFDlawDEA---AFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARSEPLILDLRG 1134
Cdd:cd19544   10 GILFHHLLAEEGDPYLLRSLLAFD---SRArldAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVEELTLDP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1135 NPEAGTVLDEHIRQRRfHRYSLQQPGLF-LFAAFVREDG-LDLVFSFHHAILDGWSVANLI--VALVAAYRGEPLPGPAP 1210
Cdd:cd19544   87 GDDALAQLRARFDPRR-YRLDLRQAPLLrAHVAEDPANGrWLLLLLFHHLISDHTSLELLLeeIQAILAGRAAALPPPVP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1211 -----ALACHVREELAALAspaavgYWTGLLE---------GARMTRLDGFGAHEpqaaqgpasHREALPDGLLERLKAT 1276
Cdd:cd19544  166 yrnfvAQARLGASQAEHEA------FFREMLGdvdeptapfGLLDVQGDGSDITE---------ARLALDAELAQRLRAQ 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523 1277 AAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGR-PELPDADRMVGLFLNTVPVRSEIAGCSwieVADAL 1349
Cdd:cd19544  231 ARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRmQGGAGADRALGMFINTLPLRVRLGGRS---VREAV 301
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 471-850 5.98e-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: 93.05  E-value: 5.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGgayVPInpdhplervrllledcgarvvlvd 550
Cdd:cd17639    5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPI------------------------ 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 eraATLGESLGETRVLHLERLPQSTGDLpaANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYP--IGERD 628
Cdd:cd17639   58 ---VTVYATLGEDALIHSLNETECSAIF--TDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDD 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  629 VLLQKTPVT----FDVSVWELFWwsftGARLsllppgAEKDPREMLRSIQR----DAV----TVIHFVP----------- 685
Cdd:cd17639  133 RYLAYLPLAhifeLAAENVCLYR----GGTI------GYGSPRTLTDKSKRgckgDLTefkpTLMVGVPaiwdtirkgvl 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  686 ---------------------------SMLTPFLDLLDGDPTARAAASSLRLVFCSGEALAPlQVARFRRLFGdaVRLVN 738
Cdd:cd17639  203 aklnpmgglkrtlfwtayqsklkalkeGPGTPLLDELVFKKVRAALGGRLRYMLSGGAPLSA-DTQEFLNIVL--CPVIQ 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  739 LYGPTE----ATV-DVSDHECASdnptrvpIGRPIDNLRLYVLD------RALRPQPLgavGELYIGGVGVARGYLNRPE 807
Cdd:cd17639  280 GYGLTEtcagGTVqDPGDLETGR-------VGPPLPCCEIKLVDweeggySTDKPPPR---GEILIRGPNVFKGYYKNPE 349

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 15598523  808 LNAERFlvdpfvAGGRLYRTGDLARWLADGNLEYLGRADDQVK 850
Cdd:cd17639  350 KTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVK 386
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1051-1452 6.09e-19

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: 92.05  E-value: 6.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1051 PTSRLSLGLLFHSRQRPDSSVYhDVFHY-RFDLAWDEAAFRHALDRVVAAYPALRSSFDLSgASEPLQLVHTQARSEPLI 1129
Cdd:cd19533    3 PLTSAQRGVWFAEQLDPEGSIY-NLAEYlEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTPVPIRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1130 LDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAFVREDGLDLVF-SFHHAILDGWSvANLIVALVAA-YRG----- 1202
Cdd:cd19533   81 IDLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYqRVHHIVMDGFS-FALFGQRVAEiYTAllkgr 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1203 EPLPGPAPALACHVREELAALASPAAVG---YWTGLLEGArmTRLDGFGAHEPQAAQGPASHREALPDGLLERLKATAAQ 1279
Cdd:cd19533  160 PAPPAPFGSFLDLVEEEQAYRQSERFERdraFWTEQFEDL--PEPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAAEA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1280 RGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRpeLPDADR-MVGLFLNTVPVRSEIA-GCSWIEVADALFRQERDGH 1357
Cdd:cd19533  238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR--LGAAARqTPGMVANTLPLRLTVDpQQTFAELVAQVSRELRSLL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1358 AHRRYPLSAIQQIVGDELSSA-FNYVNLHVLEPLWQLR-DFRVWEETNFA------LLVNVIATpSDGMYLRIDSDGRG- 1428
Cdd:cd19533  316 RHQRYRYEDLRRDLGLTGELHpLFGPTVNYMPFDYGLDfGGVVGLTHNLSsgptndLSIFVYDR-DDESGLRIDFDANPa 394

                        410       420
                 ....*....|....*....|....*
gi 15598523 1429 -ISRSQAALIGATFVELLWRLADHP 1452
Cdd:cd19533  395 lYSGEDLARHQERLLRLLEEAAADP 419
PRK09274 PRK09274
peptide synthase; Provisional
 1499-1869 8.87e-19

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 92.65  E-value: 8.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1499 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVA 1578
Cdd:PRK09274   40 DELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1579 HPEhAHVA---------AAERVLPV-----------EELVADIEPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHRM 1636
Cdd:PRK09274  120 IPK-AHLArrlfgwgkpSVRRLVTVggrllwggttlATLLRDGAAAPFPMADLapDDMAAILFTSGSTGTPKGVVYTHGM 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1637 WANYTQwQLRVASG-VPGLRTLQFAPLsfdMAFqeiFSTLCGGGelqliSNRERMDPS--------ALLHVLERRQVQRV 1707
Cdd:PRK09274  199 FEAQIE-ALREDYGiEPGEIDLPTFPL---FAL---FGPALGMT-----SVIPDMDPTrpatvdpaKLFAAIERYGVTNL 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1708 llpFVA---LQRLAEASNALGVRPGALRVVVSSGEQLriTEDVRAFCAAM--PGLLLENQYGPTET---HQVTYHSLSGD 1779
Cdd:PRK09274  267 ---FGSpalLERLGRYGEANGIKLPSLRRVISAGAPV--PIAVIERFRAMlpPDAEILTPYGATEAlpiSSIESREILFA 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1780 PAHYPDLPP---IGRPLDGVEVQVL---DAAL------RPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVehpWRPGA 1847
Cdd:PRK09274  342 TRAATDNGAgicVGRPVDGVEVRIIaisDAPIpewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKI---PDGQG 418

                         410       420
                  ....*....|....*....|...
gi 15598523  1848 RLY-RTGDLGRILGNGEIVWLGR 1869
Cdd:PRK09274  419 DVWhRMGDLGYLDAQGRLWFCGR 441
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1502-1906 8.94e-19

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: 91.48  E-value: 8.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1502 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPldvsypaqrlALILETAQPFRvvahpe 1581
Cdd:cd05974    2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP----------ATTLLTPDDLR------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1582 hahvaaaERVLPVEELVADIEPETFAapqlDELAMLLFTSGSTGRPKGVELSHRmwaNYTQWQLRVASGV---PGLRTLQ 1658
Cdd:cd05974   66 -------DRVDRGGAVYAAVDENTHA----DDPMLLYFTSGTTSKPKLVEHTHR---SYPVGHLSTMYWIglkPGDVHWN 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1659 FA-PLSFDMAFQEIFSTLCGGGELQLIsNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASnaLGVRPGALRVVVSS 1737
Cdd:cd05974  132 ISsPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD--LASFDVKLREVVGA 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1738 GEQL--RITEDVRAfcaaMPGLLLENQYGPTETHQVTYHSlsgdPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVG---- 1811
Cdd:cd05974  209 GEPLnpEVIEQVRR----AWGLTIRDGYGQTETTALVGNS----PGQPVKAGSMGRPLPGYRVALLDPDGAPATEGeval 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1812 VTGELYFGGdcLARGYHRAPKLTAERFvehpwrpGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIM 1891
Cdd:cd05974  281 DLGDTRPVG--LMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLI 351

                        410
                 ....*....|....*
gi 15598523 1892 rqaeRQPGLRGAAVV 1906
Cdd:cd05974  352 ----EHPAVAEAAVV 362
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 456-878 9.15e-19

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 92.75  E-value: 9.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   456 ARTPQRTAL-LEADGGT-LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLE 533
Cdd:PRK07768   12 ARTSPRGMVtGEPDAPVrHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   534 RVRLLLEDCGARVVLVDERAATLGE---SLGET------RVLHLERLpQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGV 604
Cdd:PRK07768   92 DLAVWAEDTLRVIGMIGAKAVVVGEpflAAAPVleekgiRVLTVADL-LAADPIDPVETGEDDLALMQLTSGSTGSPKAV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   605 MVEHRSVVNRLNWMQRRYPIG-ERDVLLQKTPVTFDVS-VWELFWWSFTGARLSLLPPgAE--KDPREMLRSIQRDAVTV 680
Cdd:PRK07768  171 QITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGmVGFLTVPMYFGAELVKVTP-MDflRDPLLWAELISKYRGTM 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   681 I---HFVPSMLTPFLDllDGDPTARAAASSLRLVFCSGEALAPLQVARFRRL---FG-DAVRLVNLYGPTEATVDVSDHE 753
Cdd:PRK07768  250 TaapNFAYALLARRLR--RQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAgarFGlRPEAILPAYGMAEATLAVSFSP 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   754 C----------------------ASDNPTR--VPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNrpeln 809
Cdd:PRK07768  328 CgaglvvdevdadllaalrravpATKGNTRrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLT----- 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523   810 aerflVDPFVAggrlyrTGDLARWLADGNLEYL---------GRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVA 878
Cdd:PRK07768  403 -----MDGFIP------AQDADGWLDTGDLGYLteegevvvcGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVA 469
PRK13382 PRK13382
bile acid CoA ligase;
1477-1963 1.08e-18

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 92.51  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1477 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 1556
Cdd:PRK13382   45 PTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLN 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1557 VSYPAQRLALILE-----------------------TAQPFRVVAHPEHAHVAAAErVLPVEELVADIEPetfaAPQLDE 1613
Cdd:PRK13382  125 TSFAGPALAEVVTregvdtviydeefsatvdraladCPQATRIVAWTDEDHDLTVE-VLIAAHAGQRPEP----TGRKGR 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1614 laMLLFTSGSTGRPKGVELSHRMWA-------NYTQWQLR--VASGVPGLRTLQFAPLSFDMAFQeifSTlcgggelqlI 1684
Cdd:PRK13382  200 --VILLTSGTTGTPKGARRSGPGGIgtlkailDRTPWRAEepTVIVAPMFHAWGFSQLVLAASLA---CT---------I 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1685 SNRERMDPSALLHVLERRQVQRVLLPFVALQRL----AEASNALGVRpgALRVVVSSGEQLRiTEDVRAFCAAMpGLLLE 1760
Cdd:PRK13382  266 VTRRRFDPEATLDLIDRHRATGLAVVPVMFDRImdlpAEVRNRYSGR--SLRFAAASGSRMR-PDVVIAFMDQF-GDVIY 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1761 NQYGPTETHQVTYHSLSGDPAHyPDLPpiGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHR-APKLTAERFV 1839
Cdd:PRK13382  342 NNYNATEAGMIATATPADLRAA-PDTA--GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSgSTKDFHDGFM 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1840 EhpwrpgarlyrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAA 1919
Cdd:PRK13382  419 A-----------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLA----THPDVAEAAVIGVDDEQYGQRLAA 483

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 15598523  1920 FLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK13382  484 FVVLKPGASATPEtLKQHVRDNLANYKVPRDIVVLDELPRGATGK 528
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 591-877 1.87e-18

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: 88.90  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  591 VIYTSGSTGMPKGVMVEHRSVVNR---LNWMQRrypIGERDVLLQKTPVtFDVSVweLFWWSFT---GARLSLLPpgaEK 664
Cdd:cd17636    5 AIYTAAFSGRPNGALLSHQALLAQalvLAVLQA---IDEGTVFLNSGPL-FHIGT--LMFTLATfhaGGTNVFVR---RV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  665 DPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDptaRAAASSLRLVFCSGE--ALAPLQVARFRRLFGdavrlvnLYGP 742
Cdd:cd17636   76 DAEEVLELIEAERCTHAFLLPPTIDQIVELNADG---LYDLSSLRSSPAAPEwnDMATVDTSPWGRKPG-------GYGQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  743 TE----ATVDVSDHECASDNptrvpiGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFlvdpf 818
Cdd:cd17636  146 TEvmglATFAALGGGAIGGA------GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT----- 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523  819 vAGGrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVV 877
Cdd:cd17636  215 -RGG-WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 421-939 2.02e-18

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 91.58  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   421 PLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVARTPQRTALLEA-DGGTLSYAELDAKVQAVADALRAAGVRTDERV 499
Cdd:PLN02330    4 EIQKQEDNEHIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAvTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   500 ALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD----ERAATLGES---LGETRVLH----- 567
Cdd:PLN02330   84 VVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNdtnyGKVKGLGLPvivLGEEKIEGavnwk 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   568 --LERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVnrLNWMQRRYPIGErDVLLQKTPVTFdVSVWEL 645
Cdd:PLN02330  164 elLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLV--ANLCSSLFSVGP-EMIGQVVTLGL-IPFFHI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   646 FwwSFTGARLSLLPPGAEK------DPREMLRSIQRDAVTVIHFVPSML-----TPFLDLLDgdptarAAASSLRLVFCS 714
Cdd:PLN02330  240 Y--GITGICCATLRNKGKVvvmsrfELRTFLNALITQEVSFAPIVPPIIlnlvkNPIVEEFD------LSKLKLQAIMTA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   715 GEALAPLQVARFRRLFgDAVRLVNLYGPTE---ATVDVSDHECASDNPTRVPIGRPIDNLRLYVLD-RALRPQPLGAVGE 790
Cdd:PLN02330  312 AAPLAPELLTAFEAKF-PGVQVQEAYGLTEhscITLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGE 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   791 LYIGGVGVARGYLNRPELNAERFLVDpfvagGRLYrTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPG 870
Cdd:PLN02330  391 LCVRSQCVMQGYYNNKEETDRTIDED-----GWLH-TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPS 464

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523   871 VRDAAVVARDSAVRG-----THLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFfvrIDSLPLSANGKLDRRQL 939
Cdd:PLN02330  465 VEDAAVVPLPDEEAGeipaaCVVINPKAKESEEDILNFVAANVAHYKKVRVVQF---VDSIPKSLSGKIMRRLL 535
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 487-953 2.78e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 91.24  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   487 ALRAAGVRTDER------VALLVARGPHLLPAILGVQRAGGAYVPINPDH---PLER-VRLLleDCgaRVVLVD-ERAAT 555
Cdd:PRK13388   37 AARAAALIALADpdrplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRrgaALAAdIRRA--DC--QLLVTDaEHRPL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   556 L-GESLGETRVL------HLERLPQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERD 628
Cdd:PRK13388  113 LdGLDLPGVRVLdvdtpaYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   629 VLLQKTPVTFDVSVWELfwWS---FTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFVPSmltPFLDLLDGDPTARAAA 705
Cdd:PRK13388  193 VCYVSMPLFHSNAVMAG--WApavASGAAVALPA---KFSASGFLDDVRRYGATYFNYVGK---PLAYILATPERPDDAD 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   706 SSLRLVFcsGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVsdhecasdnpTRVP------IGRPIDNLRLYVLDrA 779
Cdd:PRK13388  265 NPLRVAF--GNEASPRDIAEFSRRFG--CQVEDGYGSSEGAVIV----------VREPgtppgsIGRGAPGVAIYNPE-T 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   780 LRPQPLG-------------AVGELY-IGGVGVARGYLNRPELNAERflvdpfVAGGRlYRTGDLARWLADGNLEYLGRA 845
Cdd:PRK13388  330 LTECAVArfdahgallnadeAIGELVnTAGAGFFEGYYNNPEATAER------MRHGM-YWSGDLAYRDADGWIYFAGRT 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   846 DDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVardsAVRGTHlVGYYVAAA-------ELDPGQLRAGLSATlPDFMLPA 918
Cdd:PRK13388  403 ADWMRVDGENLSAAPIERILLRHPAINRVAVY----AVPDER-VGDQVMAAlvlrdgaTFDPDAFAAFLAAQ-PDLGTKA 476

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 15598523   919 F--FVRI-DSLPLSANGKLDRRQLPAppEQVAAVAPRT 953
Cdd:PRK13388  477 WprYVRIaADLPSTATNKVLKRELIA--QGWATGDPVT 512
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
451-939 2.90e-18

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 91.38  E-value: 2.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   451 FAEQVARTPQRTALLEADGGTLSYAELDAKVQAVADALRAA-GVRTDERVA-LLVARGPHLlPAILGVQRAGGAYVPINP 528
Cdd:PRK05620   18 YGSTVHGDTTVTTWGGAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGsMMYNCAEHL-EVLFAVACMGAVFNPLNK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   529 DHPLERVRLLLEDCGARVVLVDER-AATLGESLGET-RVLHLERLPQSTGDLPAANVAPG-------------------- 586
Cdd:PRK05620   97 QLMNDQIVHIINHAEDEVIVADPRlAEQLGEILKECpCVRAVVFIGPSDADSAAAHMPEGikvysyealldgrstvydwp 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   587 -----DLAYVIYTSGSTGMPKGVMVEHRSVVnrLNWMQRRypigERDVLLQKTPVTF--DVSVWELFWWS------FTGA 653
Cdd:PRK05620  177 eldetTAAAICYSTGTTGAPKGVVYSHRSLY--LQSLSLR----TTDSLAVTHGESFlcCVPIYHVLSWGvplaafMSGT 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   654 RLSLlpPGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARAaasSLRLVFCSGEALAPLQVARFRRLFGda 733
Cdd:PRK05620  251 PLVF--PGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERM---SLQEIYVGGSAVPPILIKAWEERYG-- 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   734 VRLVNLYGPTE-ATVDVSDHECA-----SDNPTRVPIGRPIDNLRLYVLD--RALRPQPLGAvGELYIGGVGVARGYLNR 805
Cdd:PRK05620  324 VDVVHVWGMTEtSPVGTVARPPSgvsgeARWAYRVSQGRFPASLEYRIVNdgQVMESTDRNE-GEIQVRGNWVTASYYHS 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   806 P----------------ELNAERFLVDPFVaggrlyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALP 869
Cdd:PRK05620  403 PteegggaastfrgedvEDANDRFTADGWL------RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAP 476

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598523   870 GVRDAAVVARDSAVRGTHLVGYYVAAAELDPG-----QLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK05620  477 EVVECAVIGYPDDKWGERPLAVTVLAPGIEPTretaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 1619-1963 3.12e-18

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: 88.23  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1619 FTSGSTGRPKGVELSHRMWA-----NYTQWQLRVASG--VPGlrtlqfaPLSFDMAFQEIFSTLCGGGELQLISNrerMD 1691
Cdd:cd17633    7 FTSGTTGLPKAYYRSERSWIesfvcNEDLFNISGEDAilAPG-------PLSHSLFLYGAISALYLGGTFIGQRK---FN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1692 PSALLHVLERRQVQRVLLPFVALQRLAEASNalgvrPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQV 1771
Cdd:cd17633   77 PKSWIRKINQYNATVIYLVPTMLQALARTLE-----PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1772 TYHSL-SGDPAHypdlpPIGRPLDGVEVQVLDAAlrpvpVGVTGELYFGGDCLARGYHRAPKLTaerfvEHPWrpgarlY 1850
Cdd:cd17633  152 TYNFNqESRPPN-----SVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSN-----PDGW------M 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1851 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGepEAVDL 1930
Cdd:cd17633  211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLK----AIPGIEEAIVVGIPDARFGEIAVALYSG--DKLTY 284

                        330       340       350
                 ....*....|....*....|....*....|...
gi 15598523 1931 AELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd17633  285 KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGK 317
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 453-939 6.13e-18

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: 89.89  E-value: 6.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  453 EQVARTPQRTALLEADGGT-LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHP 531
Cdd:cd17642   25 KRYASVPGTIAFTDAHTGVnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  532 LERVRLLLEDCGARVVLVDER-------------------AATLGESLGETRVL------HLERLPQSTGDLPAANVAPG 586
Cdd:cd17642  105 ERELDHSLNISKPTIVFCSKKglqkvlnvqkklkiiktiiILDSKEDYKGYQCLytfitqNLPPGFNEYDFKPPSFDRDE 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  587 DLAYVIYTSGSTGMPKGVMVEHRSVVNRLNwmQRRYP-----IGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPG 661
Cdd:cd17642  185 QVALIMNSSGSTGLPKGVQLTHKNIVARFS--HARDPifgnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKF 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  662 AEKdprEMLRSIQRDAVTVIHFVPSML-----TPFLDLLDgdptaraaASSLRLVFCSGealAPLQvarfrRLFGDAV-R 735
Cdd:cd17642  263 EEE---LFLRSLQDYKVQSALLVPTLFaffakSTLVDKYD--------LSNLHEIASGG---APLS-----KEVGEAVaK 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  736 LVNL------YGPTEATVDVSDHECASDNPTRVPIGRPIDNLRLYVLDRAlrpQPLGA--VGELYIGGVGVARGYLNRPE 807
Cdd:cd17642  324 RFKLpgirqgYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTG---KTLGPneRGELCVKGPMIMKGYVNNPE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  808 lnAERFLVDpfvAGGRLyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRL--------AALPGVRD------ 873
Cdd:cd17642  401 --ATKALID---KDGWL-HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILlqhpkifdAGVAGIPDedagel 474

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523  874 -AAVVARDSAVRGT-HLVGYYVAAAELDPGQLRAGLsatlpdfmlpaffVRIDSLPLSANGKLDRRQL 939
Cdd:cd17642  475 pAAVVVLEAGKTMTeKEVMDYVASQVSTAKRLRGGV-------------KFVDEVPKGLTGKIDRRKI 529
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 466-939 6.39e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 89.77  E-value: 6.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   466 EADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD-HPlERVRLLLEDCGA 544
Cdd:PRK07008   34 EGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlFP-EQIAYIVNHAED 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   545 RVVLVDERAATLGESLGE--TRVLHL------ERLPQSTGDLPA----ANVAPGDLAY----------VIYTSGSTGMPK 602
Cdd:PRK07008  113 RYVLFDLTFLPLVDALAPqcPNVKGWvamtdaAHLPAGSTPLLCyetlVGAQDGDYDWprfdenqassLCYTSGTTGNPK 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   603 GVMVEHRSVVnrLNWMQRRYP----IGERDVLLQKTPVtFDVSVWEL-FWWSFTGARLSLlpPGAEKDPREMLRSIQRDA 677
Cdd:PRK07008  193 GALYSHRSTV--LHAYGAALPdamgLSARDAVLPVVPM-FHVNAWGLpYSAPLTGAKLVL--PGPDLDGKSLYELIEAER 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   678 VTVIHFVPsmlTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTE-------ATVDVS 750
Cdd:PRK07008  268 VTFSAGVP---TVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYG--VEVIHAWGMTEmsplgtlCKLKWK 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   751 DHECASDNPTRVPI--GRPIDNLRLYVLDRALRPQPLGAV--GELYIGGVGVARGYLNRPElnaerflvDPFVAGgrLYR 826
Cdd:PRK07008  343 HSQLPLDEQRKLLEkqGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYFRGDA--------SPLVDG--WFP 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   827 TGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVArdsavrGTH--------LVGYYVAAAEL 898
Cdd:PRK07008  413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA------CAHpkwderplLVVVKRPGAEV 486

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 15598523   899 DPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK07008  487 TREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 8-334 1.15e-17

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: 87.74  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    8 PLSPYQRDIWVAAAQFPE--LDQYTIfsydRFTGEVDTQALERALLQAARDTEAFRLRLGETD-GTPYQWLDTDAEFEAR 84
Cdd:cd19545    3 PCTPLQEGLMALTARQPGayVGQRVF----ELPPDIDLARLQAAWEQVVQANPILRTRIVQSDsGGLLQVVVKESPISWT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   85 HVDlradrDPEAAVRSWLRDAFRHaypldGRSLVDLALLHSDQALYVYVRT-HHIVSDAWGLQLFLSRVRAGYLGELGEP 163
Cdd:cd19545   79 EST-----SLDEYLEEDRAAPMGL-----GGPLVRLALVEDPDTERYFVWTiHHALYDGWSLPLILRQVLAAYQGEPVPQ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  164 QAQMPTA-SLLAQLETDdysGSEQYrgdrayFAEALEGLEPALFTRRrPAGlRRTARHRLTLERTL-LDAIRDRGESPFL 241
Cdd:cd19545  149 PPPFSRFvKYLRQLDDE---AAAEF------WRSYLAGLDPAVFPPL-PSS-RYQPRPDATLEHSIsLPSSASSGVTLAT 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  242 FLSAAVALYLARIHQNDDVVLGVPVLNR-ADRAA-KQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTLLRHQKMPL 319
Cdd:cd19545  218 VLRAAWALVLSRYTGSDDVVFGVTLSGRnAPVPGiEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGL 297

                        330       340
                 ....*....|....*....|.
gi 15598523  320 ------GDLLRGAsPLFDTTL 334
Cdd:cd19545  298 qnirrlGPDARAA-CNFQTLL 317
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 1486-1971 2.35e-17

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: 87.82  E-value: 2.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1486 EALPGSAALAFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRL 1564
Cdd:cd05929    2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAeGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1565 ALILETAQPFRVVAHPEhahVAAAERVLPVEELVADIEPETFAAPQLDELAMLLfTSGSTGRPKGVE--LSHRMWANYTQ 1642
Cdd:cd05929   82 CAIIEIKAAALVCGLFT---GGGALDGLEDYEAAEGGSPETPIEDEAAGWKMLY-SGGTTGRPKGIKrgLPGGPPDNDTL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1643 --WQLRVASGvPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRV-LLP--FVALQRL 1717
Cdd:cd05929  158 maAALGFGPG-ADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDPEEFLRLIERYRVTFAqFVPtmFVRLLKL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1718 AEA-SNALGVrpGALRVVVSSGEQLRIteDVRAFCAAMPGLLLENQYGPTETHQVTYHSlSGDPAHYPDlpPIGRPLDGv 1796
Cdd:cd05929  234 PEAvRNAYDL--SSLKRVIHAAAPCPP--WVKEQWIDWGGPIIWEYYGGTEGQGLTIIN-GEEWLTHPG--SVGRAVLG- 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1797 EVQVLDAALRPVPVGVTGELYF-GGDclARGYHRAPKLTAERFVEHPWRpgarlyRTGDLGRILGNGEIVWLGRADTQVK 1875
Cdd:cd05929  306 KVHILDEDGNEVPPGEIGEVYFaNGP--GFEYTNDPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRRSDMII 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1876 VRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA--RERQGND--AFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFA 1951
Cdd:cd05929  378 SGGVNIYPQEIENALI----AHPKVLDAAVVGvpDEELGQRvhAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIE 453

                        490       500
                 ....*....|....*....|
gi 15598523 1952 WVDGFALTPSGKRDDAALRA 1971
Cdd:cd05929  454 FVAELPRDDTGKLYRRLLRD 473
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 471-880 2.66e-17

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: 88.25  E-value: 2.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLV- 549
Cdd:cd17641   11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAe 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  550 ---------------------------------DERAATLGESLGETRVLHlERLPQsTGDLPAANVAPGDLAYVIYTSG 596
Cdd:cd17641   91 deeqvdklleiadripsvryviycdprgmrkydDPRLISFEDVVALGRALD-RRDPG-LYEREVAAGKGEDVAVLCTTSG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  597 STGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVT----FDVSVWELFWWSFT-----------------GARL 655
Cdd:cd17641  169 TTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPwigeQMYSVGQALVCGFIvnfpeepetmmedlreiGPTF 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  656 SLLPPG-------------AEKDP------REMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPT------ARAAASSLRL 710
Cdd:cd17641  249 VLLPPRvwegiaadvrarmMDATPfkrfmfELGMKLGLRALDRGKRGRPVSLWLRLASWLADALlfrplrDRLGFSRLRS 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  711 VFCSGEALAPlQVARFRRLFGdaVRLVNLYGPTEATVDVSDHECASDNPTRVpiGRPIDNLRLYVLDralrpqplgaVGE 790
Cdd:cd17641  329 AATGGAALGP-DTFRFFHAIG--VPLKQLYGQTELAGAYTVHRDGDVDPDTV--GVPFPGTEVRIDE----------VGE 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  791 LYIGGVGVARGYLNRPELNAERFLVDPFVaggrlyRTGDLARWLADGNLEYLGRADDQVKI-RGNRVEPDEVRDRLAALP 869
Cdd:cd17641  394 ILVRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSP 467

                        490
                 ....*....|.
gi 15598523  870 GVRDAAVVARD 880
Cdd:cd17641  468 YIAEAVVLGAG 478
PRK09192 PRK09192
fatty acyl-AMP ligase;
1459-1974 3.45e-17

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 87.75  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1459 AFLAPRRDAASQPEPLVDvvslFERQVEALP----GSAALAFEEQR------WTYRDLDHVARCVATRLVRAGARRGDAI 1528
Cdd:PRK09192    2 VTMSPTPTTSSLPRRYAD----FPTLVEALDyaalGEAGMNFYDRRgqleeaLPYQTLRARAEAGARRLLALGLKPGDRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1529 GVALNRSPEMIATIWGILRAGLVCVPLDV--------SYPAQrLALILETAQPFRVVAHPEHAHVAAAerVLPVEELVAD 1600
Cdd:PRK09192   78 ALIAETDGDFVEAFFACQYAGLVPVPLPLpmgfggreSYIAQ-LRGMLASAQPAAIITPDELLPWVNE--ATHGNPLLHV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1601 IEPETFAA----------PQLDELAMLLFTSGSTGRPKGVELSHR-MWAN---YTQWQLRVasgVPGLRTLQFAPLSFDM 1666
Cdd:PRK09192  155 LSHAWFKAlpeadvalprPTPDDIAYLQYSSGSTRFPRGVIITHRaLMANlraISHDGLKV---RPGDRCVSWLPFYHDM 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1667 AFQEIFST---------LCGGGE--------LQLIS-NRERM--DPSALLHVLERRQVQRVLLPF------VA------- 1713
Cdd:PRK09192  232 GLVGFLLTpvatqlsvdYLPTRDfarrplqwLDLISrNRGTIsySPPFGYELCARRVNSKDLAELdlscwrVAgigadmi 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1714 ----LQRLAEASNALGVRPGALrvVVSSGeqlrITEDVRAFCAAMPGlllenqyGPTETHQVTYHSLSGD---------P 1780
Cdd:PRK09192  312 rpdvLHQFAEAFAPAGFDDKAF--MPSYG----LAEATLAVSFSPLG-------SGIVVEEVDRDRLEYQgkavapgaeT 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1781 AHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILg 1860
Cdd:PRK09192  379 RRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADG-W------LDTGDLGYLL- 450

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1861 NGEIVWLGRADTQVKVRGFRIEPAEVELAimrqAERQPGLRG----AAVVARERQGNDAFLAAFLLGEPEAvdlaelKQA 1936
Cdd:PRK09192  451 DGYLYITGRAKDLIIINGRNIWPQDIEWI----AEQEPELRSgdaaAFSIAQENGEKIVLLVQCRISDEER------RGQ 520

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 15598523  1937 LRSELPE-----HMVPAHFAWVDGFAL--TPSGKRDDAALRALPL 1974
Cdd:PRK09192  521 LIHALAAlvrseFGVEAAVELVPPHSLprTSSGKLSRAKAKKRYL 565
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1470-1972 3.85e-17

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 87.35  E-value: 3.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1470 QPEPLVDVVSlfeRQVEalPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG 1549
Cdd:PRK10946   23 QDLPLTDILT---RHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1550 LVcvPLDVSYPAQRLALILETAQ--PFRVVAHPEHAHVAAAERVlpvEELVADI-----------------------EPE 1604
Cdd:PRK10946   98 VA--PVNALFSHQRSELNAYASQiePALLIADRQHALFSDDDFL---NTLVAEHsslrvvlllnddgehslddainhPAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1605 TFAA--PQLDELAMLLFTSGSTGRPKGVELSHrmwaNYTQWQLRVASGVPGL----RTLQF--APLSFDMAFQEIFSTLC 1676
Cdd:PRK10946  173 DFTAtpSPADEVAFFQLSGGSTGTPKLIPRTH----NDYYYSVRRSVEICGFtpqtRYLCAlpAAHNYPMSSPGALGVFL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1677 GGGELQLISnrermDPSALL--HVLERRQVQRVLL--PFVA--LQRLAEASNALGVRpgALRVVVSSGEqlRITEDVRAF 1750
Cdd:PRK10946  249 AGGTVVLAP-----DPSATLcfPLIEKHQVNVTALvpPAVSlwLQAIAEGGSRAQLA--SLKLLQVGGA--RLSETLARR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1751 CAAMPGLLLENQYGPTEThQVTYHSLSGDPAHYpdLPPIGRPL-DGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHR 1829
Cdd:PRK10946  320 IPAELGCQLQQVFGMAEG-LVNYTRLDDSDERI--FTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYK 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1830 APKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARE 1909
Cdd:PRK10946  397 SPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLL----RHPAVIHAALVSME 466

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523  1910 rqgnDAFLA----AFLLGEpEAVDLAELKQALRSE-LPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:PRK10946  467 ----DELMGekscAFLVVK-EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1050-1452 3.90e-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: 86.60  E-value: 3.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1050 FPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARSEPLI 1129
Cdd:cd19547    2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1130 LDLRG-NPEA-GTVLDEHIRQRRFHRYSLQQPGLFLFAAFVREDGLD-LVFSFHHAILDGWSVAnLIVALVAAYRGEPLP 1206
Cdd:cd19547   82 LDWSGeDPDRrAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHyLLWSHHHILLDGWCLS-LIWGDVFRVYEELAH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1207 GPAPALA-CH-VREELAALASPAAVGYwtgllEGARMTRlDGFGAHEPQAAQGPASHREALPDGL-------LERLKATA 1277
Cdd:cd19547  161 GREPQLSpCRpYRDYVRWIRARTAQSE-----ESERFWR-EYLRDLTPSPFSTAPADREGEFDTVvhefpeqLTRLVNEA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1278 AQR-GLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPVRSEI-AGCSWIEVADALFRQER 1354
Cdd:cd19547  235 ARGyGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPpELEGSEHMVGIFINTIPLRIRLdPDQTVTGLLETIHRDLA 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1355 DGHAHRRYPLSAIQQIVG----------DELSSAFNYV--NLHVLEPLWQLRDFRVWEETNFAllVNVIATPSDGMYLRI 1422
Cdd:cd19547  315 TTAAHGHVPLAQIKSWASgerlsggrvfDNLVAFENYPedNLPGDDLSIQIIDLHAQEKTEYP--IGLIVLPLQKLAFHF 392

                        410       420       430
                 ....*....|....*....|....*....|
gi 15598523 1423 DSDGRGISRSQAALIGATFVELLWRLADHP 1452
Cdd:cd19547  393 NYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 456-902 3.90e-17

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: 87.49  E-value: 3.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  456 ARTPQRTALLEADGG----TLSYAELDAKVQAVADALRAAGVRTDERVALLVARG-PHLLPAiLGVQRAGGAYVPINP-- 528
Cdd:cd05921    6 RQAPDRTWLAEREGNggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSiEHALMA-LAAMYAGVPAAPVSPay 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  529 ---DHPLERVRLLLEDCGARVVLVDErAATLGESLGE-----TRVLHLERLPQS--------------TGDLPAA--NVA 584
Cdd:cd05921   85 slmSQDLAKLKHLFELLKPGLVFAQD-AAPFARALAAifplgTPLVVSRNAVAGrgaisfaelaatppTAAVDAAfaAVG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  585 PGDLAYVIYTSGSTGMPKGVMVEHRSVV-NRLNWMQ-RRYPIGERDVLLQKTPvtfdvsvwelfwWSFT----------- 651
Cdd:cd05921  164 PDTVAKFLFTSGSTGLPKAVINTQRMLCaNQAMLEQtYPFFGEEPPVLVDWLP------------WNHTfggnhnfnlvl 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  652 --GARLSL-----LPPGAEkdprEMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARAA-ASSLRLVFCSGEALAPLQV 723
Cdd:cd05921  232 ynGGTLYIddgkpMPGGFE----ETLRNLREISPTVYFNVPAGWEMLVAALEKDEALRRRfFKRLKLMFYAGAGLSQDVW 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  724 ARFRRL----FGDAVRLVNLYGPTEAtvdvSDHECASDNPTRVP--IGRPIDNLrlyvldrALRPQPLGAVGELYIGGVG 797
Cdd:cd05921  308 DRLQALavatVGERIPMMAGLGATET----APTATFTHWPTERSglIGLPAPGT-------ELKLVPSGGKYEVRVKGPN 376

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  798 VARGYLNRPELNAERFLVDPFvaggrlYRTGDLARwLADGN-----LEYLGRADDQVKIR-GNRVEPDEVRDRLAAL--P 869
Cdd:cd05921  377 VTPGYWRQPELTAQAFDEEGF------YCLGDAAK-LADPDdpakgLVFDGRVAEDFKLAsGTWVSVGPLRARAVAAcaP 449

                        490       500       510
                 ....*....|....*....|....*....|...
gi 15598523  870 GVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQ 902
Cdd:cd05921  450 LVHDAVVAGEDRAEVGALVFPDLLACRRLVGLQ 482
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 1477-1945 4.64e-17

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: 87.55  E-value: 4.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1477 VVSLFERQVEALPGSAALAFEEQR-----WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLV 1551
Cdd:cd05968   63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1552 CVPLDVSYPAQRLALILE--------TAQPF----RVVAHPEHAHVAAA-----ERVLPVEEL--------VADIEPETF 1606
Cdd:cd05968  143 VVPIFSGFGKEAAATRLQdaeakaliTADGFtrrgREVNLKEEADKACAqcptvEKVVVVRHLgndftpakGRDLSYDEE 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1607 AAPQLDELA--------MLLFTSGSTGRPKGVELSHRMWA------NYTQWQLRvasgvPGLRTLQFAPLSFDMAFQEIF 1672
Cdd:cd05968  223 KETAGDGAErtesedplMIIYTSGTTGKPKGTVHVHAGFPlkaaqdMYFQFDLK-----PGDLLTWFTDLGWMMGPWLIF 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1673 STLCGGGELQLISNR-ERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPG--ALRVVVSSGEQlrITEDVRA 1749
Cdd:cd05968  298 GGLILGATMVLYDGApDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDlsSLRVLGSTGEP--WNPEPWN 375

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1750 FCAAMPG---LLLENQYGPTEthqvtyhsLSGDPAHYPDLPPI-----GRPLDGVEVQVLDAALRPVPVGVtGEL----- 1816
Cdd:cd05968  376 WLFETVGkgrNPIINYSGGTE--------ISGGILGNVLIKPIkpssfNGPVPGMKADVLDESGKPARPEV-GELvllap 446

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1817 YFGgdcLARGYHRAPkltaERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeR 1896
Cdd:cd05968  447 WPG---MTRGFWRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLN----A 515

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 15598523 1897 QPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHM 1945
Cdd:cd05968  516 HPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADEL 564
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 1463-1963 6.49e-17

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 86.96  E-value: 6.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1463 PRRDAASQPEPLVDVVSLFERQV---EALPGSAalafeeqrWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMI 1539
Cdd:PLN02330   23 PVPDKLTLPDFVLQDAELYADKVafvEAVTGKA--------VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1540 ATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEH-AHVAAAErvLPV--------------EELV--ADIE 1602
Cdd:PLN02330   95 IVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNyGKVKGLG--LPVivlgeekiegavnwKELLeaADRA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1603 PETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPG-LRTLQFAPLSFDMAFQEI-FSTLCG 1677
Cdd:PLN02330  173 GDTSDNEEIlqTDLCALPFSSGTTGISKGVMLTHRnLVANLCSSLFSVGPEMIGqVVTLGLIPFFHIYGITGIcCATLRN 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1678 GGELQLISnreRMDPSALLHVLERRQVQrvLLPFVALQRLAEASNAL----GVRPGALRVVVSSGEQLrITEDVRAFCAA 1753
Cdd:PLN02330  253 KGKVVVMS---RFELRTFLNALITQEVS--FAPIVPPIILNLVKNPIveefDLSKLKLQAIMTAAAPL-APELLTAFEAK 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1754 MPGLLLENQYGPTETHQVTYhsLSGDPAHYPDLP---PIGRPLDGVEVQVLDAAL-RPVPVGVTGELYFGGDCLARGYHR 1829
Cdd:PLN02330  327 FPGVQVQEAYGLTEHSCITL--THGDPEKGHGIAkknSVGFILPNLEVKFIDPDTgRSLPKNTPGELCVRSQCVMQGYYN 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1830 APKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARE 1909
Cdd:PLN02330  405 NKEETDRTIDEDGW------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILL----THPSVEDAAVVPLP 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15598523  1910 RQGNDAFLAAFLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PLN02330  475 DEEAGEIPAACVVINPKAKESEEdILNFVAANVAHYKKVRVVQFVDSIPKSLSGK 529
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 471-939 6.68e-17

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: 86.99  E-value: 6.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAG-------GAYVP------INPDHPlerVRL 537
Cdd:cd05967   82 TYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAAkelasrIDDAKP---KLI 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  538 LLEDCGA---RVV----LVDErAATLGESLGEtRVLHLERlPQSTGDL-------------------PAANVAPGDLAYV 591
Cdd:cd05967  159 VTASCGIepgKVVpykpLLDK-ALELSGHKPH-HVLVLNR-PQVPADLtkpgrdldwsellakaepvDCVPVAATDPLYI 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  592 IYTSGSTGMPKGVMVEHRSVVNRLNW-MQRRYPIGERDVllqktpvtfdvsvwelfWWSFT------GARLSLLPP---G 661
Cdd:cd05967  236 LYTSGTTGKPKGVVRDNGGHAVALNWsMRNIYGIKPGDV-----------------WWAASdvgwvvGHSYIVYGPllhG 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  662 AEK-----------DPREMLRSIQRDAVTVIHFVPSMLTPFL-DLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRL 729
Cdd:cd05967  299 ATTvlyegkpvgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRkEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENT 378

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  730 FGdaVRLVNLYGPTEATvdvsdhECASDNPTRV---PI-----GRPIDNLRLYVLDRALRPQPLGAVGELYIGGvGVARG 801
Cdd:cd05967  379 LG--VPVIDHWWQTETG------WPITANPVGLeplPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPG 449

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  802 YLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDS 881
Cdd:cd05967  450 CLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRD 529

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  882 AVRGTHLVGYYV--AAAELDPGQLRAGLSATLPDFMLP------AFFVriDSLPLSANGKLDRRQL 939
Cdd:cd05967  530 ELKGQVPLGLVVlkEGVKITAEELEKELVALVREQIGPvaafrlVIFV--KRLPKTRSGKILRRTL 593
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 1616-1965 1.14e-16

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: 83.86  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1616 MLLFTSGSTGRPKGVELSHR--MWANYtqwQLRVASGV-PGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDP 1692
Cdd:cd17637    4 VIIHTAAVAGRPRGAVLSHGnlIAANL---QLIHAMGLtEADVYLNMLPLFHIAGLNLALATFHAGGANVVM---EKFDP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1693 SALLHVLERRQVQrVLLPFVA-LQRLAEASNALGVRPGALRVVVSsgeqLRITEDVRAFCAAMPGLLLeNQYGPTETHQ- 1770
Cdd:cd17637   78 AEALELIEEEKVT-LMGSFPPiLSNLLDAAEKSGVDLSSLRHVLG----LDAPETIQRFEETTGATFW-SLYGQTETSGl 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1771 VTYHSLSGDPAhypdlpPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFvehpwRPGarLY 1850
Cdd:cd17637  152 VTLSPYRERPG------SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-----RNG--WH 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1851 RTGDLGRILGNGEIVWLGRADTQ--VKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA-RERQGNDAFLAAFLLGEPEA 1927
Cdd:cd17637  219 HTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVIL----EHPAIAEVCVIGvPDPKWGEGIKAVCVLKPGAT 294

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 15598523 1928 VDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 1965
Cdd:cd17637  295 LTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSID 332
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 1493-1906 1.25e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 85.43  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1493 ALAFEEQRWTYRDLDHVARCVATRLvrAGARRgdaIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ 1572
Cdd:PRK07787   18 AVRIGGRVLSRSDLAGAATAVAERV--AGARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1573 PFRVVAHPEHAhvAAAERVLPVEELVAdiEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-------MWANYTQWQL 1645
Cdd:PRK07787   93 AQAWLGPAPDD--PAGLPHVPVRLHAR--SWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRaiaadldALAEAWQWTA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1646 R--VASGVP-----GLRTLQFAPLSFdmafqeifstlcGGGELQLIsnreRMDPSALLHVLERRQVQRVLLPFVaLQRLA 1718
Cdd:PRK07787  169 DdvLVHGLPlfhvhGLVLGVLGPLRI------------GNRFVHTG----RPTPEAYAQALSEGGTLYFGVPTV-WSRIA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1719 EASNALGVRPGAlRVVVSSGEQLRITEDVRafCAAMPGLLLENQYGPTETHQVTyhSLSGDPAHYPDLppIGRPLDGVEV 1798
Cdd:PRK07787  232 ADPEAARALRGA-RLLVSGSAALPVPVFDR--LAALTGHRPVERYGMTETLITL--STRADGERRPGW--VGLPLAGVET 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1799 QVLDAALRPVPVGV--TGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQ-VK 1875
Cdd:PRK07787  305 RLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGRESTDlIK 378

                         410       420       430
                  ....*....|....*....|....*....|.
gi 15598523  1876 VRGFRIEPAEVELAIMrqaeRQPGLRGAAVV 1906
Cdd:PRK07787  379 SGGYRIGAGEIETALL----GHPGVREAAVV 405
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 456-939 1.25e-16

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: 85.51  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  456 ARTPQRTALLEADGGTLSYAELDAKVQAVADALRAAGVRTDERVallvarGPHLLPAILGVQRAGGAYVPINPDHPLERV 535
Cdd:cd05929    2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGV------YIYLINSILTVFAAAAAWKCGACPAYKSSR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  536 RLLLEDCGARVVLVD---ERAATLGESLGetRVLHLERLPQSTGDLPAANVAPGDlaYVIYTSGSTGMPKGVMVEH--RS 610
Cdd:cd05929   76 APRAEACAIIEIKAAalvCGLFTGGGALD--GLEDYEAAEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGIKRGLpgGP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  611 VVNRLNWM-QRRYPIGERDVLLQKTPVTFDVSvwelFWWSFTGARLSLLPPGAEK-DPREMLRSIQRDAVTVIHFVPSML 688
Cdd:cd05929  152 PDNDTLMAaALGFGPGADSVYLSPAPLYHAAP----FRWSMTALFMGGTLVLMEKfDPEEFLRLIERYRVTFAQFVPTMF 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  689 TPFLDLLDGDPtARAAASSLRLVFCSGEALAPLQVARFRRLFGDavRLVNLYGPTEA---TVdvsdheCASDNPTRVP-- 763
Cdd:cd05929  228 VRLLKLPEAVR-NAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGP--IIWEYYGGTEGqglTI------INGEEWLTHPgs 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  764 IGRPIDNlRLYVLDRALRPQPLGAVGELYIGGvGVARGYLNRPELNAERFLVDPFVAggrlyrTGDLARWLADGNLEYLG 843
Cdd:cd05929  299 VGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST------LGDVGYLDEDGYLYLTD 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  844 RADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVA--------RDSAVRGTHLVGyyvAAAELDPGQLRAGLSATLPDFM 915
Cdd:cd05929  371 RRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGvpdeelgqRVHAVVQPAPGA---DAGTALAEELIAFLRDRLSRYK 447

                        490       500
                 ....*....|....*....|....
gi 15598523  916 LPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05929  448 CPRSIEFVAELPRDDTGKLYRRLL 471
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 1611-1963 2.21e-16

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 85.26  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1611 LDELAMLLFTSGSTGRPKGVELSH-----RMWANYTQWQLRVASGVPGLRTLQ---FAPLSFDMAFQEIFSTLC---GGG 1679
Cdd:PRK12492  206 LDDIAVLQYTGGTTGLAKGAMLTHgnlvaNMLQVRACLSQLGPDGQPLMKEGQevmIAPLPLYHIYAFTANCMCmmvSGN 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1680 ELQLISNRErmDPSALLHVLERRQvqrvllpFVALQRLAEASNALGVRPG-------ALRVVVSSGEQLritedVRAFC- 1751
Cdd:PRK12492  286 HNVLITNPR--DIPGFIKELGKWR-------FSALLGLNTLFVALMDHPGfkdldfsALKLTNSGGTAL-----VKATAe 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1752 --AAMPGLLLENQYGPTETHQVTYHSLSGDPAHypdLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHR 1829
Cdd:PRK12492  352 rwEQLTGCTIVEGYGLTETSPVASTNPYGELAR---LGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQ 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1830 APKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VA 1907
Cdd:PRK12492  429 QPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM----AHPKVANCAAigVP 498

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  1908 RERQGNDAFLaaFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK12492  499 DERSGEAVKL--FVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGK 552
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 472-839 2.23e-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: 84.96  E-value: 2.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  472 LSYAELDAKVQAVADALRAAGVRT--DERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLV 549
Cdd:cd05927    6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  550 DERAATLgeSLGEtrVLHLERLPQSTGDLPAanvaPGDLAYVIYTSGSTGMPKGVMVEHRSVVN---RLNW-MQRRYPIG 625
Cdd:cd05927   86 DAGVKVY--SLEE--FEKLGKKNKVPPPPPK----PEDLATICYTSGTTGNPKGVMLTHGNIVSnvaGVFKiLEILNKIN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  626 ERDVLLQKTPVT--FDVSVWELFWwsFTGARLSLLppgaEKDPREMLRSIQRDAVTVIHFVPSMLT-------------- 689
Cdd:cd05927  158 PTDVYISYLPLAhiFERVVEALFL--YHGAKIGFY----SGDIRLLLDDIKALKPTVFPGVPRVLNriydkifnkvqakg 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  690 --------------------------PFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPT 743
Cdd:cd05927  232 plkrklfnfalnyklaelrsgvvrasPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALG--CPVLEGYGQT 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  744 E----ATVDVSDHECASDnptrvpIGRPIDNLRLYVLD------RALRPQPlgaVGELYIGGVGVARGYLNRPELNAERF 813
Cdd:cd05927  310 EctagATLTLPGDTSVGH------VGGPLPCAEVKLVDvpemnyDAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEAL 380

                        410       420
                 ....*....|....*....|....*.
gi 15598523  814 LVDPFvaggrlYRTGDLARWLADGNL 839
Cdd:cd05927  381 DEDGW------LHTGDIGEWLPNGTL 400
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 451-939 3.56e-16

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 83.77  E-value: 3.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   451 FAEQvarTPQRTALlEADGGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDH 530
Cdd:PRK09029   12 WAQV---RPQAIAL-RLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   531 PLERVRLLLEDCGARVVLVDERAATlgesLGETRVLHLerlpQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHR- 609
Cdd:PRK09029   88 PQPLLEELLPSLTLDFALVLEGENT----FSALTSLHL----QLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQa 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   610 ---SVVNRLNWMqrryPIGERDVLLQKTPVtFDVS----VWElfwWSFTGARLSLlppGAEKDPREMLRSiqrdaVTVIH 682
Cdd:PRK09029  160 hlaSAEGVLSLM----PFTAQDSWLLSLPL-FHVSgqgiVWR---WLYAGATLVV---RDKQPLEQALAG-----CTHAS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   683 FVPSMLTPFLDlldgdptARAAASSLRLVFCSGEALaPLQVARFRRLFGdaVRLVNLYGPTEA--TVdvsdheCASDNPT 760
Cdd:PRK09029  224 LVPTQLWRLLD-------NRSEPLSLKAVLLGGAAI-PVELTEQAEQQG--IRCWCGYGLTEMasTV------CAKRADG 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   761 RVPIGRPIDNLRLYVLDralrpqplgavGELYIGGVGVARGYLNRPELNaerflvdPFVAGGRLYRTGDLARWlADGNLE 840
Cdd:PRK09029  288 LAGVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEW-QNGELT 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   841 YLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPaff 920
Cdd:PRK09029  349 ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVNLAEWLQDKLARFQQP--- 425

                         490       500
                  ....*....|....*....|..
gi 15598523   921 VRIDSLPLS-ANG--KLDRRQL 939
Cdd:PRK09029  426 VAYYLLPPElKNGgiKISRQAL 447
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 448-939 3.99e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 84.23  E-value: 3.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   448 PTLFAEQVART-PQRTALLEadGGT-LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVP 525
Cdd:PRK08162   20 PLSFLERAAEVyPDRPAVIH--GDRrRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   526 INPDHPLERVRLLLEDCGARVVLVD-ERAATLGESLGETRVLHL----ERLPQSTGDLPA------ANVAPGDLAYVI-- 592
Cdd:PRK08162   98 LNTRLDAASIAFMLRHGEAKVLIVDtEFAEVAREALALLPGPKPlvidVDDPEYPGGRFIgaldyeAFLASGDPDFAWtl 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   593 -----------YTSGSTGMPKGVMVEHR-----SVVNRLNWMQRRYPigerdVLLQKTPVtFDVSVWeLFWWSFT---GA 653
Cdd:PRK08162  178 padewdaialnYTSGTTGNPKGVVYHHRgaylnALSNILAWGMPKHP-----VYLWTLPM-FHCNGW-CFPWTVAaraGT 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   654 RLSLlppgAEKDPREMLRSIQRDAVTviHF-----VPSMltpfldLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRR 728
Cdd:PRK08162  251 NVCL----RKVDPKLIFDLIREHGVT--HYcgapiVLSA------LINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   729 LfgdAVRLVNLYGPTE----ATV--------DVSDHECASDNpTRVPIGRPIDNlRLYVLDRA-LRPQPLGA--VGELYI 793
Cdd:PRK08162  319 I---GFDLTHVYGLTEtygpATVcawqpewdALPLDERAQLK-ARQGVRYPLQE-GVTVLDPDtMQPVPADGetIGEIMF 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   794 GGVGVARGYLNRPELNAERFlvdpfvAGGrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRD 873
Cdd:PRK08162  394 RGNIVMKGYLKNPKATEEAF------AGG-WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLV 466

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523   874 AAVVARDSAVRGThlvgyyVAAAELdpgQLRAGLSAT-----------LPDFMLPAfFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK08162  467 AAVVAKPDPKWGE------VPCAFV---ELKDGASATeeeiiahcrehLAGFKVPK-AVVFGELPKTSTGKIQKFVL 533
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 1502-1869 4.37e-16

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: 84.43  E-value: 4.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1502 TYRDL-DHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHP 1580
Cdd:cd17632   69 TYAELwERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1581 EHAHVA-------------------------------AAERVLPV------EELVADIEPETFAAPQL------DELAML 1617
Cdd:cd17632  149 EHLDLAveavleggtpprlvvfdhrpevdahraalesARERLAAVgipvttLTLIAVRGRDLPPAPLFrpepddDPLALL 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1618 LFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLR-TLQFAPLSFDMAFQEIFSTLCGGGELQLISnreRMDPSALL 1696
Cdd:cd17632  229 IYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASiTLNFMPMSHIAGRISLYGTLARGGTAYFAA---ASDMSTLF 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1697 HVL-ERRQVQRVLLPFVA------LQRLAEASNALGVRPGALRVVVssGEQLR-----------------ITEDVRAFCA 1752
Cdd:cd17632  306 DDLaLVRPTELFLVPRVCdmlfqrYQAELDRRSVAGADAETLAERV--KAELRervlggrllaavcgsapLSAEMKAFME 383

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1753 AMPGLLLENQYGPTETHQVTyhslsgdpahypdlppigrpLDGVEV--QVLDAALRPVP-VG--VT------GELYFGGD 1821
Cdd:cd17632  384 SLLDLDLHDGYGSTEAGAVI--------------------LDGVIVrpPVLDYKLVDVPeLGyfRTdrphprGELLVKTD 443

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 15598523 1822 CLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGR 1869
Cdd:cd17632  444 TLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDR 485
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 445-898 4.86e-16

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 84.22  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   445 ATLPTLFAEQVARTPQRTALL----EADGG----TLSYAELDAKVQAVADALRAAGVRTDeRVALLVARGPHLLPAILGV 516
Cdd:PRK05850    1 SSVPSLLRERASLQPDDAAFTfidyEQDPAgvaeTLTWSQLYRRTLNVAEELRRHGSTGD-RAVILAPQGLEYIVAFLGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   517 QRAGGAYVPINPDHP---LERVRLLLEDCGARVVL-----VDERAATLGESLGET--RVLHLERLPQSTGDLPAANVAPG 586
Cdd:PRK05850   80 LQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLttsavVDDVTEYVAPQPGQSapPVIEVDLLDLDSPRGSDARPRDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   587 -DLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYpIGERDVLLqkTPVTFDVSvwelfWWSF---TGARLSLLPPGA 662
Cdd:PRK05850  160 pSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY-FGDTGGVP--PPDTTVVS-----WLPFyhdMGLVLGVCAPIL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   663 EKDPREMLRSI---QRDAvtvihfvpsmltPFLDLLDGDPTARAAA----------------------SSLRLVFCSGEA 717
Cdd:PRK05850  232 GGCPAVLTSPVaflQRPA------------RWMQLLASNPHAFSAApnfafelavrktsdddmagldlGGVLGIISGSER 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   718 LAPLQVARFRRLFG------DAVRlvNLYGPTEATVDVS-------------DHE---------CASDNPTR-VPIGRPI 768
Cdd:PRK05850  300 VHPATLKRFADRFApfnlreTAIR--PSYGLAEATVYVAtrepgqppesvrfDYEklsaghakrCETGGGTPlVSYGSPR 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   769 DNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERF---LVDPfVAG---GRLYRTGDLArWLADGNLEYL 842
Cdd:PRK05850  378 SPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDP-SPGtpeGPWLRTGDLG-FISEGELFIV 455

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523   843 GRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAV-VARDSAvrgTHLvgyyVAAAEL 898
Cdd:PRK05850  456 GRIKDLLIVDGRNHYPDDIEATIQEITGGRVAAIsVPDDGT---EKL----VAIIEL 505
PRK08315 PRK08315
AMP-binding domain protein; Validated
 1480-1963 8.15e-16

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 83.32  E-value: 8.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1480 LFERQVEALPGSAALAFEEQ--RWTYRDLDHVARCVATRLVRAGARRGDAIGV-ALNRsPEMIATIWGILRAGLVCVPLD 1556
Cdd:PRK08315   21 LLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIwAPNV-PEWVLTQFATAKIGAILVTIN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1557 VSYPAQRLALILE--------TAQPFRVVAH--------PEHAHVAA----AERV-----------------LPVEELVA 1599
Cdd:PRK08315  100 PAYRLSELEYALNqsgckaliAADGFKDSDYvamlyelaPELATCEPgqlqSARLpelrrviflgdekhpgmLNFDELLA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1600 DiePETFAAPQLDELAMLL---------FTSGSTGRPKGVELSHRMWAN----------YTQwQLRVASGVPglrtlqfa 1660
Cdd:PRK08315  180 L--GRAVDDAELAARQATLdpddpiniqYTSGTTGFPKGATLTHRNILNngyfigeamkLTE-EDRLCIPVP-------- 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1661 plsfdmafqeifstL--CGG---GELQLISNR-------ERMDPsalLHVLERRQVQR------VLLPFVALQRLAE-AS 1721
Cdd:PRK08315  249 --------------LyhCFGmvlGNLACVTHGatmvypgEGFDP---LATLAAVEEERctalygVPTMFIAELDHPDfAR 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1722 NAL-----GVRPGAL-------RVVvssgEQLRITEDVRAfcaampglllenqYGPTETHQVTYHSLSGDPAhypDL--P 1787
Cdd:PRK08315  312 FDLsslrtGIMAGSPcpievmkRVI----DKMHMSEVTIA-------------YGMTETSPVSTQTRTDDPL---EKrvT 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1788 PIGRPLDGVEVQVLDAAL-RPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNG--EI 1864
Cdd:PRK08315  372 TVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW------MHTGDLAVMDEEGyvNI 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1865 VwlGRadtqVK---VRGFR-IEPAEVElaimrqaE---RQPGLRGAAV--VARERQGNDafLAAFL-LGEPEAVDLAELK 1934
Cdd:PRK08315  446 V--GR----IKdmiIRGGEnIYPREIE-------EflyTHPKIQDVQVvgVPDEKYGEE--VCAWIiLRPGATLTEEDVR 510

                         570       580
                  ....*....|....*....|....*....
gi 15598523  1935 QALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK08315  511 DFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 1448-1891 1.10e-15

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 83.02  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1448 LADHPDEAADFAFLAPRRDAASQPEPLVDVVslFE---RQVE-ALPGSAALAF----EEQRWTYRDLDHVARCVATRLVR 1519
Cdd:PRK04319   15 LKDYEETYATFSWEEVEKEFSWLETGKVNIA--YEaidRHADgGRKDKVALRYldasRKEKYTYKELKELSNKFANVLKE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1520 AGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLdvsYPA-------QRL------ALILETAQPFRVVA----HPEH 1582
Cdd:PRK04319   93 LGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL---FEAfmeeavrDRLedseakVLITTPALLERKPAddlpSLKH 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1583 -----AHVAAAERVLPVEELVADiEPETFAAP--QLDELAMLLFTSGSTGRPKGVELSHR-MWANY--TQWQLRVASG-- 1650
Cdd:PRK04319  170 vllvgEDVEEGPGTLDFNALMEQ-ASDEFDIEwtDREDGAILHYTSGSTGKPKGVLHVHNaMLQHYqtGKYVLDLHEDdv 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1651 ---------VPGLRTLQFAPLsfdmafqeifstLCGggeLQLISNRERMDPSALLHVLERrqvQRVLLPF---VALQRLA 1718
Cdd:PRK04319  249 ywctadpgwVTGTSYGIFAPW------------LNG---ATNVIDGGRFSPERWYRILED---YKVTVWYtapTAIRMLM 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1719 EASNAL--GVRPGALRVVVSSGEQLR---ITEDVRAFcaampGLLLENQYGPTET--HQVtyhslsgdpAHYP--DLPP- 1788
Cdd:PRK04319  311 GAGDDLvkKYDLSSLRHILSVGEPLNpevVRWGMKVF-----GLPIHDNWWMTETggIMI---------ANYPamDIKPg 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1789 -IGRPLDGVEVQVLDAALRPVPVGVTGELYF--GGDCLARGYHRAPkltaERFvEHPWRPGarLYRTGDLGRILGNGEIV 1865
Cdd:PRK04319  377 sMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNP----EKY-ESYFAGD--WYVSGDSAYMDEDGYFW 449

                         490       500
                  ....*....|....*....|....*.
gi 15598523  1866 WLGRADTQVKVRGFRIEPAEVELAIM 1891
Cdd:PRK04319  450 FQGRVDDVIKTSGERVGPFEVESKLM 475
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 454-939 1.22e-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: 83.07  E-value: 1.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    454 QVARTPQRTALL-EADGG----TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAG-------- 520
Cdd:TIGR02188   66 HLEARPDKVAIIwEGDEPgevrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGaihsvvfg 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    521 --------------GAYVPINPD--------HPLER-VRLLLEDCGARV--VLVDERAATLGESLGETRVLHLERLPQST 575
Cdd:TIGR02188  146 gfsaealadrindaGAKLVITADeglrggkvIPLKAiVDEALEKCPVSVehVLVVRRTGNPVVPWVEGRDVWWHDLMAKA 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    576 GD-LPAANVAPGDLAYVIYTSGSTGMPKGVMveHrSVVNRLNW--MQRRYpigerdvllqktpvTFDVSVWELFW----- 647
Cdd:TIGR02188  226 SAyCEPEPMDSEDPLFILYTSGSTGKPKGVL--H-TTGGYLLYaaMTMKY--------------VFDIKDGDIFWctadv 288

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    648 -WsFTGARLSLLPP---GAEK----------DPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDgDPTARAAASSLRLVFC 713
Cdd:TIGR02188  289 gW-ITGHSYIVYGPlanGATTvmfegvptypDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGD-EWVKKHDLSSLRLLGS 366

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    714 SGEALAPLQVARFRRLFGD-AVRLVNLYGPTEATVDVSDHEcasdnPTRVPI-----GRPIDNLRLYVLDraLRPQPLGA 787
Cdd:TIGR02188  367 VGEPINPEAWMWYYKVVGKeRCPIVDTWWQTETGGIMITPL-----PGATPTkpgsaTLPFFGIEPAVVD--EEGNPVEG 439

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    788 VGElyiGGV--------GVARGYLNRPelnaERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPD 859
Cdd:TIGR02188  440 PGE---GGYlvikqpwpGMLRTIYGDH----ERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTA 512

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    860 EVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQ-----LRAGLSATLPDFMLPA--FFVriDSLPLSANG 932
Cdd:TIGR02188  513 EIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDelrkeLRKHVRKEIGPIAKPDkiRFV--PGLPKTRSG 590


                   ....*..
gi 15598523    933 KLDRRQL 939
Cdd:TIGR02188  591 KIMRRLL 597
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 1500-1864 2.10e-15

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: 81.88  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1500 RW-TYRDLDHVARCVATRLVRAGARRGDA--IGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRV 1576
Cdd:cd05927    4 EWiSYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1577 VahpehahVAAAERVLPVEELV----ADIEPETFAAPqlDELAMLLFTSGSTGRPKGVELSHRMWANYTQ---WQLRVAS 1649
Cdd:cd05927   84 F-------CDAGVKVYSLEEFEklgkKNKVPPPPPKP--EDLATICYTSGTTGNPKGVMLTHGNIVSNVAgvfKILEILN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1650 GV-PGLRTLQFAPLS--FDMAFQEifSTLCGGGELQLIS--NRERMDPSALL---------HVLER------------RQ 1703
Cdd:cd05927  155 KInPTDVYISYLPLAhiFERVVEA--LFLYHGAKIGFYSgdIRLLLDDIKALkptvfpgvpRVLNRiydkifnkvqakGP 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1704 VQRVLLPFVALQRLAEASN-------------------ALGvrpGALRVVVSSGEQlrITEDVRAFCAAMPGLLLENQYG 1764
Cdd:cd05927  233 LKRKLFNFALNYKLAELRSgvvraspfwdklvfnkikqALG---GNVRLMLTGSAP--LSPEVLEFLRVALGCPVLEGYG 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1765 PTETHQVTYHSLSGDPahypDLPPIGRPLDGVEVQVLDA------ALRPVPvgvTGELYFGGDCLARGYHRAPKLTAERF 1838
Cdd:cd05927  308 QTECTAGATLTLPGDT----SVGHVGGPLPCAEVKLVDVpemnydAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEAL 380

                        410       420
                 ....*....|....*....|....*.
gi 15598523 1839 VEHPWrpgarlYRTGDLGRILGNGEI 1864
Cdd:cd05927  381 DEDGW------LHTGDIGEWLPNGTL 400
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 1481-1643 2.17e-15

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 82.23  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1481 FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 1560
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1561 AQRLALILETAQPFRVVAHPEHAHV---AAAERVLPVEELVADIE----------------------PETFAAPQLDELA 1615
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEELVEAfeeARADLARPPRLWVAGGDtlddpegyedlaaaaagapttnPASRSGVTAKDTA 202

                         170       180
                  ....*....|....*....|....*...
gi 15598523  1616 MLLFTSGSTGRPKGVELSHRMWANYTQW 1643
Cdd:PRK08279  203 FYIYTSGTTGLPKAAVMSHMRWLKAMGG 230
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 1613-1963 3.20e-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: 79.47  E-value: 3.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1613 ELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQE-IFSTLCGGGElqlISNRERMD 1691
Cdd:cd17638    1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAgIVACLLTGAT---VVPVAVFD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1692 PSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETHQV 1771
Cdd:cd17638   78 VDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPV-ELVRRMRSELGFETVLTAYGLTEAGVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1772 TYHSLSGDPAHYPDlpPIGRPLDGVEVQVLDAalrpvpvgvtGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYR 1851
Cdd:cd17638  157 TMCRPGDDAETVAT--TCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW------LH 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1852 TGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDAflAAFLLG-EPEAV 1928
Cdd:cd17638  219 TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALA----EHPGVAQVAVigVPDERMGEVG--KAFVVArPGVTL 292

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 15598523 1929 DLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd17638  293 TEEDVIAWCRERLANYKVPRFVRFLDELPRNASGK 327
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 1497-1970 3.47e-15

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: 81.36  E-value: 3.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1497 EEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFR 1575
Cdd:cd05928   38 DEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKC 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1576 VVAH----PEHAHVAAAERVLPVEELVADIEPE---------TFAAPQ--------LDELAmLLFTSGSTGRPKGVELSH 1634
Cdd:cd05928  118 IVTSdelaPEVDSVASECPSLKTKLLVSEKSRDgwlnfkellNEASTEhhcvetgsQEPMA-IYFTSGTTGSPKMAEHSH 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1635 rmwanyTQWQLRVASGVPGLRTLQFAPLSFDM--------AFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQr 1706
Cdd:cd05928  197 ------SSLGLGLKVNGRYWLDLTASDIMWNTsdtgwiksAWSSLFEPWIQGACV-FVHHLPRFDPLVILKTLSSYPIT- 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1707 VLLPFVALQRLAEASNALGVRPGALRVVVSSGEQlrITEDVRAFCAAMPGLLLENQYGPTETHQV--TYHSLSGDPAHyp 1784
Cdd:cd05928  269 TFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEP--LNPEVLEKWKAQTGLDIYEGYGQTETGLIcaNFKGMKIKPGS-- 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1785 dlppIGRPLDGVEVQVLDAALRPVPVGVTGELY--------FggdCLARGYHRAPKLTAERFVehpwrpgARLYRTGDLG 1856
Cdd:cd05928  345 ----MGKASPPYDVQIIDDNGNVLPPGTEGDIGirvkpirpF---GLFSGYVDNPEKTAATIR-------GDFYLTGDRG 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1857 RILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQ--GN--DAFL---AAFLLGEPEAVd 1929
Cdd:cd05928  411 IMDEDGYFWFMGRADDVINSSGYRIGPFEVESALI----EHPAVVESAVVSSPDPirGEvvKAFVvlaPQFLSHDPEQL- 485

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 15598523 1930 LAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd05928  486 TKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 1502-1963 4.11e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 80.89  E-value: 4.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1502 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPE 1581
Cdd:PRK13391   26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1582 HAHVAAA--------------------ERVLPVEELVADIePETfaaPQLDEL--AMLLFTSGSTGRPKGV--------- 1630
Cdd:PRK13391  106 KLDVARAllkqcpgvrhrlvldgdgelEGFVGYAEAVAGL-PAT---PIADESlgTDMLYSSGTTGRPKGIkrplpeqpp 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1631 -------ELSHRMWaNYTQwQLRVASGVPGLRTlqfAPLSFDMAFQEIfstlcgGGELQLIsnrERMDPSALLHVLERRQ 1703
Cdd:PRK13391  182 dtplpltAFLQRLW-GFRS-DMVYLSPAPLYHS---APQRAVMLVIRL------GGTVIVM---EHFDAEQYLALIEEYG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1704 V---QRVLLPFVALQRLAEAsnalgVRpgaLRVVVSSGEqlritedvRAFCAAMP-------------GLLLENQYGPTE 1767
Cdd:PRK13391  248 VthtQLVPTMFSRMLKLPEE-----VR---DKYDLSSLE--------VAIHAAAPcppqvkeqmidwwGPIIHEYYAATE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1768 THQVTYhslsGDPAHYPDLP-PIGRPLDGVeVQVLDAALRPVPVGVTGELYFGGDcLARGYHRAPKLTAERFVEHP-WRp 1845
Cdd:PRK13391  312 GLGFTA----CDSEEWLAHPgTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGG-RPFEYLNDPAKTAEARHPDGtWS- 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1846 garlyRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGND--AFLAAFL 1921
Cdd:PRK13391  385 -----TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLI----THPKVADAAVfgVPNEDLGEEvkAVVQPVD 455

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 15598523  1922 LGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK13391  456 GVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGK 497
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 84-336 6.81e-15

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: 79.40  E-value: 6.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   84 RHVDLRADR---DPEAAVRSWLRDAF-RHAYPLDGRS--LVDLALLHSDQA--LYVYVRTHHIVSDAWGLQLFLSRVRAG 155
Cdd:cd19544   73 RQAELPVEEltlDPGDDALAQLRARFdPRRYRLDLRQapLLRAHVAEDPANgrWLLLLLFHHLISDHTSLELLLEEIQAI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  156 YLGELGEPQAQMP----TASLLAQLETDDYsgseqyrgdRAYFAEALEGL-EPALftrrrPAGL-------RRTARHRLT 223
Cdd:cd19544  153 LAGRAAALPPPVPyrnfVAQARLGASQAEH---------EAFFREMLGDVdEPTA-----PFGLldvqgdgSDITEARLA 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  224 LERTLLDAIRD----RGESPFLFLSAAVALYLARIHQNDDVVLGVpVL-------NRADRAakqvVGHFANTLPLRIRTA 292
Cdd:cd19544  219 LDAELAQRLRAqarrLGVSPASLFHLAWALVLARCSGRDDVVFGT-VLsgrmqggAGADRA----LGMFINTLPLRVRLG 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15598523  293 pEQTVDEFLAQLREATRTLLRHQKMPLGDLLR-----GASPLFDTTLSY 336
Cdd:cd19544  294 -GRSVREAVRQTHARLAELLRHEHASLALAQRcsgvpAPTPLFSALLNY 341
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 1586-1975 7.67e-15

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 81.12  E-value: 7.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1586 AAAERVLPVeelvADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQW-QL-------RVASGVP---- 1652
Cdd:PRK08633  760 LLAARLLPA----RLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHnILSNIEQIsDVfnlrnddVILSSLPffhs 835

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1653 -GLRTLQFAPLSF-----------------DMAFQEIFSTLCGGGE-LQLISNRERMDPsallhvlerrqvqrvlLPFva 1713
Cdd:PRK08633  836 fGLTVTLWLPLLEgikvvyhpdptdalgiaKLVAKHRATILLGTPTfLRLYLRNKKLHP----------------LMF-- 897

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1714 lqrlaeasnalgvrpGALRVVVSSGEQLRitEDVR-AFCAAMPGLLLENqYGPTETHQVTyhSLSGDPAHYPDLPP---- 1788
Cdd:PRK08633  898 ---------------ASLRLVVAGAEKLK--PEVAdAFEEKFGIRILEG-YGATETSPVA--SVNLPDVLAADFKRqtgs 957

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1789 ----IGRPLDGVEVQVLDA-ALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEhpwRPGARLYRTGDLGRILGNGE 1863
Cdd:PRK08633  958 kegsVGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGF 1034

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1864 IVWLGRADTQVKVRGFRIEPAEVELAIMRQAERQPGLRGAAVVARERQGNdaflAAFLLGEPEAVDLAELKQALR-SELP 1942
Cdd:PRK08633 1035 LTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVPDEKKGE----KLVVLHTCGAEDVEELKRAIKeSGLP 1110

                         410       420       430
                  ....*....|....*....|....*....|...
gi 15598523  1943 EHMVPAHFAWVDGFALTPSGKRDDAALRALPLE 1975
Cdd:PRK08633 1111 NLWKPSRYFKVEALPLLGSGKLDLKGLKELALA 1143
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 472-913 9.15e-15

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: 79.82  E-value: 9.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLV-- 549
Cdd:cd05932    7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgk 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  550 ----DERAATLGESLgETRVLH--------------LERLPQSTGDLPAAnvaPGDLAYVIYTSGSTGMPKGVMVEHRSV 611
Cdd:cd05932   87 lddwKAMAPGVPEGL-ISISLPppsaancqyqwddlIAQHPPLEERPTRF---PEQLATLIYTSGTTGQPKGVMLTFGSF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  612 VNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAEKDPREMlrsiQRDAVTVIHFVPSMLTPF 691
Cdd:cd05932  163 AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDV----QRARPTLFFSVPRLWTKF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  692 ------------LDLLDGDP-----TARAAASSLRLVFC----SGEALAPLQVARFRRLFGdaVRLVNLYGPTEATvdVS 750
Cdd:cd05932  239 qqgvqdkipqqkLNLLLKIPvvnslVKRKVLKGLGLDQCrlagCGSAPVPPALLEWYRSLG--LNILEAYGMTENF--AY 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  751 DHECASDNPTRVPIGRPIDNLRLYVLDRalrpqplgavGELYIGGVGVARGYLNRPELNAERFLVDPFVaggrlyRTGDL 830
Cdd:cd05932  315 SHLNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFL------RTGDK 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  831 ARWLADGNLEYLGRADDQVKI-RGNRVEPDEVRDRLAALPGVRDAAVVARDSavrgTHLVGYYVAAAELDP-------GQ 902
Cdd:cd05932  379 GELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSGL----PAPLALVVLSEEARLradafarAE 454

                        490
                 ....*....|.
gi 15598523  903 LRAGLSATLPD 913
Cdd:cd05932  455 LEASLRAHLAR 465
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 8-340 3.56e-14

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: 77.35  E-value: 3.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    8 PLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRlrlgetdgTPYQWLDTDAEFEArhvd 87
Cdd:cd19547    3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILR--------TGFTWRDRAEPLQY---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   88 LRADRDPEAAVRSWL-RDAFRHAYPLD---------GRSLVDLALLH------SDQALYVYVRTHHIVSDAWGLQLFLSR 151
Cdd:cd19547   71 VRDDLAPPWALLDWSgEDPDRRAELLErlladdraaGLSLADCPLYRltlvrlGGGRHYLLWSHHHILLDGWCLSLIWGD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  152 VRAGY--LGELGEPQAQ--MPTASLLAQLETDDYSGSEQYRGDRAYFAEalegLEPALFTRRrPA---GLRRTARHRLT- 223
Cdd:cd19547  151 VFRVYeeLAHGREPQLSpcRPYRDYVRWIRARTAQSEESERFWREYLRD----LTPSPFSTA-PAdreGEFDTVVHEFPe 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  224 -LERTLLDAIRDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAA--KQVVGHFANTLPLRIRTAPEQTVDEF 300
Cdd:cd19547  226 qLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEgsEHMVGIFINTIPLRIRLDPDQTVTGL 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 15598523  301 LAQLREATRTLLRHQKMPLGDLLRGAS-------PLFDTTLSYMRWP 340
Cdd:cd19547  306 LETIHRDLATTAAHGHVPLAQIKSWASgerlsggRVFDNLVAFENYP 352
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 36-411 5.83e-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: 76.46  E-value: 5.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   36 RFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLDTDAE--FEARHVDLRAdrdpeaavrswlrdAFRHAYPLD 113
Cdd:cd19537   31 RLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPrvQRVDTLDVWK--------------EINRPFDLE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  114 GRSLVDLALLHSdqalYVYVRTHHIVSDAWGLQLFLSRVRAGYLGELGEPQ----------AQMPTASLLA----QLETD 179
Cdd:cd19537   97 REDPIRVFISPD----TLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVrreyldstawSRPASPEDLDfwseYLSGL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  180 DYSGSEQYRGDRAYfaealeglepalftrrrpAGLRRTARHRLTLERTLLDAIRDRGESPFLFLSAAVALYLARIHQNDD 259
Cdd:cd19537  173 PLLNLPRRTSSKSY------------------RGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  260 VVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQ--TVDEFLAQLREATRTLLRHqKMPLGDLLRGAS--------PL 329
Cdd:cd19537  235 IVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPSSSdaSAADFLRAVRRSSQAALAH-AIPWHQLLEHLGlppdspnhPL 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  330 FDTTLSYMRwpAAQAIPNASVETVaqthahdpDALAIWVS--------EFD--GHSDAQVDFEYACDVFDADFpMDAAAR 399
Cdd:cd19537  314 FDVMVTFHD--DRGVSLALPIPGV--------EPLYTWAEgakfplmfEFTalSDDSLLLRLEYDTDCFSEEE-IDRIES 382

                        410
                 ....*....|..
gi 15598523  400 HIETFLRALVEG 411
Cdd:cd19537  383 LILAALELLVEG 394
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 593-939 7.31e-14

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 76.98  E-value: 7.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   593 YTSGSTGMPKGVMVEHR-----SVVNRLNWMQRRYPigerdVLLQKTPVtFDVSVWELFWWsfTGARLSLLPPGAEKDPR 667
Cdd:PLN03102  193 YTSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCP-----VYLWTLPM-FHCNGWTFTWG--TAARGGTSVCMRHVTAP 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   668 EMLRSIQRDAVTVIHFVPsmlTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLfgdAVRLVNLYGPTEATV 747
Cdd:PLN03102  265 EIYKNIEMHNVTHMCCVP---TVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL---GFQVMHAYGLTEATG 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   748 DVSDHECaSDNPTRVPIGRPID--------NLRLYVLD----RALR--PQPLGAVGELYIGGVGVARGYLNRPELNAERF 813
Cdd:PLN03102  339 PVLFCEW-QDEWNRLPENQQMElkarqgvsILGLADVDvknkETQEsvPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   814 lvdpfvAGGRLyRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV 893
Cdd:PLN03102  418 ------KHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV 490

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523   894 -------AAAELDPGQLRAG-----LSATLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PLN03102  491 lekgettKEDRVDKLVTRERdlieyCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 585-878 7.43e-14

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: 76.76  E-value: 7.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  585 PGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGAE- 663
Cdd:cd05908  105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLf 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  664 -KDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARF-RRLFGDAVR---LVN 738
Cdd:cd05908  185 iRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFlDHMSKYGLKrnaILP 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  739 LYGPTEATVDVS------------------------------DHECAsdnpTRVPIGRPIDNLRLYVLDRALRPQPLGAV 788
Cdd:cd05908  265 VYGLAEASVGASlpkaqspfktitlgrrhvthgepepevdkkDSECL----TFVEVGKPIDETDIRICDEDNKILPDGYI 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  789 GELYIGGVGVARGYLNRPELNAERFLVDPFVaggrlyRTGDLArWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAAL 868
Cdd:cd05908  341 GHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEEL 413

                        330
                 ....*....|
gi 15598523  869 PGVRDAAVVA 878
Cdd:cd05908  414 EGVELGRVVA 423
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 473-939 8.16e-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: 76.74  E-value: 8.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  473 SYAELDAKVQAVADALR-AAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDE 551
Cdd:cd05928   43 SFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  552 RAATLGESLG------ETRVL----------HLERLPQSTGDLPAANVAPGDLAYVIY-TSGSTGMPKgvMVEHR----- 609
Cdd:cd05928  123 ELAPEVDSVAsecpslKTKLLvseksrdgwlNFKELLNEASTEHHCVETGSQEPMAIYfTSGTTGSPK--MAEHShsslg 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  610 --SVVNRLNWMQrrypIGERDVLLQKTPVTFDVSVW-ELF--WWSFTGARLSLLPpgaEKDPREMLRSIQRDAVTVIHFV 684
Cdd:cd05928  201 lgLKVNGRYWLD----LTASDIMWNTSDTGWIKSAWsSLFepWIQGACVFVHHLP---RFDPLVILKTLSSYPITTFCGA 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  685 PsmlTPFLDLLDGDPTaRAAASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEaTVDVsdheCASDNPTRVP- 763
Cdd:cd05928  274 P---TVYRMLVQQDLS-SYKFPSLQHCVTGGEPLNPEVLEKWKAQTG--LDIYEGYGQTE-TGLI----CANFKGMKIKp 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  764 --IGRPIDNLRLYVLDRALRPQPLGAVGELYI-----GGVGVARGYLNRPELNAERFLvdpfvagGRLYRTGDLARWLAD 836
Cdd:cd05928  343 gsMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIR-------GDFYLTGDRGIMDED 415

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  837 GNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAEL---DPGQLRAGL-----S 908
Cdd:cd05928  416 GYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFlshDPEQLTKELqqhvkS 495

                        490       500       510
                 ....*....|....*....|....*....|.
gi 15598523  909 ATLPdFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05928  496 VTAP-YKYPRKVEFVQELPKTVTGKIQRNEL 525
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 1493-1971 8.17e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 76.64  E-value: 8.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1493 ALAFEEQRWTYRDLDHVARCVATRLV-RAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETA 1571
Cdd:PRK07867   21 GLYFEDSFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1572 QPFRVVAHPEHAHVAAAE----RVLPVE-----ELVADI--EPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWAny 1640
Cdd:PRK07867  101 DCQLVLTESAHAELLDGLdpgvRVINVDspawaDELAAHrdAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA-- 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1641 tqwqlrvASGVP-----GLRTLQFAPLSFDMafqeiFST----------LCGGGELQLisnRERMDPSALLHVLER---- 1701
Cdd:PRK07867  179 -------SAGVMlaqrfGLGPDDVCYVSMPL-----FHSnavmagwavaLAAGASIAL---RRKFSASGFLPDVRRygat 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1702 ------RQVQRVLlpfVALQRLAEASNalgvrpgALRVVVSSGEQLRiteDVRAFcAAMPGLLLENQYGPTETHQVTYHS 1775
Cdd:PRK07867  244 yanyvgKPLSYVL---ATPERPDDADN-------PLRIVYGNEGAPG---DIARF-ARRFGCVVVDGFGSTEGGVAITRT 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1776 lsgdpahyPDLPP--IGRPLDGveVQVLDAA-LRPVPVGV------------TGELY-FGGDCLARGYHRAPKLTAERFv 1839
Cdd:PRK07867  310 --------PDTPPgaLGPLPPG--VAIVDPDtGTECPPAEdadgrllnadeaIGELVnTAGPGGFEGYYNDPEADAERM- 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1840 ehpwRPGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR-ERQGNDAFLA 1918
Cdd:PRK07867  379 ----RGG--VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILL----RYPDATEVAVYAVpDPVVGDQVMA 448

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15598523  1919 AFLLGEPEAVDLAELKQAL--RSELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 1971
Cdd:PRK07867  449 ALVLAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1984-2060 1.16e-13

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: 67.96  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1984 APRDDYERTLAGLLGELLDRP--RVGIRDSFF-DLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSA 2060
Cdd:COG0236    1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 472-853 1.97e-13

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 75.92  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   472 LSYAELDAKVQAVADALRAAGVRTDeRVALLVARGPHLLPAILGVQRAGGAYVPI-NPDHP--LERVRLLLEDCGARVVL 548
Cdd:PRK07769   56 LTWSQFGARNRAVGARLQQVTKPGD-RVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAIL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   549 VDERAAtlgESLGE----------TRVLHLERLPQSTGD-LPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNW 617
Cdd:PRK07769  135 TTTDSA---EGVRKffrarpakerPRVIAVDAVPDEVGAtWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQ 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   618 MQRRYPIGERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPGA-EKDPREMLRSIQR---DAVTVIHFVPSMltPF-L 692
Cdd:PRK07769  212 VIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAfVRRPGRWIRELARkpgGTGGTFSAAPNF--AFeH 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   693 DLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRlFGDAVRLVNL--------YGPTEATVDVSDH------------ 752
Cdd:PRK07769  290 AAARGLPKDGEPPLDLSNVKGLLNGSEPVSPASMRK-FNEAFAPYGLpptaikpsYGMAEATLFVSTTpmdeeptviyvd 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   753 ----------ECASDNPTRVP------IGRpiDNLRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERF--- 813
Cdd:PRK07769  369 rdelnagrfvEVPADAPNAVAqvsagkVGV--SEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqni 446

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 15598523   814 ---LVDPFVAGG-----RLYRTGDLARWLaDGNLEYLGRADDQVKIRG 853
Cdd:PRK07769  447 lksRLSESHAEGapddaLWVRTGDYGVYF-DGELYITGRVKDLVIIDG 493
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 458-877 2.89e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 75.22  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   458 TPQRTALLEADGG-TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVR 536
Cdd:PLN02860   18 TLRGNAVVTISGNrRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   537 LLLEDCGARVVLVDERAATLGESLGETR-----------------------VLHLERLPQSTGDLPAANV--APGDLAYV 591
Cdd:PLN02860   98 SAMLLVRPVMLVTDETCSSWYEELQNDRlpslmwqvflespsssvfiflnsFLTTEMLKQRALGTTELDYawAPDDAVLI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   592 IYTSGSTGMPKGVMVEHRSVVnrlnwMQRRYPI-----GERDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPpgaEKDP 666
Cdd:PLN02860  178 CFTSGTTGRPKGVTISHSALI-----VQSLAKIaivgyGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLP---KFDA 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   667 REMLRSIQRDAVTVIHFVPSMLTpflDLLDGDPTA--RAAASSLRLVFCSGEALAPLQVARFRRLFGDAvRLVNLYGPTE 744
Cdd:PLN02860  250 KAALQAIKQHNVTSMITVPAMMA---DLISLTRKSmtWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNA-KLFSAYGMTE 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   745 A---------------TVDVSDHECASDNPTRVP------IGRPIDNLRLYV-LDRALRpqplgaVGELYIGGVGVARGY 802
Cdd:PLN02860  326 AcssltfmtlhdptleSPKQTLQTVNQTKSSSVHqpqgvcVGKPAPHVELKIgLDESSR------VGRILTRGPHVMLGY 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523   803 LNRPELNAERFLVDPFVAggrlyrTGDLArWLAD-GNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVV 877
Cdd:PLN02860  400 WGQNSETASVLSNDGWLD------TGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV 468
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 472-937 3.16e-13

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 75.16  E-value: 3.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   472 LSYAELDAKVQAVADALRAAGVRTDeRVALLVARGPHLLPAILGVQRAGGAYVPI-NPDHP--LERVRLLLEDCGARVVL 548
Cdd:PRK12476   69 LTWTQLGVRLRAVGARLQQVAGPGD-RVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   549 VDERAATLGES-------LGETRVLHLERLPQSTG-DLPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNrlNWMQR 620
Cdd:PRK12476  148 TTTAAAEAVEGflrnlprLRRPRVIAIDAIPDSAGeSFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGT--NLVQM 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   621 RYPIGERDVLLQKT---PVTFDVSVWELFWWSFTGARLSLLPPGA-EKDPREMLR--SIQRDAVTVIHFVPSM------- 687
Cdd:PRK12476  226 ILSIDLLDRNTHGVswlPLYHDMGLSMIGFPAVYGGHSTLMSPTAfVRRPQRWIKalSEGSRTGRVVTAAPNFayewaaq 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   688 --LTPFLDLLD---------GDPTARAAASSLRlvfcsgEALAPLQVAR--FRRLFG--DAVRLVNLYGP-TEATVDVSD 751
Cdd:PRK12476  306 rgLPAEGDDIDlsnvvliigSEPVSIDAVTTFN------KAFAPYGLPRtaFKPSYGiaEATLFVATIAPdAEPSVVYLD 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   752 HE---------CASDNPTRVP---IGRPIDNLRLYVLDRAL-RPQPLGAVGELYIGGVGVARGYLNRPELNAERF---LV 815
Cdd:PRK12476  380 REqlgagravrVAADAPNAVAhvsCGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgakLQ 459

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   816 DPFVAG---------GRLYRTGDLARWLaDGNLEYLGRADDQVKIRGNRVEPDEVRDRLA-ALPGVRDAAVVARD-SAVR 884
Cdd:PRK12476  460 SRLAEGshadgaaddGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAeASPMVRRGYVTAFTvPAED 538

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598523   885 GTHLVgyYVA-----AAELDPGQ----LRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRR 937
Cdd:PRK12476  539 NERLV--IVAeraagTSRADPAPaidaIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARR 598
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 1463-1950 3.28e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 74.98  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1463 PRRDAASQP-EPLvdvvSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIAT 1541
Cdd:PRK08162    9 DRNAANYVPlTPL----SFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1542 IWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVA-AAERVLPV------------------------EE 1596
Cdd:PRK08162   85 HFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVArEALALLPGpkplvidvddpeypggrfigaldyEA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1597 LVADIEPETFAAPQLDEL-AMLL-FTSGSTGRPKGVELSHRMWAnytqwqLRVASGVpglrtlqfapLSFDMAFQEIF-S 1673
Cdd:PRK08162  165 FLASGDPDFAWTLPADEWdAIALnYTSGTTGNPKGVVYHHRGAY------LNALSNI----------LAWGMPKHPVYlW 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1674 TL----CGGGelqliSNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNAlgvrPGALRVVVSSGEQLR--ITEDV 1747
Cdd:PRK08162  229 TLpmfhCNGW-----CFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGA----PIVLSALINAPAEWRagIDHPV 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1748 RAFCAAMP------------GLLLENQYGPTETHQVTyhSLSGDPAHYPDLPPIGRP----LDGV------EVQVLDAA- 1804
Cdd:PRK08162  300 HAMVAGAAppaaviakmeeiGFDLTHVYGLTETYGPA--TVCAWQPEWDALPLDERAqlkaRQGVryplqeGVTVLDPDt 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1805 LRPVPV-GVT-GELYFGGDCLARGYHRAPKLTAERFvEHPWrpgarlYRTGDLGRILGNGEIvwlgradtQVKVR----- 1877
Cdd:PRK08162  378 MQPVPAdGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGW------FHTGDLAVLHPDGYI--------KIKDRskdii 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1878 ---GFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGND--AFLAaflLGEPEAVDLAELKQALRSELPEHMVPAHF 1950
Cdd:PRK08162  443 isgGENISSIEVEDVLY----RHPAVLVAAVVAKpdPKWGEVpcAFVE---LKDGASATEEEIIAHCREHLAGFKVPKAV 515
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1790-1972 3.38e-13

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 73.54  E-value: 3.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1790 GRPLDGVEVQVLDaalrpvpvgvtGELYFGGDCLARGYHRAPKLTAerFVEHPWrpgarlYRTGDLGrILGNGEIVWLGR 1869
Cdd:PRK07824  195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVDPDP--FAEPGW------FRTDDLG-ALDDGVLTVLGR 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1870 ADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNdAFLAAFLLGEPEAVDLAELKQALRSELPEHMVP 1947
Cdd:PRK07824  255 ADDAISTGGLTVLPQVVEAALA----THPAVADCAVfgLPDDRLGQ-RVVAAVVGDGGPAPTLEALRAHVARTLDRTAAP 329

                         170       180
                  ....*....|....*....|....*
gi 15598523  1948 AHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:PRK07824  330 RELHVVDELPRRGIGKVDRRALVRR 354
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 431-833 3.86e-13

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 74.92  E-value: 3.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   431 IHTRNATDQAfPEQATLPTLFAEQVARTPQRTALLEADGG----TLSYAELDAKVQAVADALRAAGVRTDERVALLVARG 506
Cdd:PRK08180   26 IYLRSAEPLG-DYPRRLTDRLVHWAQEAPDRVFLAERGADggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNS 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   507 P-HLLPAiLGVQRAGGAYVPINP-----DHPLERVRLLLEDCGARVVLVDERAA----------------TLGESLGETR 564
Cdd:PRK08180  105 IeHALLA-LAAMYAGVPYAPVSPayslvSQDFGKLRHVLELLTPGLVFADDGAAfaralaavvpadvevvAVRGAVPGRA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   565 VLHLERL--PQSTGDLPAAN--VAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPigerdVLLQKTPVTFDv 640
Cdd:PRK08180  184 ATPFAALlaTPPTAAVDAAHaaVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFP-----FLAEEPPVLVD- 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   641 svwelfW--WSFT-GARLSL-----------------LPPGAEkdprEMLRSIqRDAVTVIHF-VPS---MLTPFldlLD 696
Cdd:PRK08180  258 ------WlpWNHTfGGNHNLgivlynggtlyiddgkpTPGGFD----ETLRNL-REISPTVYFnVPKgweMLVPA---LE 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   697 GDPT-ARAAASSLRLVFCSGEALAPLQVARFRRL----FGDAVRLVNLYGPTEATVDVSDheCASDNPTRVPIGRPIDNL 771
Cdd:PRK08180  324 RDAAlRRRFFSRLKLLFYAGAALSQDVWDRLDRVaeatCGERIRMMTGLGMTETAPSATF--TTGPLSRAGNIGLPAPGC 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598523   772 rlyvldrALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARW 833
Cdd:PRK08180  402 -------EVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1775-2063 4.26e-13

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 72.48  E-value: 4.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1775 SLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEH--PWRPGARLYRT 1852
Cdd:COG3433    2 AIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPfiPVPYPAQPGRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1853 GDLGRILGNGEIVWLGRADTQVKVRGFRIEPaEVELAIMRQAERQPGLRGAAVVARERQGNDAFLAAfLLGEPEAVDLAE 1932
Cdd:COG3433   82 ADDLRLLLRRGLGPGGGLERLVQQVVIRAER-GEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIV-GAVAALDGLAAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1933 LKQALRSELPEHMVPAHFAW-VDGFALTPSGKRDDAALRALPLEHGTNIEYLAPRDDYERTLAGL---LGELLDRP--RV 2006
Cdd:COG3433  160 AALAALDKVPPDVVAASAVVaLDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEEELradVAELLGVDpeEI 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523 2007 GIRDSFFDLGGTSLSAMRFMLLIEKRyGVDLPMAALIETPTVEGLAERLRERSAVRA 2063
Cdd:COG3433  240 DPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 451-950 5.17e-13

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: 74.61  E-value: 5.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  451 FAEQV---ARTPQRTALLEADGGT---LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYV 524
Cdd:cd05943   72 YAENLlrhADADDPAAIYAAEDGErteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWS 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  525 PINPD------------------------------HP-LERVRLL---LEDCGARVVLVDERAATLGESLGETRVLHLER 570
Cdd:cd05943  152 SCSPDfgvpgvldrfgqiepkvlfavdaytyngkrHDvREKVAELvkgLPSLLAVVVVPYTVAAGQPDLSKIAKALTLED 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  571 L--PQSTGDLPAANVAPGDLAYVIYTSGSTGMPK-------GVMVEHRSVVnRLNWmqrryPIGERDVLLQKTPVTfdvs 641
Cdd:cd05943  232 FlaTGAAGELEFEPLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEH-ILHC-----DLRPGDRLFYYTTCG---- 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  642 vWELfwWSF------TGARLSLL--PPGAeKDPREMLRSIQRDAVTVihFVPSmlTPFLDLL---DGDPTARAAASSLRL 710
Cdd:cd05943  302 -WMM--WNWlvsglaVGATIVLYdgSPFY-PDTNALWDLADEEGITV--FGTS--AKYLDALekaGLKPAETHDLSSLRT 373

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  711 VFCSGEALAPLQVARFRRLFGDAVRLVNLYGPTeatvDVSdhEC-ASDNPTrVPIGR-----PIDNLRLYVLDRALRPQP 784
Cdd:cd05943  374 ILSTGSPLKPESFDYVYDHIKPDVLLASISGGT----DII--SCfVGGNPL-LPVYRgeiqcRGLGMAVEAFDEEGKPVW 446

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  785 lGAVGELYIggvgvARGYLNRPelnaERFLVDPfvaGGRLYRT------------GDLARWLADGNLEYLGRADDQVKIR 852
Cdd:cd05943  447 -GEKGELVC-----TKPFPSMP----VGFWNDP---DGSRYRAayfakypgvwahGDWIEITPRGGVVILGRSDGTLNPG 513

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  853 GNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAA--AELDP-------GQLRAGLSatlPDFmLPAFFVRI 923
Cdd:cd05943  514 GVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLRegVELDDelrkrirSTIRSALS---PRH-VPAKIIAV 589

                        570       580       590
                 ....*....|....*....|....*....|....
gi 15598523  924 DSLPLSANGKldRRQLP-------APPEQVAAVA 950
Cdd:cd05943  590 PDIPRTLSGK--KVEVAvkkiiagRPVKNAGALA 621
PLN02479 PLN02479
acetate-CoA ligase
 445-949 5.20e-13

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 74.50  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   445 ATLPTLFAEQVART-PQRTALLEadgGTLSYAELDA--KVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGG 521
Cdd:PLN02479   19 ALTPLWFLERAAVVhPTRKSVVH---GSVRYTWAQTyqRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   522 AYVPINPDHPLERVRLLLEDCGARVVLVDERAATLGE----------------------------------SLGETRVLH 567
Cdd:PLN02479   96 VVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEealkilaekkkssfkppllivigdptcdpkslqyALGKGAIEY 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   568 LERLpqSTGDLPAANVAPGDLAYVI---YTSGSTGMPKGVMVEHR-----SVVNRLNWmqrryPIGERDVLLQKTPVtFD 639
Cdd:PLN02479  176 EKFL--ETGDPEFAWKPPADEWQSIalgYTSGTTASPKGVVLHHRgaylmALSNALIW-----GMNEGAVYLWTLPM-FH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   640 VSVWeLFWWS---FTGARLSLLPPGAekdpREMLRSIQRDAVTviHFVPSMLTpfLDLLDGDPTARAAASSLRL--VFCS 714
Cdd:PLN02479  248 CNGW-CFTWTlaaLCGTNICLRQVTA----KAIYSAIANYGVT--HFCAAPVV--LNTIVNAPKSETILPLPRVvhVMTA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   715 GEALAPLQVARFRRLfgdAVRLVNLYGPTE----ATVdvsdheCA-SDNPTRVPigrPIDNLRL-------YV----LD- 777
Cdd:PLN02479  319 GAAPPPSVLFAMSEK---GFRVTHTYGLSEtygpSTV------CAwKPEWDSLP---PEEQARLnarqgvrYIglegLDv 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   778 ---RALRPQPL--GAVGELYIGGVGVARGYLNRPELNAERFlvdpfvAGGrLYRTGDLARWLADGNLEYLGRADDQVKIR 852
Cdd:PLN02479  387 vdtKTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF------ANG-WFHSGDLGVKHPDGYIEIKDRSKDIIISG 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   853 GNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLvgyyVAAAELDPGQLRAGLSATLPDFM------LPAFFVR---- 922
Cdd:PLN02479  460 GENISSLEVENVVYTHPAVLEASVVARPDERWGESP----CAFVTLKPGVDKSDEAALAEDIMkfcrerLPAYWVPksvv 535

                         570       580
                  ....*....|....*....|....*..
gi 15598523   923 IDSLPLSANGKLDRRQLPAPPEQVAAV 949
Cdd:PLN02479  536 FGPLPKTATGKIQKHVLRAKAKEMGPV 562
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 1482-1963 5.28e-13

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: 74.52  E-value: 5.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1482 ERQVEALPGSAALAFE------EQRWTYRDL-DHVARCvATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVP 1554
Cdd:cd05966   60 DRHLKERGDKVAIIWEgdepdqSRTITYRELlREVCRF-ANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1555 LDVSYPAQRLA---------LILETAQPFR-------------------------VVAHPEHAHVAAAERVLPVEELVAD 1600
Cdd:cd05966  139 VFAGFSAESLAdrindaqckLVITADGGYRggkviplkeivdealekcpsvekvlVVKRTGGEVPMTEGRDLWWHDLMAK 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1601 IEPETFAAPqLDELAML--LFTSGSTGRPKGVELSHRMWANYTQwqlrvasgvpglRTLQFAplsFDMAFQEIF------ 1672
Cdd:cd05966  219 QSPECEPEW-MDSEDPLfiLYTSGSTGKPKGVVHTTGGYLLYAA------------TTFKYV---FDYHPDDIYwctadi 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1673 ------STLCGG----GELQLIsnRERM----DPSALLHVLERRQVqrvllpfvalqrlaeasNALGVRPGALRVVVSSG 1738
Cdd:cd05966  283 gwitghSYIVYGplanGATTVM--FEGTptypDPGRYWDIVEKHKV-----------------TIFYTAPTAIRALMKFG 343

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1739 EQ---------LRITEDV------RAF-----------CAAMpgllleNQYGPTET--HQVTyhslsgdpaHYPDLPPI- 1789
Cdd:cd05966  344 DEwvkkhdlssLRVLGSVgepinpEAWmwyyevigkerCPIV------DTWWQTETggIMIT---------PLPGATPLk 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1790 ----GRPLDGVEVQVLDAALRPVPVGVTGELYF-----GgdcLARGYHRAPkltaERFVEHPWRPGARLYRTGDLGRILG 1860
Cdd:cd05966  409 pgsaTRPFFGIEPAILDEEGNEVEGEVEGYLVIkrpwpG---MARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDE 481

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1861 NGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGNdaFLAAFLL---GEPEAVDLA-ELK 1934
Cdd:cd05966  482 DGYYWITGRVDDVINVSGHRLGTAEVESALV----AHPAVAEAAVVGRphDIKGE--AIYAFVTlkdGEEPSDELRkELR 555

                        570       580
                 ....*....|....*....|....*....
gi 15598523 1935 QALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:cd05966  556 KHVRKEIGPIATPDKIQFVPGLPKTRSGK 584
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 1499-1928 7.38e-13

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: 74.00  E-value: 7.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1499 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIatiWGILRA---GLVCVPLDVSYPAQRLALILETAQPFR 1575
Cdd:cd17641   10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWV---WAELAAqaiGALSLGIYQDSMAEEVAYLLNYTGARV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1576 VVAHPE-------------------------------HAHVAAAERVLPVEELVADIEPETF----AAPQLDELAMLLFT 1620
Cdd:cd17641   87 VIAEDEeqvdklleiadripsvryviycdprgmrkydDPRLISFEDVVALGRALDRRDPGLYerevAAGKGEDVAVLCTT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1621 SGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMafQEIFST----LCGGG----------------- 1679
Cdd:cd17641  167 SGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIG--EQMYSVgqalVCGFIvnfpeepetmmedlrei 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1680 ------------ELQLISNRERMDPS-------------ALLHVLERRQVQRVLLPFVALQR-LAEA------SNALGVR 1727
Cdd:cd17641  245 gptfvllpprvwEGIAADVRARMMDAtpfkrfmfelgmkLGLRALDRGKRGRPVSLWLRLASwLADAllfrplRDRLGFS 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1728 pgALRVVVSSGEQLriTEDVRAFCAAMpGLLLENQYGPTETHQV-TYHslsgdPAHYPDLPPIGRPLDGVEVQVLDaalr 1806
Cdd:cd17641  325 --RLRSAATGGAAL--GPDTFRFFHAI-GVPLKQLYGQTELAGAyTVH-----RDGDVDPDTVGVPFPGTEVRIDE---- 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1807 pvpvgvTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRA-DTQVKVRGFRIEPAE 1885
Cdd:cd17641  391 ------VGEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQF 458

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 15598523 1886 VElaimRQAERQPGLRGAAVVARERQgndaFLAAFLLGEPEAV 1928
Cdd:cd17641  459 IE----NKLKFSPYIAEAVVLGAGRP----YLTAFICIDYAIV 493
PLN02246 PLN02246
4-coumarate--CoA ligase
 1502-1908 1.14e-12

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 73.09  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1502 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA----------LILETA 1571
Cdd:PLN02246   52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAkqakasgaklIITQSC 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1572 QPFRVVAHPEHAHV------AAAERVLPVEELVADIE---PETFAAPqlDELAMLLFTSGSTGRPKGVELSHR-MWANYT 1641
Cdd:PLN02246  132 YVDKLKGLAEDDGVtvvtidDPPEGCLHFSELTQADEnelPEVEISP--DDVVALPYSSGTTGLPKGVMLTHKgLVTSVA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1642 QwqlRVASGVPGL------RTLQFAPLsfdmaFQeIFS----TLCG---GGELQLISnreRMDPSALLHVLERRQVqrVL 1708
Cdd:PLN02246  210 Q---QVDGENPNLyfhsddVILCVLPM-----FH-IYSlnsvLLCGlrvGAAILIMP---KFEIGALLELIQRHKV--TI 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1709 LPFVALQRLAEASNALGVRP--GALRVVVSS----GEQLritEDvrAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAH 1782
Cdd:PLN02246  276 APFVPPIVLAIAKSPVVEKYdlSSIRMVLSGaaplGKEL---ED--AFRAKLPNAVLGQGYGMTEAGPVLAMCLAFAKEP 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1783 YPDLP-PIGRPLDGVEVQVLD----AALrpvPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGR 1857
Cdd:PLN02246  351 FPVKSgSCGTVVRNAELKIVDpetgASL---PRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW------LHTGDIGY 421

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15598523  1858 ILGNGEIVWLGRADTQVKVRGFRIEPAEVE-LAImrqaeRQPGLRGAAVVAR 1908
Cdd:PLN02246  422 IDDDDELFIVDRLKELIKYKGFQVAPAELEaLLI-----SHPSIADAAVVPM 468
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 1502-1859 1.49e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 73.16  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1502 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPA-----QRLALILETAQPFRV 1576
Cdd:PRK12582   82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1577 VAH----------------PEHAHVAAA---ERVLPVEELVA-----DIEpETFAAPQLDELAMLLFTSGSTGRPKGVEL 1632
Cdd:PRK12582  162 FAQsgapfaralaaldlldVTVVHVTGPgegIASIAFADLAAtpptaAVA-AAIAAITPDTVAKYLFTSGSTGMPKAVIN 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1633 SHRMWANYTQWQLRVASGVPGLR---TLQFAPLSFDMAFQEIFS-TLCGGGELQL-------------ISNRERMDP--- 1692
Cdd:PRK12582  241 TQRMMCANIAMQEQLRPREPDPPppvSLDWMPWNHTMGGNANFNgLLWGGGTLYIddgkplpgmfeetIRNLREISPtvy 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1693 -------SALLHVLERRQVQRVLLpFVALQRLA-----------EASNALGVRPGALRVVVSSGeqlritedvrafcaam 1754
Cdd:PRK12582  321 gnvpagyAMLAEAMEKDDALRRSF-FKNLRLMAyggatlsddlyERMQALAVRTTGHRIPFYTG---------------- 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1755 pglllenqYGPTETHQVTYhslsgdPAHYPDLPP--IGRPLDGVEVQVldaalrpVPVGVTGELYFGGDCLARGYHRAPK 1832
Cdd:PRK12582  384 --------YGATETAPTTT------GTHWDTERVglIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPE 442

                         410       420
                  ....*....|....*....|....*..
gi 15598523  1833 LTAERFVEHPWrpgarlYRTGDLGRIL 1859
Cdd:PRK12582  443 LTAAAFDEEGF------YRLGDAARFV 463
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 473-939 2.38e-12

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 72.09  E-value: 2.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   473 SYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDER 552
Cdd:PRK06018   41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   553 AATLGESLGEtRVLHLER---------LPQST---------------GDLPAANVAPGDLAYVIYTSGSTGMPKGVMVEH 608
Cdd:PRK06018  121 FVPILEKIAD-KLPSVERyvvltdaahMPQTTlknavayeewiaeadGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSH 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   609 RSvvNRLNWMQRRYP----IGERDVLLQKTPVtFDVSVWEL-FWWSFTGARLSLlpPGAEKDPREMLRSIQRDAVTVIHF 683
Cdd:PRK06018  200 RS--NVLHALMANNGdalgTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVM--PGAKLDGASVYELLDTEKVTFTAG 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   684 VPsmlTPFLDLLDGDPTARAAASSLRLVFCSGEALAPLQVARFRRLfgdAVRLVNLYGPTE----ATVDV-----SDHEC 754
Cdd:PRK06018  275 VP---TVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM---GVEVRHAWGMTEmsplGTLAAlkppfSKLPG 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   755 ASDNPTRVPIGRPIDNLRLYVLDRALRPQPLG--AVGELYIGGVGVARGYLnrpELNAERFLVDPFvaggrlYRTGDLAR 832
Cdd:PRK06018  349 DARLDVLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYY---RVDGEILDDDGF------FDTGDVAT 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   833 WLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVvardsavrgthlVGYYVAAAELDP---GQLRAGLSA 909
Cdd:PRK06018  420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV------------IGVYHPKWDERPlliVQLKPGETA 487

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 15598523   910 T---LPDFM--------LPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PRK06018  488 TreeILKYMdgkiakwwMPDDVAFVDAIPHTATGKILKTAL 528
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
1510-1976 2.76e-12

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 71.72  E-value: 2.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1510 ARCVATRLVRAGarRGDAIGVALNRSPEMIATIWGILRAG--LVCVPLDV-SYPAQRLALilETAQPF------RVVAHP 1580
Cdd:PRK05851   41 AENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGaaVSILPGPVrGADDGRWAD--ATLTRFagigvrTVLSHG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1581 EH-AHVAAAERVLPVEELV---ADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELS-HRMWANYTQWQLRVASGVPGLR 1655
Cdd:PRK05851  117 SHlERLRAVDSSVTVHDLAtaaHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSpGAVLSNLRGLNARVGLDAATDV 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1656 TLQFAPLSFDMAFQEIFSTLCGGGELQLI-SNRERMDPSALLHVLERRQVQRVLLPFVALQRLAE-ASNALGVRPGALRV 1733
Cdd:PRK05851  197 GCSWLPLYHDMGLAFLLTAALAGAPLWLApTTAFSASPFRWLSWLSDSRATLTAAPNFAYNLIGKyARRVSDVDLGALRV 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1734 VVSSGEQLRItEDVRAFCAAM------PGLLLENqYGPTE-THQVTY----HSLSGDPAHYPD------LPPIGRPLDGV 1796
Cdd:PRK05851  277 ALNGGEPVDC-DGFERFATAMapfgfdAGAAAPS-YGLAEsTCAVTVpvpgIGLRVDEVTTDDgsgarrHAVLGNPIPGM 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1797 EVQVldaALRPVPVGVT----GELYFGGDCLARGYhrapkltaerFVEHPWRPGArLYRTGDLGrILGNGEIVWLGRADT 1872
Cdd:PRK05851  355 EVRI---SPGDGAAGVAgreiGEIEIRGASMMSGY----------LGQAPIDPDD-WFPTGDLG-YLVDGGLVVCGRAKE 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1873 QVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARERQGNDA----FLAAFLLGEPEAVDLAELKQALRSELpeHMVPA 1948
Cdd:PRK05851  420 LITVAGRNIFPTEIE----RVAAQVRGVREGAVVAVGTGEGSArpglVIAAEFRGPDEAGARSEVVQRVASEC--GVVPS 493

                         490       500       510
                  ....*....|....*....|....*....|
gi 15598523  1949 HFAWVDGFAL--TPSGKrddaaLRALPLEH 1976
Cdd:PRK05851  494 DVVFVAPGSLprTSSGK-----LRRLAVKR 518
PRK07529 PRK07529
AMP-binding domain protein; Validated
 1488-1972 4.07e-12

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 71.52  E-value: 4.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1488 LPGSAALAfEEQRWTYRDL-DHVARCvATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCvPLDVSYPAQRLAL 1566
Cdd:PRK07529   47 LLDADPLD-RPETWTYAELlADVTRT-ANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1567 ILE--------TAQPF----------RVVAH-PEHAHVA----------------------AAERVLPVEELVA---DIE 1602
Cdd:PRK07529  124 LLRaagakvlvTLGPFpgtdiwqkvaEVLAAlPELRTVVevdlarylpgpkrlavplirrkAHARILDFDAELArqpGDR 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1603 PETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANytQWQLRVASGVPGLRTLQFA-PLsFDM--AFQEIFSTLCGG 1678
Cdd:PRK07529  204 LFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGnEVAN--AWLGALLLGLGPGDTVFCGlPL-FHVnaLLVTGLAPLARG 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1679 GELQLISNRERMDPSALLH---VLERRQVQR-VLLPFV---ALQRLAEASNAlgvrpGALRVVVSSGEQLRItEDVRAFC 1751
Cdd:PRK07529  281 AHVVLATPQGYRGPGVIANfwkIVERYRINFlSGVPTVyaaLLQVPVDGHDI-----SSLRYALCGAAPLPV-EVFRRFE 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1752 AAMpGLLLENQYGPTETHQVtyHSLSgdpahYPDLPP----IGRPLDGVEVQVL-----DAALRPVPVGVTGELYFGGDC 1822
Cdd:PRK07529  355 AAT-GVRIVEGYGLTEATCV--SSVN-----PPDGERrigsVGLRLPYQRVRVVilddaGRYLRDCAVDEVGVLCIAGPN 426

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1823 LARGYHRAPKltaerfvEHPWRPGARLYRTGDLGRILGNGeIVWL-GRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLR 1901
Cdd:PRK07529  427 VFSGYLEAAH-------NKGLWLEDGWLNTGDLGRIDADG-YFWLtGRAKDLIIRGGHNIDPAAIEEALL----RHPAVA 494

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1902 GAAVVARErqgnDAF-----LAAFLLGEPEAVDLAELKQALRSELPEHM-VPAHFAWVDGFALTPSGK------RDDAAL 1969
Cdd:PRK07529  495 LAAAVGRP----DAHagelpVAYVQLKPGASATEAELLAFARDHIAERAaVPKHVRILDALPKTAVGKifkpalRRDAIR 570


                  ...
gi 15598523  1970 RAL 1972
Cdd:PRK07529  571 RVL 573
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 1472-1927 4.56e-12

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 71.41  E-value: 4.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1472 EPLVDVVS-LFERQveALPGSAAL--AFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILR 1547
Cdd:PLN02574   37 DPNLDAVSfIFSHH--NHNGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1548 AGLVCVPLD-VSYPAQRLALILETA--------------QPFR--VVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQ 1610
Cdd:PLN02574  115 LGGIVTTMNpSSSLGEIKKRVVDCSvglaftspenveklSPLGvpVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1611 L--DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGV---PGLRTLQFAPLS-FDMAFQEIFSTlcggGELQLI 1684
Cdd:PLN02574  195 IkqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQyeyPGSDNVYLAALPmFHIYGLSLFVV----GLLSLG 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1685 SN---RERMDPSALLHVLERRQVQRvlLPFVA--LQRLAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLL 1759
Cdd:PLN02574  271 STivvMRRFDASDMVKVIDRFKVTH--FPVVPpiLMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDF 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1760 ENQYGPTETHQVTYHSLSGDpaHYPDLPPIGRPLDGVEVQVLD---AALrpVPVGVTGELYFGGDCLARGYHRAPKLTAE 1836
Cdd:PLN02574  349 IQGYGMTESTAVGTRGFNTE--KLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQS 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1837 RFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAF 1916
Cdd:PLN02574  425 TIDKDGW------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLI----SHPEIIDAAVTAVPDKECGEI 494

                         490
                  ....*....|.
gi 15598523  1917 LAAFLLGEPEA 1927
Cdd:PLN02574  495 PVAFVVRRQGS 505
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 454-939 5.11e-12

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: 71.44  E-value: 5.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  454 QVARTPQRTALL-EADGG----TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPI-- 526
Cdd:cd05966   62 HLKERGDKVAIIwEGDEPdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfa 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  527 --NPDHPLERVrlllEDCGARVVL-----------------VDErAATLGESLgeTRVLHLERL---------------- 571
Cdd:cd05966  142 gfSAESLADRI----NDAQCKLVItadggyrggkviplkeiVDE-ALEKCPSV--EKVLVVKRTggevpmtegrdlwwhd 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  572 --PQSTGDLPAANVAPGDLAYVIYTSGSTGMPKGVMveHrSVVNRLNW--MQRRYpigerdvllqktpvTFDVSVWELFW 647
Cdd:cd05966  215 lmAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVV--H-TTGGYLLYaaTTFKY--------------VFDYHPDDIYW 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  648 ------WsFTGARLSLLPP---GAEK----------DPREMLRSIQRDAVTVIHFVPS---MLTPFLDlldgDPTARAAA 705
Cdd:cd05966  278 ctadigW-ITGHSYIVYGPlanGATTvmfegtptypDPGRYWDIVEKHKVTIFYTAPTairALMKFGD----EWVKKHDL 352

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  706 SSLRLVFCSGEALAPLQVARFRRLFGDA-VRLVNLYGPTEatvdvSDHECASDNPTRVPI-----GRPIDNLRLYVLDRA 779
Cdd:cd05966  353 SSLRVLGSVGEPINPEAWMWYYEVIGKErCPIVDTWWQTE-----TGGIMITPLPGATPLkpgsaTRPFFGIEPAILDEE 427

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  780 LRPQPLGAVGELYIGGV--GVARGYLNRPElnaeRFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVE 857
Cdd:cd05966  428 GNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLG 503

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  858 PDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV-----AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANG 932
Cdd:cd05966  504 TAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdgeEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSG 583


                 ....*..
gi 15598523  933 KLDRRQL 939
Cdd:cd05966  584 KIMRRIL 590
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1052-1337 5.80e-12

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: 70.18  E-value: 5.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1052 TSRLSLG---LLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSF-DLSGASEPLQLVHtqARSeP 1127
Cdd:cd19532    1 TEPMSFGqsrFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVL--ASS-P 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1128 LILdlrgnpEAGTVLDEHIRQRRF-----HRYSLQQPGLFLFAAFVREDGL-DLVFSFHHAILDGWSVANLIVALVAAYR 1201
Cdd:cd19532   78 LRL------EHVQISDEAEVEEEFerlknHVYDLESGETMRIVLLSLSPTEhYLIFGYHHIAMDGVSFQIFLRDLERAYN 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1202 GEPLPGPA---PALACHVREELAALASPAAVGYWTG----------LLEGAR-MTR--LDGFGAHEpqaaqgpASHReaL 1265
Cdd:cd19532  152 GQPLLPPPlqyLDFAARQRQDYESGALDEDLAYWKSefstlpeplpLLPFAKvKSRppLTRYDTHT-------AERR--L 222

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523 1266 PDGLLERLKATAAQrglpLKS----LLLAA-HCLtLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEI 1337
Cdd:cd19532  223 DAALAARIKEASRK----LRVtpfhFYLAAlQVL-LARLLDVDDICIGIADANRTD-EDFMETIGFFLNLLPLRFRR 293
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 1488-1906 6.80e-12

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: 70.63  E-value: 6.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1488 LPGSAAL--AFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA 1565
Cdd:cd17642   30 VPGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1566 LILETAQPFRVVAHPEhahvaAAERVLPVEELVADIEP----------------ETF-----------------AAPQLD 1612
Cdd:cd17642  110 HSLNISKPTIVFCSKK-----GLQKVLNVQKKLKIIKTiiildskedykgyqclYTFitqnlppgfneydfkppSFDRDE 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1613 ELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASG---VPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISnreR 1689
Cdd:cd17642  185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGnqiIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMY---K 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1690 MDPSALLHVLERRQVQRVLL-----PFVALQRLAEA---SNalgvrpgaLRVVVSSGEQL-RITEDVRAFCAAMPGllLE 1760
Cdd:cd17642  262 FEEELFLRSLQDYKVQSALLvptlfAFFAKSTLVDKydlSN--------LHEIASGGAPLsKEVGEAVAKRFKLPG--IR 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1761 NQYGPTETHQVTYHSLSGDpahypDLP-PIGRPLDGVEVQVLDAAL-RPVPVGVTGELYFGGDCLARGYHRAPKLTAERF 1838
Cdd:cd17642  332 QGYGLTETTSAILITPEGD-----DKPgAVGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKALI 406

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523 1839 VEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRQaerQPGLRGAAVV 1906
Cdd:cd17642  407 DKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELE-SILLQ---HPKIFDAGVA 464
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 1473-1907 9.63e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 70.54  E-value: 9.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1473 PLVDVVSLFERQVEALPGSAAlafeeqrwtYRDLDHVA------------------RCVATRLVRAgARRGDAIGVALNR 1534
Cdd:PRK12476   32 PGTTLISLIERNIANVGDTVA---------YRYLDHSHsaagcaveltwtqlgvrlRAVGARLQQV-AGPGDRVAILAPQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1535 SPEMIATIWGILRAGLVCVPL---DVSYPAQRLALILETAQPFRV-----VAHPEHAHVAA-----AERVLPVEElVADI 1601
Cdd:PRK12476  102 GIDYVAGFFAAIKAGTIAVPLfapELPGHAERLDTALRDAEPTVVltttaAAEAVEGFLRNlprlrRPRVIAIDA-IPDS 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1602 EPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEI-FSTLCg 1677
Cdd:PRK12476  181 AGESFVPVELdtDDVSHLQYTSGSTRPPVGVEITHRaVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIgFPAVY- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1678 GGELQLisnrerMDPSALLhvleRRqvqrvllPFVALQRLAEAS---NALGVRP------GALRVVVSSGEQLRIT---- 1744
Cdd:PRK12476  260 GGHSTL------MSPTAFV----RR-------PQRWIKALSEGSrtgRVVTAAPnfayewAAQRGLPAEGDDIDLSnvvl 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1745 ---------EDVRAFCAA-----MPGLLLENQYG------------PTETHQVTY---------HSLSGDPAHyPDLPP- 1788
Cdd:PRK12476  323 iigsepvsiDAVTTFNKAfapygLPRTAFKPSYGiaeatlfvatiaPDAEPSVVYldreqlgagRAVRVAADA-PNAVAh 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1789 -----IGRPLDGVEVQvlDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFV----------EHPWR--PGARLYR 1851
Cdd:PRK12476  402 vscgqVARSQWAVIVD--PDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegSHADGaaDDGTWLR 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523  1852 TGDLGRILGnGEIVWLGRADTQVKVRGFRIEPAEVELAImrqAERQPGLRGAAVVA 1907
Cdd:PRK12476  480 TGDLGVYLD-GELYITGRIADLIVIDGRNHYPQDIEATV---AEASPMVRRGYVTA 531
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 472-852 1.06e-11

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 70.53  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   472 LSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPD-------HPLERVRLLLEDCGA 544
Cdd:PLN02387  107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASlgeealcHSLNETEVTTVICDS 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   545 -----------------RVVLVDERAATLGESLGE------TRVLHLERLPQST---GDLPAanvaPGDLAYVIYTSGST 598
Cdd:PLN02387  187 kqlkklidissqletvkRVIYMDDEGVDSDSSLSGssnwtvSSFSEVEKLGKENpvdPDLPS----PNDIAVIMYTSGST 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   599 GMPKGVMVEHRSVVNRLNWMQRRYP-IGERDVLLQKTPVTfdvSVWELfwwsftGARLSLLPPGAE---KDPREMLRS-- 672
Cdd:PLN02387  263 GLPKGVMMTHGNIVATVAGVMTVVPkLGKNDVYLAYLPLA---HILEL------AAESVMAAVGAAigyGSPLTLTDTsn 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   673 -IQR----DAV----TVIHFVPSMLTPFLD---------------LLDGDPTARAAA----------------------- 705
Cdd:PLN02387  334 kIKKgtkgDASalkpTLMTAVPAILDRVRDgvrkkvdakgglakkLFDIAYKRRLAAiegswfgawglekllwdalvfkk 413

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   706 ------SSLRLVFCSGealAPLQvarfrrlfGDAVRLVNL---------YGPTEAtvdvsdheCAS------DNPTRVPI 764
Cdd:PLN02387  414 iravlgGRIRFMLSGG---APLS--------GDTQRFINIclgapigqgYGLTET--------CAGatfsewDDTSVGRV 474

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   765 GRPIDNLRLYVLD-------RALRPQPLgavGELYIGGVGVARGYLNRPELNAERFLVDPfvAGGRLYRTGDLARWLADG 837
Cdd:PLN02387  475 GPPLPCCYVKLVSweeggylISDKPMPR---GEIVIGGPSVTLGYFKNQEKTDEVYKVDE--RGMRWFYTGDIGQFHPDG 549

                         490
                  ....*....|....*
gi 15598523   838 NLEYLGRADDQVKIR 852
Cdd:PLN02387  550 CLEIIDRKKDIVKLQ 564
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1612-1943 1.54e-11

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 69.52  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1612 DELAMLLFTSGSTGRPKGVELSHR-MWANYTQ---WQLRVASGVPGLRTLQ--------FAPLSFDMAFQEIfstlcgGG 1679
Cdd:PRK08751  208 DDIAFLQYTGGTTGVAKGAMLTHRnLVANMQQahqWLAGTGKLEEGCEVVItalplyhiFALTANGLVFMKI------GG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1680 ELQLISNRERMdPSALlhvlerRQVQRVllPFVALQRLAEASNALGVRPGALRVVVSS-----GEQLRITEDVRAFCAAM 1754
Cdd:PRK08751  282 CNHLISNPRDM-PGFV------KELKKT--RFTAFTGVNTLFNGLLNTPGFDQIDFSSlkmtlGGGMAVQRSVAERWKQV 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1755 PGLLLENQYGPTETHQvtyhSLSGDPAHYPDLP-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKL 1833
Cdd:PRK08751  353 TGLTLVEAYGLTETSP----AACINPLTLKEYNgSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEE 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1834 TAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE--LAIMrqaerqPG-LRGAAV-VARE 1909
Cdd:PRK08751  429 TAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEdvIAMM------PGvLEVAAVgVPDE 496

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 15598523  1910 RQG---------NDAFLAAFLLGEPEAVDLAELKQA----LRSELPE 1943
Cdd:PRK08751  497 KSGeivkvvivkKDPALTAEDVKAHARANLTGYKQPriieFRKELPK 543
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 469-939 1.61e-11

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport 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 hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 69.63  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  469 GGTLSYAELDAKVQAVADALRA-AGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDhpLERVRLL--LEDCGAR 545
Cdd:cd05938    3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTN--IRSKSLLhcFRCCGAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  546 VVLVD-ERAATLGESLGETR-------VLHLERLPQSTGDLPA---------------ANVAPGDLAYVIYTSGSTGMPK 602
Cdd:cd05938   81 VLVVApELQEAVEEVLPALRadgvsvwYLSHTSNTEGVISLLDkvdaasdepvpaslrAHVTIKSPALYIYTSGTTGLPK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  603 GVMVEHRSVVNRLNwMQRRYPIGERDVLLQKTPVtfdvsvwelfwWSFTGARLSLLppGA-EKDPREMLRS--------- 672
Cdd:cd05938  161 AARISHLRVLQCSG-FLSLCGVTADDVIYITLPL-----------YHSSGFLLGIG--GCiELGATCVLKPkfsasqfwd 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  673 -IQRDAVTVIHFVPSML-----TPfldlldgdPTARAAASSLRLVFCSGeaLAPLQVARFRRLFGDaVRLVNLYGPTEAT 746
Cdd:cd05938  227 dCRKHNVTVIQYIGELLrylcnQP--------QSPNDRDHKVRLAIGNG--LRADVWREFLRRFGP-IRIREFYGSTEGN 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  747 VD-------------VS--------------DHEcaSDNPTRVPIGRPIdnlrlyvldralrPQPLGAVGELyiggvgVA 799
Cdd:cd05938  296 IGffnytgkigavgrVSylykllfpfelikfDVE--KEEPVRDAQGFCI-------------PVAKGEPGLL------VA 354

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  800 R--------GYLNRPELNAERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGV 871
Cdd:cd05938  355 KitqqspflGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFL 434

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523  872 RDAAVVardsavrGTHLVGYY----VAA------AELDPGQLRAGLSATLPDFMLPAfFVRI-DSLPLSANGKLDRRQL 939
Cdd:cd05938  435 QEVNVY-------GVTVPGHEgrigMAAvklkpgHEFDGKKLYQHVREYLPAYARPR-FLRIqDSLEITGTFKQQKVRL 505
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 950-1025 1.73e-11

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: 61.79  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  950 APRTATEAELAAVWADVLGV--AEVGVHDDFYA-LGGDSILMLRIRAAAQRR-GLGFELADLMRNPTVAGLAERLVRPLA 1025
Cdd:COG0236    1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEEKLA 80
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 6-328 1.78e-11

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: 69.05  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    6 RLPLSPYQRDIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLdtdAEFEARH 85
Cdd:cd19546    4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRI---LDADAAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   86 VDLRADRDPEAAVRSWLRDAFRHAYPLDGR---SLVDLALLHSDQALYVYVrtHHIVSDAWGLQLFLSRVRAGYlGELGE 162
Cdd:cd19546   81 PELPVVPATEEELPALLADRAAHLFDLTREtpwRCTLFALSDTEHVLLLVV--HRIAADDESLDVLVRDLAAAY-GARRE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  163 PQAqmPTASLLAqLETDDYSGSEQ--YRGDR----------AYFAEALEGLEPAL---FTRRRPA-GLRRTARHRLTLE- 225
Cdd:cd19546  158 GRA--PERAPLP-LQFADYALWERelLAGEDdrdsligdqiAYWRDALAGAPDELelpTDRPRPVlPSRRAGAVPLRLDa 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  226 ---RTLLDAIRDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAA-KQVVGHFANTLPLRIRTAPEQTVDEFL 301
Cdd:cd19546  235 evhARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEGDlEGMVGPFARPLALRTDLSGDPTFRELL 314

                        330       340
                 ....*....|....*....|....*..
gi 15598523  302 AQLREATRTLLRHQKMPLGDLLRGASP 328
Cdd:cd19546  315 GRVREAVREARRHQDVPFERLAELLAL 341
PRK05857 PRK05857
fatty acid--CoA ligase;
1514-1971 2.92e-11

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 68.50  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1514 ATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVV----------AHPEHA 1583
Cdd:PRK05857   55 AADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALvapgskmassAVPEAL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1584 HVAAAERV-LPVEELVADIEPET-FAAPQL-----DELAMLlFTSGSTGRPKGVELSHRMW-----------ANYTQWql 1645
Cdd:PRK05857  135 HSIPVIAVdIAAVTRESEHSLDAaSLAGNAdqgseDPLAMI-FTSGTTGEPKAVLLANRTFfavpdilqkegLNWVTW-- 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1646 rvasgVPGLRTLQFAPLSFDMAFQEIFSTLCGGGelQLISNRERMdpSALLHVLERRQVQRVLLPFVALQRLAEASNALG 1725
Cdd:PRK05857  212 -----VVGETTYSPLPATHIGGLWWILTCLMHGG--LCVTGGENT--TSLLEILTTNAVATTCLVPTLLSKLVSELKSAN 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1726 VRPGALRVVVSSGEQLrITEDVRAFCAAmpGLLLENQYGPTEThQVTYHSLSGDPAHYPDLP--PIGRPLDGVEVQVLDA 1803
Cdd:PRK05857  283 ATVPSLRLVGYGGSRA-IAADVRFIEAT--GVRTAQVYGLSET-GCTALCLPTDDGSIVKIEagAVGRPYPGVDVYLAAT 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1804 ------ALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVR 1877
Cdd:PRK05857  359 dgigptAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG-W------VNTGDLLERREDGFFYIKGRSSEMIICG 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1878 GFRIEPAEVElaimRQAERQPGLRGAAV--VARERQGNDAFLAAFLLGEPEAVDLAELKQAL----RSELPEHMVPAHFA 1951
Cdd:PRK05857  432 GVNIAPDEVD----RIAEGVSGVREAACyeIPDEEFGALVGLAVVASAELDESAARALKHTIaarfRRESEPMARPSTIV 507

                         490       500
                  ....*....|....*....|
gi 15598523  1952 WVDGFALTPSGKRDDAALRA 1971
Cdd:PRK05857  508 IVTDIPRTQSGKVMRASLAA 527
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 2071-2345 3.04e-11

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 65.64  E-value: 3.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2071 RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGST--PLAVLEDIAASYLAAIRRvQPEGPYYLGGW 2148
Cdd:COG3208    1 PRPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGepPLTSLEELADDLAEELAP-LLDRPFALFGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2149 SFGGFVAYEMARQLRALDPQAVAQLIVldS------ITVDRNHAGSASDEALLlffyWELVWFERSDKEVEPLPEGASLe 2222
Cdd:COG3208   80 SMGALLAFELARRLERRGRPLPAHLFV--SgrraphLPRRRRPLHDLSDAELL----AELRRLGGTPEEVLADPELLEL- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2223 qkldhiveraieagVLPAgtpratvqrlyelFRASWQALIGYRPevsdqdmtllRADGPLPLalkPMHDAAGTHygDPK- 2301
Cdd:COG3208  153 --------------FLPI-------------LRADFRLLETYRY----------TPGPPLDC---PITALGGDD--DPLv 190

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15598523 2302 -----NGWQHWTSGRLDVIDVPGDHLVLMKEPyvETVAAEIAALLEPST 2345
Cdd:COG3208  191 speelAAWREHTTGPFRLRVFPGGHFFLRDHP--AELLALIRAALAALA 237
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 568-877 3.14e-11

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 67.87  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  568 LERLPQSTG-DLPAAN------VAPGDLAYVIYTSGSTGMPKGVMVEhRSVVNRLNWMQRRY----PIGERDVLLqktpV 636
Cdd:COG1541   58 LAKLPFTTKeDLRDNYpfglfaVPLEEIVRIHASSGTTGKPTVVGYT-RKDLDRWAELFARSlraaGVRPGDRVQ----N 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  637 TFDVSvwelFWWSFTGARLsllppGAEK-----------DPREMLRSIQRDAVTVIHFVPSMLtpfLDLLDgdpTARA-- 703
Cdd:COG1541  133 AFGYG----LFTGGLGLHY-----GAERlgatvipagggNTERQLRLMQDFGPTVLVGTPSYL---LYLAE---VAEEeg 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  704 ---AASSLRLVFCSGEALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVSdHECASDNPTRVPigrpiDNLRLY-VLDRA 779
Cdd:COG1541  198 idpRDLSLKKGIFGGEPWSEEMRKEIEERWG--IKAYDIYGLTEVGPGVA-YECEAQDGLHIW-----EDHFLVeIIDPE 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  780 -LRPQPLGAVGELYIGGvgvargylnrpeLNAERFlvdPFVaggRlYRTGDLARWLADGN--------LEY-LGRADDQV 849
Cdd:COG1541  270 tGEPVPEGEEGELVVTT------------LTKEAM---PLI---R-YRTGDLTRLLPEPCpcgrthprIGRiLGRADDML 330

                        330       340
                 ....*....|....*....|....*...
gi 15598523  850 KIRGNRVEPDEVRDRLAALPGVRDAAVV 877
Cdd:COG1541  331 IIRGVNVFPSQIEEVLLRIPEVGPEYQI 358
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1991-2049 3.92e-11

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: 60.27  E-value: 3.92e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523   1991 RTLAGLLGELLDRP--RVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVE 2049
Cdd:pfam00550    1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1464-1975 4.27e-11

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 68.84  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1464 RRDAASQPepLVDVVS------------LFERQVEAL----PGSAALA-FEEQRWTYRDLDHVARcVATRLVRAGARRGD 1526
Cdd:PRK06814  607 RRSAAGAA--LYDIMSdmmfetsdydrtLFEALIEAAkihgFKKLAVEdPVNGPLTYRKLLTGAF-VLGRKLKKNTPPGE 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1527 AIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVA----------HPEHAHVAAAERVLPVEE 1596
Cdd:PRK06814  684 NVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTsrafiekarlGPLIEALEFGIRIIYLED 763

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1597 LVADIEPE--------------TFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGvpglrtlqfap 1661
Cdd:PRK06814  764 VRAQIGLAdkikgllagrfplvYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRnLLANRAQVAARIDFS----------- 832

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1662 lSFDMAFQ--EIFST--LCGGGELQLISN-RERMDPSAlLHVlerRQVQRVLLPFVA---------LQRLAEASNALGVR 1727
Cdd:PRK06814  833 -PEDKVFNalPVFHSfgLTGGLVLPLLSGvKVFLYPSP-LHY---RIIPELIYDTNAtilfgtdtfLNGYARYAHPYDFR 907

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1728 pgALRVVVSSGEQLRitEDVRAFCAAMPGLLLENQYGPTETHQVTyhSLSgDPAHYpDLPPIGRPLDGVEvqvldAALRP 1807
Cdd:PRK06814  908 --SLRYVFAGAEKVK--EETRQTWMEKFGIRILEGYGVTETAPVI--ALN-TPMHN-KAGTVGRLLPGIE-----YRLEP 974

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1808 VPvGVT--GELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAE 1885
Cdd:PRK06814  975 VP-GIDegGRLFVRGPNVMLGYLRAENPGVLEPPADGW------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAA 1047

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1886 VELAImrqAERQPGLRGAAV-VARERQGNDAFLaafLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKR 1964
Cdd:PRK06814 1048 VEELA---AELWPDALHAAVsIPDARKGERIIL---LTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKI 1121

                         570
                  ....*....|.
gi 15598523  1965 DDAALRALPLE 1975
Cdd:PRK06814 1122 DYVAVTKLAEE 1132
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
447-936 5.90e-11

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 67.48  E-value: 5.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   447 LPTLFAEQVARTPQRTALLEADGGTLS---YAELDAKVQAVA------DALRAAGVrTDERVALLVArgphllpAILGVQ 517
Cdd:PRK05851    4 LAAALSDAMTASGRDLVVLDRESGLWRrhpWPEVHGRAENVAarlldrDRPGAVGL-VGEPTVELVA-------AIQGAW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   518 RAGGAyVPINPDhpleRVRLLLEDCGARVVLvdERAATLGESLGETRVLHLERLPQ-----STGDL----------PAAN 582
Cdd:PRK05851   76 LAGAA-VSILPG----PVRGADDGRWADATL--TRFAGIGVRTVLSHGSHLERLRAvdssvTVHDLataahtnrsaSLTP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   583 VAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGE-RDVLLQKTPVTFDVSVWELFWWSFTGARLSLLPPG 661
Cdd:PRK05851  149 PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAaTDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTT 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   662 A-EKDPREMLRSIQRDAVTVI---HFVPSMLTPFLDLLDG-DPTA-RAAASSLRLVFCSGEALAPLQVARfrrlFG-DAV 734
Cdd:PRK05851  229 AfSASPFRWLSWLSDSRATLTaapNFAYNLIGKYARRVSDvDLGAlRVALNGGEPVDCDGFERFATAMAP----FGfDAG 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   735 RLVNLYGPTEATVDVSDHECA--------SDNPTRVP-----IGRPIDNLRLYVLDRALRPQPLG-AVGELYIGGVGVAR 800
Cdd:PRK05851  305 AAAPSYGLAESTCAVTVPVPGiglrvdevTTDDGSGArrhavLGNPIPGMEVRISPGDGAAGVAGrEIGEIEIRGASMMS 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   801 GYLNRPELNAerflvdpfvagGRLYRTGDLArWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVA-- 878
Cdd:PRK05851  385 GYLGQAPIDP-----------DDWFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvg 452

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523   879 -RDSAVRGTHLVgyyvaAAELDpGQLRAGLSATLPDF------MLPA--FFVRIDSLPLSANGKLDR 936
Cdd:PRK05851  453 tGEGSARPGLVI-----AAEFR-GPDEAGARSEVVQRvasecgVVPSdvVFVAPGSLPRTSSGKLRR 513
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 469-923 9.87e-11

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: 66.69  E-value: 9.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  469 GGTLSYAELDAKVQAVADALRAA-GVRTDERVALLVARGPHLLPAILGVQRAGGAYVPIN---PDHPLER-VRLlledCG 543
Cdd:cd05937    3 GKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINynlSGDPLIHcLKL----SG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  544 ARVVLVDeraatlgeslgetrvlhlerlpqstgdlpaanvaPGDLAYVIYTSGSTGMPKGVMVehrsvvnrlNWMqRRYP 623
Cdd:cd05937   79 SRFVIVD----------------------------------PDDPAILIYTSGTTGLPKAAAI---------SWR-RTLV 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  624 IGE---RDVLLQKTPVTFdvSVWELFWWS--FTGARLSLLPPGAEKDPREM-LRSIQRDAV----TVIHFVPSMLTPfld 693
Cdd:cd05937  115 TSNllsHDLNLKNGDRTY--TCMPLYHGTaaFLGACNCLMSGGTLALSRKFsASQFWKDVRdsgaTIIQYVGELCRY--- 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  694 LLDGDPTARAAASSLRLVFcsGEALAPLQVARFRRLFGDAVrLVNLYGPTEATVDVSDHE-------------------- 753
Cdd:cd05937  190 LLSTPPSPYDRDHKVRVAW--GNGLRPDIWERFRERFNVPE-IGEFYAATEGVFALTNHNvgdfgagaighhglirrwkf 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  754 ------CASDNPTRVPIGRPidnlRLYVLDRALRPQPLGAVGELYIGGVGVARGYLNRPELNAERFLVDPFVAGGRLYRT 827
Cdd:cd05937  267 enqvvlVKMDPETDDPIRDP----KTGFCVRAPVGEPGEMLGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRT 342

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  828 GDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVA-----RDSAVR--GTHLVGYYVAAAELDP 900
Cdd:cd05937  343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvpgHDGRAGcaAITLEESSAVPTEFTK 422

                        490       500
                 ....*....|....*....|...
gi 15598523  901 GQLRAGLSATLPDFMLPaFFVRI 923
Cdd:cd05937  423 SLLASLARKNLPSYAVP-LFLRL 444
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 1502-1941 1.20e-10

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: 66.36  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1502 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRlalILETAQPFRVVAHPe 1581
Cdd:cd05908   17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEH---KLKLNKVWNTLKNP- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1582 hahvaaaerVLPVEELVADIEPetfaapqlDELAMLLFTSGSTGRPKGVELSH-------RMWANYTQWQLRVasgvpgl 1654
Cdd:cd05908   93 ---------YLITEEEVLCELA--------DELAFIQFSSGSTGDPKGVMLTHenlvhnmFAILNSTEWKTKD------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1655 RTLQFAPLSFDM---AFQeiFSTLCGGGELQLISNRERM-DPSALLHVLERRQVQRVLLPFVA----LQRLaEASNALGV 1726
Cdd:cd05908  149 RILSWMPLTHDMgliAFH--LAPLIAGMNQYLMPTRLFIrRPILWLKKASEHKATIVSSPNFGykyfLKTL-KPEKANDW 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1727 RPGALRVVVSSGEQLrITEDVRAFCAAMP--GL----------LLENQYG----PTETHQVTY-----HSLSGDPAHYPD 1785
Cdd:cd05908  226 DLSSIRMILNGAEPI-DYELCHEFLDHMSkyGLkrnailpvygLAEASVGaslpKAQSPFKTItlgrrHVTHGEPEPEVD 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1786 --------LPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGR 1857
Cdd:cd05908  305 kkdsecltFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLGF 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1858 ILgNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVA----RERQGNDAFLaAFLLGEPEAVDLAEL 1933
Cdd:cd05908  379 IR-NGRLVITGREKDIIFVNGQNVYPHDIE----RIAEELEGVELGRVVAcgvnNSNTRNEEIF-CFIEHRKSEDDFYPL 452


                 ....*...
gi 15598523 1934 KQALRSEL 1941
Cdd:cd05908  453 GKKIKKHL 460
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1517-1971 2.07e-10

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 66.21  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1517 LVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL-------DVSYPAQrlalilETAQPFRVVAHPEHAHVAAAE 1589
Cdd:PRK06060   47 LRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLAnpelhrdDHALAAR------NTEPALVVTSDALRDRFQPSR 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1590 RVLPVEEL--VADIEPETFAAPQLDELAMLLFTSGSTGRPKGVelSHRMWANYT------QWQLRVASGVPGLRT--LQF 1659
Cdd:PRK06060  121 VAEAAELMseAARVAPGGYEPMGGDALAYATYTSGTTGPPKAA--IHRHADPLTfvdamcRKALRLTPEDTGLCSarMYF 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1660 A-----PLSFDMAF--QEIFSTLCGGGELQLISNrERMDPSALLHVLErrqvqrvllpFVAlqRLAEASNALGVRpgALR 1732
Cdd:PRK06060  199 AyglgnSVWFPLATggSAVINSAPVTPEAAAILS-ARFGPSVLYGVPN----------FFA--RVIDSCSPDSFR--SLR 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1733 VVVSSGEQLR--ITEDVRAFCAAMPGLlleNQYGPTETHQvTYHSLSGDPAHYPDLppiGRPLDGVEVQVLDAALRPVPV 1810
Cdd:PRK06060  264 CVVSAGEALElgLAERLMEFFGGIPIL---DGIGSTEVGQ-TFVSNRVDEWRLGTL---GRVLPPYEIRVVAPDGTTAGP 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1811 GVTGELYFGGDCLARGYHRAPK--LTAERFVEhpwrpgarlyrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVEL 1888
Cdd:PRK06060  337 GVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVER 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1889 AIMrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVD---LAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 1965
Cdd:PRK06060  406 LII---EDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDgsvMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLV 482


                  ....*.
gi 15598523  1966 DAALRA 1971
Cdd:PRK06060  483 RGALRK 488
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1085-1362 2.68e-10

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: 65.20  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1085 DEAAFRHALDRVVAAYPALRSSFDLSGasepLQLVHTQARSEPL-ILDLRGNPEAGTVLD-EHIRQRRFHR-YSLQQPGL 1161
Cdd:cd19535   38 DPDRLERAWNKLIARHPMLRAVFLDDG----TQQILPEVPWYGItVHDLRGLSEEEAEAAlEELRERLSHRvLDVERGPL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1162 FLFAAFVREDG-------LDLVfsfhhaILDGWSVANLIVALVAAYRGEPLPGPAPALA----CHVREELAALASPAAVG 1230
Cdd:cd19535  114 FDIRLSLLPEGrtrlhlsIDLL------VADALSLQILLRELAALYEDPGEPLPPLELSfrdyLLAEQALRETAYERARA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1231 YWtgllegarMTRLDGF-GAHEPQAAQGPASHREA--------LPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSR 1301
Cdd:cd19535  188 YW--------QERLPTLpPAPQLPLAKDPEEIKEPrftrrehrLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSG 259

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523 1302 SDSV---VTgaISNGRPELPDADRMVGLF--LNTVPVRSEiAGCSWIEVADALFRQERDGHAHRRY 1362
Cdd:cd19535  260 QPRFllnLT--LFNRLPLHPDVNDVVGDFtsLLLLEVDGS-EGQSFLERARRLQQQLWEDLDHSSY 322
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 1496-1970 2.77e-10

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: 65.15  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1496 FEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGlvCVPLDVSYPAQRLALIletaqpf 1574
Cdd:cd05937    1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIG--AAPAFINYNLSGDPLI------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1575 rvvahpehaHVAaaeRVLPVEELVADIepetfaapqlDELAMLLFTSGSTGRPKGVELSHRMwaNYTQWQLR--VASGVP 1652
Cdd:cd05937   72 ---------HCL---KLSGSRFVIVDP----------DDPAILIYTSGTTGLPKAAAISWRR--TLVTSNLLshDLNLKN 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1653 GLRTLQFAPLSFDMAFQEIF-STLCGGGELQL-----ISN--RERMDPSALlHVLERRQVQRVLL-----PFVALQRLAE 1719
Cdd:cd05937  128 GDRTYTCMPLYHGTAAFLGAcNCLMSGGTLALsrkfsASQfwKDVRDSGAT-IIQYVGELCRYLLstppsPYDRDHKVRV 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1720 ASNAlGVRP---GALR---VVVSSGEQLRITEDVRAF-----------CAAMPGLL----LENQYGPtethqVTYHSLSG 1778
Cdd:cd05937  207 AWGN-GLRPdiwERFRerfNVPEIGEFYAATEGVFALtnhnvgdfgagAIGHHGLIrrwkFENQVVL-----VKMDPETD 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1779 DPahypdlppIGRPLDGVEVQVldaalrpvPVGVTGE----LYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLYRTGD 1854
Cdd:cd05937  281 DP--------IRDPKTGFCVRA--------PVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGD 344

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1855 LGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARERQGND--AFLAAFLLGE----PEAV 1928
Cdd:cd05937  345 LLRQDADGRWYFLDRLGDTFRWKSENVSTTEVA----DVLGAHPDIAEANVYGVKVPGHDgrAGCAAITLEEssavPTEF 420

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 15598523 1929 DLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd05937  421 TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
437-935 3.21e-10

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 65.76  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   437 TDQAFPEQATLPTLFA--EQVART--PQRTALLEADGGTLSYAELDAKVQAVADALRAaGVRTDERVALLVARGPHLLPA 512
Cdd:PRK06814  620 SDMMFETSDYDRTLFEalIEAAKIhgFKKLAVEDPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVT 698

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   513 ILGVQRAGgaYVP--INPDHPLERVRLLLEDCGARVVLVDER---AATLGESL----GETRVLHLERLPQ--STGD---- 577
Cdd:PRK06814  699 FFALQSAG--RVPamINFSAGIANILSACKAAQVKTVLTSRAfieKARLGPLIealeFGIRIIYLEDVRAqiGLADkikg 776

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   578 --------LPAANVAPGDLAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVtfdvsvwelfWWS 649
Cdd:PRK06814  777 llagrfplVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPV----------FHS 846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   650 F--TGArlSLLPpgaekdpreMLRSIQrdavtvIHFVPSML----TPFL------DLLDGDPT-----ARAAAS----SL 708
Cdd:PRK06814  847 FglTGG--LVLP---------LLSGVK------VFLYPSPLhyriIPELiydtnaTILFGTDTflngyARYAHPydfrSL 909

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   709 RLVFCSGEALAplqvARFRRL----FGdaVRLVNLYGPTEATVDVSDHECASDNPTRVpiGRpidnlRLYVLDRALRPQP 784
Cdd:PRK06814  910 RYVFAGAEKVK----EETRQTwmekFG--IRILEGYGVTETAPVIALNTPMHNKAGTV--GR-----LLPGIEYRLEPVP 976

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   785 -LGAVGELYIGGVGVARGYLnRPElnAERFLVDPfvAGGrLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRD 863
Cdd:PRK06814  977 gIDEGGRLFVRGPNVMLGYL-RAE--NPGVLEPP--ADG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE 1050

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598523   864 RLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLD 935
Cdd:PRK06814 1051 LAAELWPDALHAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 1502-1963 3.64e-10

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 65.04  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1502 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA-----------LILE- 1569
Cdd:PRK07059   50 TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEhqlkdsgaeaiVVLEn 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1570 ---TAQpfRVVAHPEHAHVAAA--------------------ERVLPVEEL---------VADIEPETFAAPQL--DELA 1615
Cdd:PRK07059  130 fatTVQ--QVLAKTAVKHVVVAsmgdllgfkghivnfvvrrvKKMVPAWSLpghvrfndaLAEGARQTFKPVKLgpDDVA 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1616 MLLFTSGSTGRPKGVELSHR-MWANYTQ---WqLRVASGVPG----LRTLQFAPLsfdmafQEIFS-TLCG------GGE 1680
Cdd:PRK07059  208 FLQYTGGTTGVSKGATLLHRnIVANVLQmeaW-LQPAFEKKPrpdqLNFVCALPL------YHIFAlTVCGllgmrtGGR 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1681 LQLISNRErmDPSALLHVLERRQVQRvllpFVALQRLAeasNALGVRPGALRV-----VVSSGEQLRITEDVRAFCAAMP 1755
Cdd:PRK07059  281 NILIPNPR--DIPGFIKELKKYQVHI----FPAVNTLY---NALLNNPDFDKLdfsklIVANGGGMAVQRPVAERWLEMT 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1756 GLLLENQYGPTETHQVtyhsLSGDPAHYPDLP-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLT 1834
Cdd:PRK07059  352 GCPITEGYGLSETSPV----ATCNPVDATEFSgTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDET 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1835 AERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPG-LRGAAV-VARERQG 1912
Cdd:PRK07059  428 AKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIE----EVVASHPGvLEVAAVgVPDEHSG 497

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15598523  1913 NdaFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK07059  498 E--AVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGK 546
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 1493-1971 4.11e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 65.05  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1493 ALAFEEQRWTYRDldHVARCVATRLVRAGARRGDA---IGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILE 1569
Cdd:PRK13388   19 AVRYGDRTWTWRE--VLAEAAARAAALIALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1570 TAQPFRVVAHPEHAHV-----AAAERVLPVE-----ELVA---DIEPETFAAPqlDELAMLLFTSGSTGRPKGVELSHRM 1636
Cdd:PRK13388   97 RADCQLLVTDAEHRPLldgldLPGVRVLDVDtpayaELVAaagALTPHREVDA--MDPFMLIFTSGTTGAPKAVRCSHGR 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1637 W-----------------------------ANYTQWQLRVASGVPGLRTLQFAPLSF--DMA-FQEIFSTLCGGGELQLI 1684
Cdd:PRK13388  175 LafagralterfgltrddvcyvsmplfhsnAVMAGWAPAVASGAAVALPAKFSASGFldDVRrYGATYFNYVGKPLAYIL 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1685 SNRERMDpsallhvlerrqvqrvllpfvalqrlaEASNALGVRPGalrvvvSSGEQLRITEDVRAFcaampGLLLENQYG 1764
Cdd:PRK13388  255 ATPERPD---------------------------DADNPLRVAFG------NEASPRDIAEFSRRF-----GCQVEDGYG 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1765 PTEThqvtyhslSGDPAHYPDLPP--IGRPLDGVEVQVLDaALRPVPVGV-------------TGELY-FGGDCLARGYH 1828
Cdd:PRK13388  297 SSEG--------AVIVVREPGTPPgsIGRGAPGVAIYNPE-TLTECAVARfdahgallnadeaIGELVnTAGAGFFEGYY 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1829 RAPKLTAERfVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRqaeRQPGLRGAAV--V 1906
Cdd:PRK13388  368 NNPEATAER-MRHGM------YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIE-RILL---RHPAINRVAVyaV 436

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523  1907 ARERQGnDAFLAAFLLGEPEAVDLAELKQALRS--ELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 1971
Cdd:PRK13388  437 PDERVG-DQVMAALVLRDGATFDPDAFAAFLAAqpDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 646-940 4.46e-10

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 64.63  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   646 FWWSF-TGARLSLLPpgaekdpremLRSIQRDAVT-------VIHFVPSMLTpflDLLDGDPTARAAassLRLVFCSGea 717
Cdd:PRK07445  178 FMRSFlTGGKLVILP----------YKRLKSGQELppnpsdfFLSLVPTQLQ---RLLQLRPQWLAQ---FRTILLGG-- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   718 lAP-----LQVARFRRLfgdavRLVNLYGPTE-----ATVDVSDHECASDNptrvpIGRPIDNLRLyvldrALRPqplGA 787
Cdd:PRK07445  240 -APawpslLEQARQLQL-----RLAPTYGMTEtasqiATLKPDDFLAGNNS-----SGQVLPHAQI-----TIPA---NQ 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   788 VGELYIGGVGVARGYlnrpelnaerflVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAA 867
Cdd:PRK07445  301 TGNITIQAQSLALGY------------YPQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598523   868 LPGVRDAAVVARDSAVRGTHLVGYYVAAA-ELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLP 940
Cdd:PRK07445  369 TGLVQDVCVLGLPDPHWGEVVTAIYVPKDpSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 1489-1921 5.78e-10

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 64.12  E-value: 5.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAFEEQRWTYRDL-DHVARcVATRLVRAGARRGDaiGVAL---NrSPEMIATIWGILRAGLVCVPLDVSYPAQRL 1564
Cdd:PRK09029   17 PQAIALRLNDEVLTWQQLcARIDQ-LAAGFAQQGVVEGS--GVALrgkN-SPETLLAYLALLQCGARVLPLNPQLPQPLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1565 ALILETAQpFRVVAHPEHAHVAAAERVLPVEELVADIEpetfAAPQLDELAMLLFTSGSTGRPKGVELSHRMwanytqwQ 1644
Cdd:PRK09029   93 EELLPSLT-LDFALVLEGENTFSALTSLHLQLVEGAHA----VAWQPQRLATMTLTSGSTGLPKAAVHTAQA-------H 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1645 LRVASGVpgLRTLQFAP-----LS---FDMAFQEIF-STLCGGGELQLisnRERMD-PSALLHV----LERRQVQRVL-- 1708
Cdd:PRK09029  161 LASAEGV--LSLMPFTAqdswlLSlplFHVSGQGIVwRWLYAGATLVV---RDKQPlEQALAGCthasLVPTQLWRLLdn 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1709 --LPfVALQR-----------LAEASNALGvrpgalrvvvssgeqlritedVRAFCAampglllenqYGPTE---ThqVT 1772
Cdd:PRK09029  236 rsEP-LSLKAvllggaaipveLTEQAEQQG---------------------IRCWCG----------YGLTEmasT--VC 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1773 ---YHSLSGdpahypdlppIGRPLDGVEVQVldaalrpvpvgVTGELYFGGDCLARGYHRAPKLTAerFV-EHPWrpgar 1848
Cdd:PRK09029  282 akrADGLAG----------VGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLVP--LVnDEGW----- 333

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1849 lYRTGDLGRILGnGEIVWLGRADTQVKVRGFRIEPAEVELAIM-----RQA------ERQPGLRGAAVVARERQGNDAFL 1917
Cdd:PRK09029  334 -FATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINqhplvQQVfvvpvaDAEFGQRPVAVVESDSEAAVVNL 411


                  ....
gi 15598523  1918 AAFL 1921
Cdd:PRK09029  412 AEWL 415
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 957-1014 7.51e-10

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: 56.80  E-value: 7.51e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523    957 AELAAVWADVLGVA--EVGVHDDFYALGGDSILMLRIRAAAQRR-GLGFELADLMRNPTVA 1014
Cdd:pfam00550    1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1053-1428 8.76e-10

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: 63.43  E-value: 8.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1053 SRLSLGLLFHSRQRPDSSVyhdvfhyrFDLAWDEAAFRHaldrvvaayPALRSSFdLSGASEPLQLVHTQARSEPLILDL 1132
Cdd:cd20483   22 TFLNLLLVCHIKGKPDVNL--------LQKALSELVRRH---------EVLRTAY-FEGDDFGEQQVLDDPSFHLIVIDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1133 RGNPEAGTVLDEHIRQRRFHRYSLQQpGLFLFAAFVR--EDGLDLVFSFHHAILDGWSVANLIVALVAAY----RGEPL- 1205
Cdd:cd20483   84 SEAADPEAALDQLVRNLRRQELDIEE-GEVIRGWLVKlpDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDLa 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1206 PGPAPALA------CHvrEELaaLASPAA---VGYWTGLLEGARMT-RLDGFG-AHEPQAAQGPAS-HREALPDGLLERL 1273
Cdd:cd20483  163 TVPPPPVQyidftlWH--NAL--LQSPLVqplLDFWKEKLEGIPDAsKLLPFAkAERPPVKDYERStVEATLDKELLARM 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1274 KATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIagcsWIEVA-DALFRQ 1352
Cdd:cd20483  239 KRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPH-PDFDDLVGFFVNMLPIRCRM----DCDMSfDDLLES 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1353 ER----DGHAHRRYPLSAIQQIVGDELSS--------AFNYVnLHVLEPLWQLRDFRVWEETNFAllvnvIATPSDgMYL 1420
Cdd:cd20483  314 TKttclEAYEHSAVPFDYIVDALDVPRSTshfpigqiAVNYQ-VHGKFPEYDTGDFKFTDYDHYD-----IPTACD-IAL 386


                 ....*...
gi 15598523 1421 RIDSDGRG 1428
Cdd:cd20483  387 EAEEDPDG 394
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 860-933 1.17e-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: 56.78  E-value: 1.17e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523    860 EVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV--AAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGK 933
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PLN02479 PLN02479
acetate-CoA ligase
 1461-1947 1.66e-09

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 62.94  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1461 LAPRRDAASQPEPLVDVVSL-----FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRS 1535
Cdd:PLN02479    1 MAKERDIDDLPKNAANYTALtplwfLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1536 PEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ-------------------------------PFRVVA-----H 1579
Cdd:PLN02479   81 PAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKsevvmvdqefftlaeealkilaekkkssfkpPLLIVIgdptcD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1580 PEHAHVAAAERVLPVEELVADIEPETFAAPQLDELA--MLLFTSGSTGRPKGVELSHR-----MWANYTQWQLRvaSGVP 1652
Cdd:PLN02479  161 PKSLQYALGKGAIEYEKFLETGDPEFAWKPPADEWQsiALGYTSGTTASPKGVVLHHRgaylmALSNALIWGMN--EGAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1653 GLRTLqfaPLSF--DMAFQEIFSTLCGGGelqlISNRErMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGA 1730
Cdd:PLN02479  239 YLWTL---PMFHcnGWCFTWTLAALCGTN----ICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1731 lRVVvssgeqlriteDVRAFCAAMP----------GLLLENQYGPTETHQVTyhSLSGDPAHYPDLPPIGRP-------- 1792
Cdd:PLN02479  311 -RVV-----------HVMTAGAAPPpsvlfamsekGFRVTHTYGLSETYGPS--TVCAWKPEWDSLPPEEQArlnarqgv 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1793 ----LDGVEVqVLDAALRPVPV-GVT-GELYFGGDCLARGYHRAPKLTAERFvEHPWrpgarlYRTGDLGRILGNGEIVW 1866
Cdd:PLN02479  377 ryigLEGLDV-VDTKTMKPVPAdGKTmGEIVMRGNMVMKGYLKNPKANEEAF-ANGW------FHSGDLGVKHPDGYIEI 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1867 LGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGNDAFLAAFLLGEPEAVDLAELKQAL----RSE 1940
Cdd:PLN02479  449 KDRSKDIIISGGENISSLEVENVVY----THPAVLEASVVARpdERWGESPCAFVTLKPGVDKSDEAALAEDImkfcRER 524


                  ....*..
gi 15598523  1941 LPEHMVP 1947
Cdd:PLN02479  525 LPAYWVP 531
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 1477-1678 1.83e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 63.21  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1477 VVSLFERQVEALPGSAALAF---------EEQRWTYRDLDHVARCVATRLVRAGaRRGDAIGVALNRSPEMIATIWGILR 1547
Cdd:PRK07769   23 LVRHVERWAKVRGDKLAYRFldfsterdgVARDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALY 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1548 AGLVCVPL-DVSYP--AQRLALILETAQPFRVVAHPEHA--------HVAAAER--VLPVEElVADIEPETFAAPQLDE- 1613
Cdd:PRK07769  102 AGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAegvrkffrARPAKERprVIAVDA-VPDEVGATWVPPEANEd 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523  1614 -LAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAF-QEIFSTLCGG 1678
Cdd:PRK07769  181 tIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLiTVLLPALLGH 247
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 1608-1906 2.08e-09

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 62.89  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1608 APqlDELAMLLFTSGSTGRPKGVELSHRmwANYTQWQLRVAsgVPGLRT----LQFAPLSFDMAFQEIFSTLCGGGELQL 1683
Cdd:PLN02860  170 AP--DDAVLICFTSGTTGRPKGVTISHS--ALIVQSLAKIA--IVGYGEddvyLHTAPLCHIGGLSSALAMLMVGACHVL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1684 ISnreRMDPSALLHVLERRQ------VQRVLLPFVALQRLAEASNalgVRPGALRVVVSSGE-QLRITEDVRAFcaaMPG 1756
Cdd:PLN02860  244 LP---KFDAKAALQAIKQHNvtsmitVPAMMADLISLTRKSMTWK---VFPSVRKILNGGGSlSSRLLPDAKKL---FPN 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1757 LLLENQYGPTET-------------------HQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQV-LDAALRpvpvgvTGEL 1816
Cdd:PLN02860  315 AKLFSAYGMTEAcssltfmtlhdptlespkqTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIgLDESSR------VGRI 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1817 YFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeR 1896
Cdd:PLN02860  389 LTRGPHVMLGYWGQNSETASVLSNDGW------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLS----Q 458

                         330
                  ....*....|
gi 15598523  1897 QPGLRGAAVV 1906
Cdd:PLN02860  459 HPGVASVVVV 468
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 1500-1970 2.09e-09

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 62.85  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1500 RWTYRDLDHVARCVATRLVRAGARRGDAIG-VALNRSPEMiATIWGILRAGLVCVPLDVSYPAQRLALILETAQ------ 1572
Cdd:PRK06018   39 RTTYAQIHDRALKVSQALDRDGIKLGDRVAtIAWNTWRHL-EAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEdrvvit 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1573 -----PF------------RVVAHPEHAHVAAA--ERVLPVEELVADIEPEtFAAPQLDE--LAMLLFTSGSTGRPKGVE 1631
Cdd:PRK06018  118 dltfvPIlekiadklpsveRYVVLTDAAHMPQTtlKNAVAYEEWIAEADGD-FAWKTFDEntAAGMCYTSGTTGDPKGVL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1632 LSHRmwANYTQWQLRVASGVPGLRT----LQFAPLSFDMAFQEIFSTLCGGGelQLISNRERMDPSALLHVLERRQVQ-R 1706
Cdd:PRK06018  197 YSHR--SNVLHALMANNGDALGTSAadtmLPVVPLFHANSWGIAFSAPSMGT--KLVMPGAKLDGASVYELLDTEKVTfT 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1707 VLLPFVALQrLAEASNALGVRPGALRVVVSSGeqlritedvrafcAAMPGLLLE----------NQYGPTETHQVTyhSL 1776
Cdd:PRK06018  273 AGVPTVWLM-LLQYMEKEGLKLPHLKMVVCGG-------------SAMPRSMIKafedmgvevrHAWGMTEMSPLG--TL 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1777 SGDPAHYPDLPP---------IGRPLDGVEVQVLDAALRPVPVG--VTGELYFGGDCLARGYHRAPK--LTAERFvehpw 1843
Cdd:PRK06018  337 AALKPPFSKLPGdarldvlqkQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYRVDGeiLDDDGF----- 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1844 rpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE-LAImrqaeRQPGLRGAAVVA------RERQgndaf 1916
Cdd:PRK06018  412 ------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEnLAV-----GHPKVAEAAVIGvyhpkwDERP----- 475

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15598523  1917 LAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:PRK06018  476 LLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
PRK07868 PRK07868
acyl-CoA synthetase; Validated
 324-970 2.10e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 63.20  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   324 RGASPLFDTTLSYMRWPAAQAIPNASVETVA-QTHAHDPDALAIwvSEFDGH---SDAQVDFEYACDVFDADFpmdAAAR 399
Cdd:PRK07868  345 RAAQQTWPTVADWVKWLEGDGDKPENIHLMAdQPAEHTDSGVSL--SSRVAHgvgEVAEAALALARGAADAAV---AANR 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   400 HIETFLRALVEGGER--RLGELDPlsaaereeliHTRnatdqafpeqATLPTLFAEQVARTPQRTALLeADGGTLSYAEL 477
Cdd:PRK07868  420 SVRTLAVETARTLPRlaRLGQIND----------HTR----------ISLGRIIAEQARDAPKGEFLL-FDGRVHTYEAV 478

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   478 DAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLER-VRLlledCGARVVLVD----ER 552
Cdd:PRK07868  479 NRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPDTDLAAaVRL----GGVTEIITDptnlEA 554

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   553 AATLGESL-----GETRVLH---------LERLPQSTGDLPA-----ANVApGDLAYVIY-TSGSTGMPKGVmVEHRSVV 612
Cdd:PRK07868  555 ARQLPGRVlvlggGESRDLDlpddadvidMEKIDPDAVELPGwyrpnPGLA-RDLAFIAFsTAGGELVAKQI-TNYRWAL 632

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   613 NRLNwMQRRYPIGERDVLLQKTP--------VTFDVSVwelfwwsFTGARLSLlppGAEKDPREMLRSIQRDAVTVIHFV 684
Cdd:PRK07868  633 SAFG-TASAAALDRRDTVYCLTPlhhesgllVSLGGAV-------VGGSRIAL---SRGLDPDRFVQEVRQYGVTVVSYT 701

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   685 PSMLTPFLDlldgDPTARAAAS-SLRLVFCSG----------EALAPLQVARFrrlF----GDAVrLVNlygpteatvdV 749
Cdd:PRK07868  702 WAMLREVVD----DPAFVLHGNhPVRLFIGSGmptglwervvEAFAPAHVVEF---FattdGQAV-LAN----------V 763

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   750 SDHECASDNpTRVPIGRPIDNLRLYVLDRALRPQPLGAVGELYIGGVGVArgylnrpeLNAERFLVDP--------FVAG 821
Cdd:PRK07868  764 SGAKIGSKG-RPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVL--------LARARGPIDPtasvkrgvFAPA 834

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   822 GRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVrDAAvVARDSAVRGTHLVgyyVAAAELDPG 901
Cdd:PRK07868  835 DTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGV-DLA-VTYGVEVGGRQLA---VAAVTLRPG 909

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   902 ------QLRAGLSAtLPDFMLPAFFVRIDSLPLSAN-----GKLDRRQLPAPPEQVAAVAPRTA-----TEAELAAVWAD 965
Cdd:PRK07868  910 aaitaaDLTEALAS-LPVGLGPDIVHVVPEIPLSATyrptvSALRAAGIPKPGRQAWYFDPETNryrrlTPAVRAELTGG 988


                  ....*
gi 15598523   966 VLGVA 970
Cdd:PRK07868  989 HRRGA 993
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 1498-1947 2.22e-09

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: 62.37  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1498 EQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVV 1577
Cdd:cd05940    1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1578 AhpehahvaaaervlpveelvadiepetfaapqldELAMLLFTSGSTGRPKGVELSHRMWANYTQWqlrVASGVPGLRTL 1657
Cdd:cd05940   81 V----------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAF---FAGSGGALPSD 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1658 QF---APLSFDMAFQEIFST-LCGGGELQLisnRERMDPSALLHvlERRQVQRVLLPFVA--LQRLAEASNALGVRPGAL 1731
Cdd:cd05940  124 VLytcLPLYHSTALIVGWSAcLASGATLVI---RKKFSASNFWD--DIRKYQATIFQYIGelCRYLLNQPPKPTERKHKV 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1732 RVVVSSGEQLRITED---------VRAFcaampglllenqYGPTE--THQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQV 1800
Cdd:cd05940  199 RMIFGNGLRPDIWEEfkerfgvprIAEF------------YAATEgnSGFINFFGKPGAIGRNPSLLRKVAPLALVKYDL 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1801 -LDAALRP-------VPVGVTGELYFGGDCLAR--GYHRaPKLTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRA 1870
Cdd:cd05940  267 eSGEPIRDaegrcikVPRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRL 345

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523 1871 DTQVKVRGFRIEPAEVElAIMRQAerqPGLRGAAV--VARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVP 1947
Cdd:cd05940  346 GDTFRWKGENVSTTEVA-AVLGAF---PGVEEANVygVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARP 420
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 469-939 2.34e-09

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: 62.44  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  469 GGTLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVL 548
Cdd:cd05939    1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  549 VDERAATLGESLGEtrvlhlerlPQSTGDLPAANVapgdLAYvIYTSGSTGMPKGVMVEHrsvvNRLNWMQ----RRYPI 624
Cdd:cd05939   81 FNLLDPLLTQSSTE---------PPSQDDVNFRDK----LFY-IYTSGTTGLPKAAVIVH----SRYYRIAagayYAFGM 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  625 GERDVLLQKTPVTFDVSvwelfwwSFTGARLSLLpPGAEKDPREML--RSIQRDAV----TVIHFVPSMLTPfldLLDGD 698
Cdd:cd05939  143 RPEDVVYDCLPLYHSAG-------GIMGVGQALL-HGSTVVIRKKFsaSNFWDDCVkyncTIVQYIGEICRY---LLAQP 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  699 PTARAAASSLRLVFcsGEALAPLQVARFRRLFGDAvRLVNLYGPTEAT---VDVSDHECASD-NPTRVPIGRPIdnlRLY 774
Cdd:cd05939  212 PSEEEQKHNVRLAV--GNGLRPQIWEQFVRRFGIP-QIGEFYGATEGNsslVNIDNHVGACGfNSRILPSVYPI---RLI 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  775 VLDRA------------LRPQPlGAVGELyiggVGVAR---------GYLNRPElNAERFLVDPFVAGGRLYRTGDLARW 833
Cdd:cd05939  286 KVDEDtgelirdsdglcIPCQP-GEPGLL----VGKIIqndplrrfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVM 359

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  834 LADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDsaVRGTH----LVGYYVAAAELDPGQLRAGLSA 909
Cdd:cd05939  360 DELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVE--VPGVEgragMAAIVDPERKVDLDRFSAVLAK 437

                        490       500       510
                 ....*....|....*....|....*....|
gi 15598523  910 TLPDFMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:cd05939  438 SLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 471-851 2.71e-09

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: 62.47  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAG-VRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLV 549
Cdd:cd17632   67 TITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  550 DERA-----ATLGESLGETRVLHLERLPQST------------------------------GDLPAANVAPGD-----LA 589
Cdd:cd17632  147 SAEHldlavEAVLEGGTPPRLVVFDHRPEVDahraalesarerlaavgipvttltliavrgRDLPPAPLFRPEpdddpLA 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  590 YVIYTSGSTGMPKGVMVEHRSVVN---RLNWMQRRYPIGErdVLLQKTPVtfdvsvwelfwwSFTGARLSL---LPPG-- 661
Cdd:cd17632  227 LLIYTSGSTGTPKGAMYTERLVATfwlKVSSIQDIRPPAS--ITLNFMPM------------SHIAGRISLygtLARGgt 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  662 ----AEKDPREMLRSIQRDAVTVIHFVPS----MLTPFLDLL--------DGDPTARAAASSLR---------LVFCSGE 716
Cdd:cd17632  293 ayfaAASDMSTLFDDLALVRPTELFLVPRvcdmLFQRYQAELdrrsvagaDAETLAERVKAELRervlggrllAAVCGSA 372

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  717 ALAPLQVARFRRLFGdaVRLVNLYGPTEATVDVSDHEcasdnptrvpIGRPidnlrlYVLDRAL------------RPQP 784
Cdd:cd17632  373 PLSAEMKAFMESLLD--LDLHDGYGSTEAGAVILDGV----------IVRP------PVLDYKLvdvpelgyfrtdRPHP 434

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523  785 LgavGELYIGGVGVARGYLNRPELNAERFLVDPFvaggrlYRTGDLARWLADGNLEYLGRADDQVKI 851
Cdd:cd17632  435 R---GELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKL 492
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 2071-2179 4.50e-09

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 58.86  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2071 RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAV--LEDIAASYLAAIRRVQPEgPYYLGGW 2148
Cdd:COG0596   18 EAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGytLDDLADDLAALLDALGLE-RVVLVGH 96

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15598523 2149 SFGGFVAYEMARQLraldPQAVAQLIVLDSI 2179
Cdd:COG0596   97 SMGGMVALELAARH----PERVAGLVLVDEV 123
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1067-1339 6.54e-09

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: 60.90  E-value: 6.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1067 PDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGAsEPLQLVHTQARSEPlilDLRGNPEAGTVLDEHI 1146
Cdd:cd19540   19 GPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDG-GPYQVVLPAAEARP---DLTVVDVTEDELAARL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1147 RQRRFHRYSLQQpGLFLFAAFVREDGLD--LVFSFHHAILDGWSVANLIVALVAAYR----GEPlPGPAPaLAchV---- 1216
Cdd:cd19540   95 AEAARRGFDLTA-ELPLRARLFRLGPDEhvLVLVVHHIAADGWSMAPLARDLATAYAarraGRA-PDWAP-LP--Vqyad 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1217 -----REELAALASPAAV-----GYWTGLLEGA-RMTRLDGFGAHEPQAAQGPASHREALPDGLLERLKATAAQRGLPLK 1285
Cdd:cd19540  170 yalwqRELLGDEDDPDSLaarqlAYWRETLAGLpEELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALAREHGATLF 249

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15598523 1286 SLLLAAHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIAG 1339
Cdd:cd19540  250 MVLHAALAVLLSRLGAGDDIPIGTPVAGRGD-EALDDLVGMFVNTLVLRTDVSG 302
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1471-1891 8.53e-09

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 60.84  E-value: 8.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1471 PEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAigVAL---NRSPEMIAtIWGIL 1546
Cdd:PRK08974   19 PDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDR--VALmmpNLLQYPIA-LFGIL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1547 RAGLVCVPLDVSYPAQRL------------------ALILEtaqpfRVVAHPEHAHV---------AAAERVLP------ 1593
Cdd:PRK08974   96 RAGMIVVNVNPLYTPRELehqlndsgakaivivsnfAHTLE-----KVVFKTPVKHViltrmgdqlSTAKGTLVnfvvky 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1594 VEELVADIE-PET--------------FAAPQL--DELAMLLFTSGSTGRPKGVELSHR-MWANYTQwqlrvASGV--PG 1653
Cdd:PRK08974  171 IKRLVPKYHlPDAisfrsalhkgrrmqYVKPELvpEDLAFLQYTGGTTGVAKGAMLTHRnMLANLEQ-----AKAAygPL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1654 LRTLQ------------FAPLSFDMAFQEIfstlcgGGELQLISNRErmDPSALLHVLERRqvqrvllPFVALQRLAEAS 1721
Cdd:PRK08974  246 LHPGKelvvtalplyhiFALTVNCLLFIEL------GGQNLLITNPR--DIPGFVKELKKY-------PFTAITGVNTLF 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1722 NAL-------GVRPGALRVVVSSGeqLRITEDVRAFCAAMPGLLLENQYGPTE--------THQVTYHSLSgdpahypdl 1786
Cdd:PRK08974  311 NALlnneefqELDFSSLKLSVGGG--MAVQQAVAERWVKLTGQYLLEGYGLTEcsplvsvnPYDLDYYSGS--------- 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1787 ppIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAErFVEHPWrpgarlYRTGDLGRILGNGEIVW 1866
Cdd:PRK08974  380 --IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGW------LATGDIAVMDEEGFLRI 450

                         490       500
                  ....*....|....*....|....*
gi 15598523  1867 LGRADTQVKVRGFRIEPAEVELAIM 1891
Cdd:PRK08974  451 VDRKKDMILVSGFNVYPNEIEDVVM 475
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 1784-1970 1.08e-08

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: 60.36  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1784 PDLP----PIGRPLDGVEVQVLDAALRPVpVGVTGEL-----------YFGGDCLARGYHRApkltaeRFVEHP--WRpg 1846
Cdd:cd05943  417 PLLPvyrgEIQCRGLGMAVEAFDEEGKPV-WGEKGELvctkpfpsmpvGFWNDPDGSRYRAA------YFAKYPgvWA-- 487

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1847 arlyrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEvelaIMRQAERQPGLRGAAVVARERQGNDAFLAAFL-LGEP 1925
Cdd:cd05943  488 -----HGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAE----IYRVVEKIPEVEDSLVVGQEWKDGDERVILFVkLREG 558

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15598523 1926 EAVDLA---ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 1970
Cdd:cd05943  559 VELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVK 606
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 1612-1875 1.11e-08

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: 60.31  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1612 DELAMLLFTSGSTGRPKGVELSHRmwaNYTQWQLRVASGVPGL-----RTLQFAPLS--FDMAFQEIF----STLCGGGE 1680
Cdd:cd17639   88 DDLACIMYTSGSTGNPKGVMLTHG---NLVAGIAGLGDRVPELlgpddRYLAYLPLAhiFELAAENVClyrgGTIGYGSP 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1681 LQLISNR-----------------------ERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALG-----------V 1726
Cdd:cd17639  165 RTLTDKSkrgckgdltefkptlmvgvpaiwDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGtplldelvfkkV 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1727 RP---GALRVVVSSGEQLriTEDVRAF-----CAAMPGlllenqYGPTEThqvtyhSLSGDPAHYPDLPP--IGRPLDGV 1796
Cdd:cd17639  245 RAalgGRLRYMLSGGAPL--SADTQEFlnivlCPVIQG------YGLTET------CAGGTVQDPGDLETgrVGPPLPCC 310

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1797 EVQVLD------AALRPVPvgvTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRA 1870
Cdd:cd17639  311 EIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKTKEAFDGDGW------FHTGDIGEFHPDGTLKIIDRK 381


                 ....*
gi 15598523 1871 DTQVK 1875
Cdd:cd17639  382 KDLVK 386
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 3-522 1.24e-08

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 60.66  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    3 RFARLPLSPYQR------DIWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWLD 76
Cdd:COG3321  859 RRVPLPTYPFQRedaaaaLLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAA 938

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   77 TDAEFEARHVDLRADRDPEAAVRSWLRDAFRHAYPLDGRSLVDLALLHSDQALYVYVRTHHIVSDAWGLQLFLSRVRAGY 156
Cdd:COG3321  939 AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAA 1018

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  157 LGELGEPQAQMPTASLLAQLETDDYSGSEQYRGDRAYFAEALEGLEPALFTRRRPAGLRRTARHRLTLERTLLDAIRDRG 236
Cdd:COG3321 1019 AALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALA 1098

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  237 ESPFLFLSAAVALYLARIHQNDDVVLGVPVLNRADRAAKQVVGHFANTLPLRIRTAPEQTVDEFLAQLREATRTLLRHQK 316
Cdd:COG3321 1099 LAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALA 1178

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  317 MPLGDLLRGASPLFDTTLSYMRWPAAQAIPNASVETVAQTHAHDPDALAIWVSEFDGHSDAQVDFEYACDVFDADFPMDA 396
Cdd:COG3321 1179 LALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAA 1258

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  397 AARHIETFLRALVEGGERRLGELDPLSAAEREELIHTRNATDQAFPEQATLPTLFAEQVARTPQRTALLEADGGTLSYAE 476
Cdd:COG3321 1259 LAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVA 1338

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 15598523  477 LDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGA 522
Cdd:COG3321 1339 AALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 1500-1857 1.46e-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: 60.14  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1500 RWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQ-----RLALILETAQPF 1574
Cdd:cd05921   25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMsqdlaKLKHLFELLKPG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1575 RVVA----------------HPEHAHV---AAAERVLPVEELVADIE----PETFAAPQLDELAMLLFTSGSTGRPKGVE 1631
Cdd:cd05921  105 LVFAqdaapfaralaaifplGTPLVVSrnaVAGRGAISFAELAATPPtaavDAAFAAVGPDTVAKFLFTSGSTGLPKAVI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1632 LSHRMWANyTQWQLRVASGVPG---LRTLQFAPLSFDMAFQEIFS-TLCGGGEL-------------QLISNRERMDPSA 1694
Cdd:cd05921  185 NTQRMLCA-NQAMLEQTYPFFGeepPVLVDWLPWNHTFGGNHNFNlVLYNGGTLyiddgkpmpggfeETLRNLREISPTV 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1695 LLHV----------------LERRQVQRVLLPFVALQRLA----EASNALGVRPGALRVVVSSGeqlritedvrafcaam 1754
Cdd:cd05921  264 YFNVpagwemlvaalekdeaLRRRFFKRLKLMFYAGAGLSqdvwDRLQALAVATVGERIPMMAG---------------- 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1755 pglllenqYGPTETHQVTY--HSLSGDPAHypdlppIGRPLDGVEVQVldaalrpVPVGVTGELYFGGDCLARGYHRAPK 1832
Cdd:cd05921  328 --------LGATETAPTATftHWPTERSGL------IGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPE 386

                        410       420
                 ....*....|....*....|....*
gi 15598523 1833 LTAERFVEHPWrpgarlYRTGDLGR 1857
Cdd:cd05921  387 LTAQAFDEEGF------YCLGDAAK 405
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 1586-1857 5.64e-08

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 58.35  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1586 AAAERVLPVEELVADIEP----ETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMW-ANytQWQLRVASGVPGLRT---L 1657
Cdd:PRK08180  179 VPGRAATPFAALLATPPTaavdAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLcAN--QQMLAQTFPFLAEEPpvlV 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1658 QFAPLSFDMAFQEIFS-TLCGGGEL-------------QLISNRERMDP----------SALLHVLERRQV------QRV 1707
Cdd:PRK08180  257 DWLPWNHTFGGNHNLGiVLYNGGTLyiddgkptpggfdETLRNLREISPtvyfnvpkgwEMLVPALERDAAlrrrffSRL 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1708 LLPFVA-----------LQRLAEAsnalgvrpgalrvvvSSGEQLRitedvraFCAAmpglllenqYGPTEThqvtyhSL 1776
Cdd:PRK08180  337 KLLFYAgaalsqdvwdrLDRVAEA---------------TCGERIR-------MMTG---------LGMTET------AP 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1777 SGDPAHYPDLPP--IGRPLDGVEVQVldaalrpVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGD 1854
Cdd:PRK08180  380 SATFTTGPLSRAgnIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGD 446


                  ...
gi 15598523  1855 LGR 1857
Cdd:PRK08180  447 AVR 449
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 1480-1876 1.52e-07

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 56.75  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1480 LFERQVEALPGSAALAFEE--------QRW-TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGL 1550
Cdd:PLN02430   47 IFSKSVEKYPDNKMLGWRRivdgkvgpYMWkTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1551 VCVPLDVSYPAQRLALILETAQ-PFRVVAHPE-----HAHVAAAERVL-------PVEEL---VADI------------- 1601
Cdd:PLN02430  127 ICVPLYDTLGPGAVDYIVDHAEiDFVFVQDKKikellEPDCKSAKRLKaivsftsVTEEEsdkASQIgvktyswidflhm 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1602 ---EPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRmwanytqwqlRVASGVPGLRT---------------LQFAPLS 1663
Cdd:PLN02430  207 gkeNPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHE----------AVATFVRGVDLfmeqfedkmthddvyLSFLPLA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1664 --FDMAFQEIF-------------------------STLCGG-------------GELQLISNRERMDPSAL----LHVL 1699
Cdd:PLN02430  277 hiLDRMIEEYFfrkgasvgyyhgdlnalrddlmelkPTLLAGvprvferihegiqKALQELNPRRRLIFNALykykLAWM 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1700 ERRQVQRVLLPFVALQRLAEASNALGvrpGALRVVVSSGEQL--RITEDVRAFCAAmpglLLENQYGPTEThqvtyhsLS 1777
Cdd:PLN02430  357 NRGYSHKKASPMADFLAFRKVKAKLG---GRLRLLISGGAPLstEIEEFLRVTSCA----FVVQGYGLTET-------LG 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1778 GDPAHYPD----LPPIGRPLDGVEV---QVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAErFVEHPWrpgarlY 1850
Cdd:PLN02430  423 PTTLGFPDemcmLGTVGAPAVYNELrleEVPEMGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEE-VMKDGW------F 495

                         490       500
                  ....*....|....*....|....*.
gi 15598523  1851 RTGDLGRILGNGEIVWLGRADTQVKV 1876
Cdd:PLN02430  496 HTGDIGEILPNGVLKIIDRKKNLIKL 521
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 1846-1963 1.53e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 56.20  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1846 GARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV------VARERqgndafLAA 1919
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVML----RLPGVQEAVVyrgkdpVAGER------VKA 358

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15598523  1920 FLLGEpEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK08308  359 KVISH-EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGK 401
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1991-2058 5.12e-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: 49.56  E-value: 5.12e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598523    1991 RTLAGLLGeLLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRER 2058
Cdd:smart00823   19 EQVAAVLG-HAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 471-613 5.29e-07

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: 55.05  E-value: 5.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALR-AAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLV 549
Cdd:cd05905   14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  550 DE--------------RAATLGESLGETRVLHLERLPQSTGDLPAANVAP-----GDLAYVIYTSGSTGMPKGVMVEHRS 610
Cdd:cd05905   94 VEaclkglpkkllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHpptrdGDTAYIEYSFSSDGSLSGVAVSHSS 173


                 ...
gi 15598523  611 VVN 613
Cdd:cd05905  174 LLA 176
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 1482-1972 6.67e-07

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: 54.63  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1482 ERQVEA-LPGSAALAFE------EQRWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCV 1553
Cdd:cd05967   57 DRHVEAgRGDQIALIYDspvtgtERTYTYAELlDEVSR-LAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1554 PLDVSYPAQRLALILETAQPFRVVA--------------------------HPEH----------AHVAAAERVLPVEEL 1597
Cdd:cd05967  136 VVFGGFAAKELASRIDDAKPKLIVTascgiepgkvvpykplldkalelsghKPHHvlvlnrpqvpADLTKPGRDLDWSEL 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1598 VADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLR----VASG-----------VPGLRTLQFAPL 1662
Cdd:cd05967  216 LAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRniygIKPGdvwwaasdvgwVVGHSYIVYGPL 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1663 sfdmafqeifstLCGGGELQLISNRERM-DPSALLHVLERRQVQRVLLPFVALQRL----AEASNALGVRPGALRVVVSS 1737
Cdd:cd05967  296 ------------LHGATTVLYEGKPVGTpDPGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLFLA 363

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1738 GEqlRITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELY 1817
Cdd:cd05967  364 GE--RLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIV 441

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1818 FGG----DCLARGYhrapkLTAERFVEHPWR--PGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIM 1891
Cdd:cd05967  442 IKLplppGCLLTLW-----KNDERFKKLYLSkfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1892 rqaeRQPGLRGAAVVARErqgnDAF-----LAAFLLGEPEAVDLAELKQALRSELPEHMVP----AHFAWVDGFALTPSG 1962
Cdd:cd05967  515 ----SHPAVAECAVVGVR----DELkgqvpLGLVVLKEGVKITAEELEKELVALVREQIGPvaafRLVIFVKRLPKTRSG 586

                        570
                 ....*....|
gi 15598523 1963 KRDDAALRAL 1972
Cdd:cd05967  587 KILRRTLRKI 596
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 1489-1869 7.25e-07

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 54.56  E-value: 7.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1489 PGSAALAF--EEQRW-------TYRDLDHVARCVATRLVRAGARrGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 1559
Cdd:PRK05850   15 PDDAAFTFidYEQDPagvaetlTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1560 PAQ---RLALILETAQPF----------RVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQ-LDELAMLLFTSGSTG 1625
Cdd:PRK05850   94 GGAhdeRVSAVLRDTSPSvvlttsavvdDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRdLPSTAYLQYTSGSTR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1626 RPKGVELSHR-MWANYTQWQ---LRVASGVP--GLRTLQFAPLSFDMAF-QEIFSTLCGGGELQLISnrermdPSALLhv 1698
Cdd:PRK05850  174 TPAGVMVSHRnVIANFEQLMsdyFGDTGGVPppDTTVVSWLPFYHDMGLvLGVCAPILGGCPAVLTS------PVAFL-- 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1699 lerrqvQRvllPFVALQRLAEASNA----------LGVRP-----------GALRVVVSSGEQL------RITEDVRAFc 1751
Cdd:PRK05850  246 ------QR---PARWMQLLASNPHAfsaapnfafeLAVRKtsdddmagldlGGVLGIISGSERVhpatlkRFADRFAPF- 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1752 aAMPGLLLENQYG---------------PTETHQVTYHSLSGDPAHyPDLPPIGRPL------DGVEVQVLDA-ALRPVP 1809
Cdd:PRK05850  316 -NLRETAIRPSYGlaeatvyvatrepgqPPESVRFDYEKLSAGHAK-RCETGGGTPLvsygspRSPTVRIVDPdTCIECP 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523  1810 VGVTGELYFGGDCLARGYHRAPKLTAERF-----------VEHPWrpgarlYRTGDLGRILGnGEIVWLGR 1869
Cdd:PRK05850  394 AGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtPEGPW------LRTGDLGFISE-GELFIVGR 457
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 1490-1876 9.58e-07

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 54.05  E-value: 9.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1490 GSAALAFEEQ--RWTYRDLDHVARCVATRLVRAGarrGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI 1567
Cdd:PRK06334   33 TTATVCWDEQlgKLSYNQVRKAVIALATKVSKYP---DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTAC 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1568 LE--------TAQPFrvVAHPEHAHVAAAE---------------------RV-----LPVEEL-----VADIEPEtfaa 1608
Cdd:PRK06334  110 ANlvgvthvlTSKQL--MQHLAQTHGEDAEypfsliymeevrkelsfwekcRIgiymsIPFEWLmrwfgVSDKDPE---- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1609 pqldELAMLLFTSGSTGRPKGVELSHrmwANYTQWQ---LRVASGVPGLRTLQFAPLSFDMAFQ--EIFSTLCGggeLQL 1683
Cdd:PRK06334  184 ----DVAVILFTSGTEKLPKGVPLTH---ANLLANQracLKFFSPKEDDVMMSFLPPFHAYGFNscTLFPLLSG---VPV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1684 ISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRIT---EDVRAFcaamPGLLLE 1760
Cdd:PRK06334  254 VFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSlyqEALKTF----PHIQLR 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1761 NQYGPTETHQVTYHSLSGDPAHYPdlpPIGRPLDGVEVQVLDAALR-PVPVGVTGELYFGGDCLARGYHRAPKltAERFV 1839
Cdd:PRK06334  330 QGYGTTECSPVITINTVNSPKHES---CVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFV 404

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 15598523  1840 EhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKV 1876
Cdd:PRK06334  405 E---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 1500-1635 1.11e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 53.94  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1500 RWTYRDLDHVARCVATRLVRAGARRGDAIG-VALN--RSPEMiatIWGILRAGLVCVPLDVSYPAQRLALILETAQ---- 1572
Cdd:PRK07008   39 RYTYRDCERRAKQLAQALAALGVEPGDRVGtLAWNgyRHLEA---YYGVSGSGAVCHTINPRLFPEQIAYIVNHAEdryv 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1573 -------PFRVVAHP------------EHAHV-AAAERVLPVEELVaDIEPETFAAPQLDE--LAMLLFTSGSTGRPKGV 1630
Cdd:PRK07008  116 lfdltflPLVDALAPqcpnvkgwvamtDAAHLpAGSTPLLCYETLV-GAQDGDYDWPRFDEnqASSLCYTSGTTGNPKGA 194


                  ....*
gi 15598523  1631 ELSHR 1635
Cdd:PRK07008  195 LYSHR 199
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 1790-1963 1.16e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 53.99  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1790 GRPLDGVEVQVLDAALRPVPVGVTGELyfggdCLAR----------GYHrapkltaERFVEHPWRPGARLYRTGDLGRIL 1859
Cdd:PRK00174  427 TRPLPGIQPAVVDEEGNPLEGGEGGNL-----VIKDpwpgmmrtiyGDH-------ERFVKTYFSTFKGMYFTGDGARRD 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1860 GNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQ---AErqpglrgAAVVAR--ERQGNDAFlaAFLL---GEPEAVDLA 1931
Cdd:PRK00174  495 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHpkvAE-------AAVVGRpdDIKGQGIY--AFVTlkgGEEPSDELR 565

                         170       180       190
                  ....*....|....*....|....*....|...
gi 15598523  1932 -ELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PRK00174  566 kELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGK 598
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1612-1975 1.25e-06

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: 53.25  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1612 DELAMLLFTSGSTGRPKGVELSHrmwANytqwqlRVASGVPGLRTLQFAPLSFDMAFQEIF----------STLCGGGEL 1681
Cdd:cd05944    2 DDVAAYFHTGGTTGTPKLAQHTH---SN------EVYNAWMLALNSLFDPDDVLLCGLPLFhvngsvvtllTPLASGAHV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1682 QLISNRERMDPSA---LLHVLERRQVQrvllpfvALQRLAEASNALGVRP-----GALRVVVSSGEQLRItEDVRAFCAA 1753
Cdd:cd05944   73 VLAGPAGYRNPGLfdnFWKLVERYRIT-------SLSTVPTVYAALLQVPvnadiSSLRFAMSGAAPLPV-ELRARFEDA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1754 MpGLLLENQYGPTETHQVtyHSLSgdpahYPDLPP----IGRPL--DGVEVQVLDA---ALRPVPVGVTGELYFGGDCLA 1824
Cdd:cd05944  145 T-GLPVVEGYGLTEATCL--VAVN-----PPDGPKrpgsVGLRLpyARVRIKVLDGvgrLLRDCAPDEVGEICVAGPGVF 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1825 RGYhrapkLTAERFVEHPWRPGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAA 1904
Cdd:cd05944  217 GGY-----LYTEGNKNAFVADG--WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALL----RHPAVAFAG 285

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598523 1905 VVARERQGNDAFLAAFLLGEPEA-VDLAELKQALRSELPEH-MVPAHFAWVDGFALTPSGKRDDAALRALPLE 1975
Cdd:cd05944  286 AVGQPDAHAGELPVAYVQLKPGAvVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADAIH 358
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 1496-1638 1.34e-06

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport 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 hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 53.45  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1496 FEEQRWTYRDLDHVARCVATRLVR-AGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPF 1574
Cdd:cd05938    1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1575 RVVAHPEhaHVAAAERVLP---------------------------VEELVADIEPETFAAPQ-LDELAMLLFTSGSTGR 1626
Cdd:cd05938   81 VLVVAPE--LQEAVEEVLPalradgvsvwylshtsntegvislldkVDAASDEPVPASLRAHVtIKSPALYIYTSGTTGL 158

                        170
                 ....*....|...
gi 15598523 1627 PKGVELSH-RMWA 1638
Cdd:cd05938  159 PKAARISHlRVLQ 171
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 471-608 1.41e-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: 53.52  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVD 550
Cdd:cd05933    8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  551 ERAATLGESLGETRVLHLERLPQSTGDLPAA---------------------------NVAPGDLAYVIYTSGSTGMPKG 603
Cdd:cd05933   88 NQKQLQKILQIQDKLPHLKAIIQYKEPLKEKepnlyswdefmelgrsipdeqldaiisSQKPNQCCTLIYTSGTTGMPKG 167


                 ....*
gi 15598523  604 VMVEH 608
Cdd:cd05933  168 VMLSH 172
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 785-1292 1.80e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 53.72  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  785 LGAVGELYIGGVGVARGYLNRPElnaERFLVD----PFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDE 860
Cdd:COG3321  834 LTALAQLWVAGVPVDWSALYPGR---GRRRVPlptyPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLA 910

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  861 VRDRLAALPGVRDAAVVARDSAVRGTHLVGYYVAAAELDPGQLRAGLSATLPDFMLPAFFVRIDSLPLSANGKLDRRQLP 940
Cdd:COG3321  911 LAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAA 990

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  941 APPEQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQRRGLGFELADLMRNPTVAGLAERL 1020
Cdd:COG3321  991 AAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLL 1070

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1021 VRPLAERSYQPFELVSEVDKPRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAY 1100
Cdd:COG3321 1071 LAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAAL 1150

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1101 PALRSSFDLSGASEPLQLVHTQARSEPLILDLRGNPEAGTVLDEHIRQRRFHRYSLQQPGLFLFAAFVREDGLDLVFSFH 1180
Cdd:COG3321 1151 ALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAA 1230

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1181 HAILDGWSVANLIVALVAAYRGEPLPGPAPALACHVREELAALASPAAVGYWTGLLEGARMTRLDGFGAHEPQAAQGPAS 1260
Cdd:COG3321 1231 AALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAA 1310

                        490       500       510
                 ....*....|....*....|....*....|..
gi 15598523 1261 HREALPDGLLERLKATAAQRGLPLKSLLLAAH 1292
Cdd:COG3321 1311 AAAAAAAAAALAAALLAAALAALAAAVAAALA 1342
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 1790-1972 2.07e-06

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 52.69  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1790 GRPLDGVEVQVLDAAlrpvpvgvTGELYFGGDCLARGYHraPKLtaerfvehpwRPGARLYRTGDLGRILGNGEIVWLGR 1869
Cdd:PRK07445  286 GQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQI----------LDSQGIFETDDLGYLDAQGYLHILGR 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1870 ADTQVKVRGFRIEPAEVELAImrqaeRQPGL-RGAAV--VARERQGNdaFLAAFLLGEPEAVDLAELKQALRSELPEHMV 1946
Cdd:PRK07445  346 NSQKIITGGENVYPAEVEAAI-----LATGLvQDVCVlgLPDPHWGE--VVTAIYVPKDPSISLEELKTAIKDQLSPFKQ 418

                         170       180
                  ....*....|....*....|....*.
gi 15598523  1947 PAHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:PRK07445  419 PKHWIPVPQLPRNPQGKINRQQLQQI 444
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 1885-1963 2.96e-06

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: 46.77  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   1885 EVELAIMRQaerqPGLRGAAVVARERQGNDAFLAAFL-LGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:pfam13193    1 EVESALVSH----PAVAEAAVVGVPDELKGEAPVAFVvLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1610-1972 7.17e-06

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 51.25  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1610 QLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQlRVASGVPGLRTLQFAPL--SFDMAFQeIFSTLCGGGELQLIsn 1686
Cdd:PRK08043  363 QPEDAALILFTSGSEGHPKGVVHSHKsLLANVEQIK-TIADFTPNDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLY-- 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1687 rermdPSALLHvlerrqvqRVlLPFVALQR----LAEASNALG-----VRP---GALRVVVSSGEQLriTEDVRAFCAAM 1754
Cdd:PRK08043  439 -----PSPLHY--------RI-VPELVYDRnctvLFGTSTFLGnyarfANPydfARLRYVVAGAEKL--QESTKQLWQDK 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1755 PGLLLENQYGPTETHQVTyhSLSGDPAHYPDlpPIGRPLDGvevqvLDAALRPVPvGVT--GELYFGGDCLARGYHRapk 1832
Cdd:PRK08043  503 FGLRILEGYGVTECAPVV--SINVPMAAKPG--TVGRILPG-----MDARLLSVP-GIEqgGRLQLKGPNIMNGYLR--- 569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1833 ltaerfVEHPWR---PGAR---------LYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE-LAIMRQAERQpg 1899
Cdd:PRK08043  570 ------VEKPGVlevPTAEnargemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEqLALGVSPDKQ-- 641

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598523  1900 lrgAAVVARERQGNDAFLAAFLLgEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:PRK08043  642 ---HATAIKSDASKGEALVLFTT-DSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 1592-1941 1.51e-05

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 49.76  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1592 LPV---EELVADIEPETFAAPQlDELAMLLFTSGSTGRPKGVELSHRMWANytqWQLRVA-----SGV-PGLRtLQFAP- 1661
Cdd:COG1541   61 LPFttkEDLRDNYPFGLFAVPL-EEIVRIHASSGTTGKPTVVGYTRKDLDR---WAELFArslraAGVrPGDR-VQNAFg 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1662 -------LSFDMAFQEIFSTLC--GGGE----LQLIsnrERMDPSALlhvlerrqvqrVLLPFVALqRLAEASNALGVRP 1728
Cdd:COG1541  136 yglftggLGLHYGAERLGATVIpaGGGNterqLRLM---QDFGPTVL-----------VGTPSYLL-YLAEVAEEEGIDP 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1729 GA--LRVVVSSGEqlRITEDVRAFCAAMPGLLLENQYGPTET-HQVTYHSLSGDPAHYPDlppigrplDGVEVQVLD-AA 1804
Cdd:COG1541  201 RDlsLKKGIFGGE--PWSEEMRKEIEERWGIKAYDIYGLTEVgPGVAYECEAQDGLHIWE--------DHFLVEIIDpET 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1805 LRPVPVGVTGELYFggDCLAR-GYhraPKLtaerfvehpwrpgaRlYRTGDLGRIL--------GNGEIV-WLGRADTQV 1874
Cdd:COG1541  271 GEPVPEGEEGELVV--TTLTKeAM---PLI--------------R-YRTGDLTRLLpepcpcgrTHPRIGrILGRADDML 330

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523 1875 KVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGN-DAFLaafLLGEP-EAVDLAELKQALRSEL 1941
Cdd:COG1541  331 IIRGVNVFPSQIEEVLL----RIPEVGPEYQIVVDREGGlDELT---VRVELaPGASLEALAEAIAAAL 392
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1079-1334 3.06e-05

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: 48.72  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1079 RFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGAseplQLVHTQARSEPLILDLRgnpeagtVLDehIRQ---RRFHRYS 1155
Cdd:cd19537   31 RLSGDVDRDRLASAWNTVLARHRILRSRYVPRDG----GLRRSYSSSPPRVQRVD-------TLD--VWKeinRPFDLER 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1156 LQqpglfLFAAFVREDGLDLVFSfhHAILDGWSVANLIVALVAAYRGEPLPGPAP---ALACHVREelaalASPAAVGYW 1232
Cdd:cd19537   98 ED-----PIRVFISPDTLLVVMS--HIICDLTTLQLLLREVSAAYNGKLLPPVRReylDSTAWSRP-----ASPEDLDFW 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1233 TGLLEGARMTRLDGFGAHEpqAAQGpASHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISN 1312
Cdd:cd19537  166 SEYLSGLPLLNLPRRTSSK--SYRG-TSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYL 242

                        250       260
                 ....*....|....*....|..
gi 15598523 1313 GRPElPDADRMVGLFLNTVPVR 1334
Cdd:cd19537  243 NRTS-EEDMETVGLFLEPLPIR 263
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1702-2198 3.98e-05

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 49.10  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1702 RQVQRVLLPFVALQR-----------LAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQ 1770
Cdd:COG3321  856 RGRRRVPLPTYPFQRedaaaallaaaLAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVAL 935

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1771 VTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPKLTAERFVEHPWRPGARLY 1850
Cdd:COG3321  936 AAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAA 1015

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1851 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL 1930
Cdd:COG3321 1016 AAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAAL 1095

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1931 AELKQALRSE--LPEHMVPAHFAWVDGFALTPSGKRDDAALRALPLEHGTNIEYLAPRDDYERTLAGLLGELLDRPRVGI 2008
Cdd:COG3321 1096 ALALAALAAAllLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLL 1175

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2009 RDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRAFDPLVPIRAGGSRPPLFLVHPLGGH 2088
Cdd:COG3321 1176 ALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAAL 1255

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2089 VLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALDPQ 2168
Cdd:COG3321 1256 LAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAA 1335

                        490       500       510
                 ....*....|....*....|....*....|
gi 15598523 2169 AVAQLIVLDSITVDRNHAGSASDEALLLFF 2198
Cdd:COG3321 1336 AVAAALALAAAAAAAAAAAAAAAAAAALAA 1365
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 8-262 5.18e-05

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: 48.40  E-value: 5.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    8 PLSPYQRdiWVAAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTPYQWL--DTDAEFEARH 85
Cdd:cd19534    3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIrgDVEELFRLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   86 VDLRADrDPEAAVRSWLRDAFRHAYPLDGRsLVDLALLH-SDQALYVYVRTHHIVSDA--WglQLFLSRVRAGYLGELGE 162
Cdd:cd19534   81 VDLSSL-AQAAAIEALAAEAQSSLDLEEGP-LLAAALFDgTDGGDRLLLVIHHLVVDGvsW--RILLEDLEAAYEQALAG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  163 PQAQMPT-------ASLLAqletdDYSGSEQYRGDRAYFAEALEGLEPALFTRR-RPAGLRRTARHRLTLERT---LLDA 231
Cdd:cd19534  157 EPIPLPSktsfqtwAELLA-----EYAQSPALLEELAYWRELPAADYWGLPKDPeQTYGDARTVSFTLDEEETealLQEA 231

                        250       260       270
                 ....*....|....*....|....*....|.
gi 15598523  232 IRDRGESPFLFLSAAVALYLARIHQNDDVVL 262
Cdd:cd19534  232 NAAYRTEINDLLLAALALAFQDWTGRAPPAI 262
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 2077-2328 5.92e-05

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 47.11  E-value: 5.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2077 PPLFLVHPLGGHVLCYLPLVRALPPD-QPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQ---PEGPYYLGGWSFGG 2152
Cdd:pfam00561    1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILealGLEKVNLVGHSMGG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2153 FVAYEMArqlrALDPQAVAQLIVLDSItvDRNHAGSASDEALLLFFYWelvWFERSDKEVEPLPEGASLEQKLDHIVERA 2232
Cdd:pfam00561   81 LIALAYA----AKYPDRVKALVLLGAL--DPPHELDEADRFILALFPG---FFDGFVADFAPNPLGRLVAKLLALLLLRL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   2233 IEAGVLPAGTPRATVQRLY---ELFRASWQALIGYRPEVSDQDmtLLRADGPLpLALKPMHDaagtHYGDPKNGWQ--HW 2307
Cdd:pfam00561  152 RLLKALPLLNKRFPSGDYAlakSLVTGALLFIETWSTELRAKF--LGRLDEPT-LIIWGDQD----PLVPPQALEKlaQL 224

                          250       260
                   ....*....|....*....|.
gi 15598523   2308 TSGRLDVIDVPGDHLVLMKEP 2328
Cdd:pfam00561  225 FPNARLVVIPDAGHFAFLEGP 245
PRK03584 PRK03584
acetoacetate--CoA ligase;
441-608 6.20e-05

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 48.25  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   441 FPEqATLPtlFAEQV--ARTPQRTALLEA--DGG--TLSYAELDAKVQAVADALRAAGVRTDERVA--------LLVA-- 504
Cdd:PRK03584   81 FPG-ARLN--YAENLlrHRRDDRPAIIFRgeDGPrrELSWAELRRQVAALAAALRALGVGPGDRVAaylpnipeTVVAml 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   505 ------------------RG---------PHLLPAILGVQRAGGAYvpinpDHpLERVRLLLEDCG--ARVVLVDeraaT 555
Cdd:PRK03584  158 ataslgaiwsscspdfgvQGvldrfgqiePKVLIAVDGYRYGGKAF-----DR-RAKVAELRAALPslEHVVVVP----Y 227

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598523   556 LGESLGETRVLHLERLPQSTGDLPAANVAPGDLA-----YVIYTSGSTGMPK-------GVMVEH 608
Cdd:PRK03584  228 LGPAAAAAALPGALLWEDFLAPAEAAELEFEPVPfdhplWILYSSGTTGLPKcivhghgGILLEH 292
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1085-1339 6.64e-05

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: 48.03  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1085 DEAAFRHALDRVVAAYPALRSSFDLSGaSEPLQLVHTQARSEPLILDLRGNPEAgtvLDEHIRQRRFHRYSLQQPGLFLF 1164
Cdd:cd19538   37 DVQALQQALYDVVERHESLRTVFPEED-GVPYQLILEEDEATPKLEIKEVDEEE---LESEINEAVRYPFDLSEEPPFRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1165 AAFVREDGLD-LVFSFHHAILDGWSVANLIVALVAAYRG---------EPLPGPAPALACHVREELAALASPAA-----V 1229
Cdd:cd19538  113 TLFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRArckgeapelAPLPVQYADYALWQQELLGDESDPDSliarqL 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1230 GYWTGLLEGA-RMTRL--DGFGAHEPQAAQGpaSHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVV 1306
Cdd:cd19538  193 AYWKKQLAGLpDEIELptDYPRPAESSYEGG--TLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIP 270

                        250       260       270
                 ....*....|....*....|....*....|...
gi 15598523 1307 TGAISNGRPELPDADrMVGLFLNTVPVRSEIAG 1339
Cdd:cd19538  271 IGSPVAGRNDDSLED-LVGFFVNTLVLRTDTSG 302
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 473-851 7.60e-05

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 48.09  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   473 SYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAGGAYVPINPDHPLERVRLLLEDCGARVVLVDER 552
Cdd:PLN02614   81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   553 ------------------AATLG----ESLGETRVLHL------ERLPQSTG---DLPAANvaPGDLAYVIYTSGSTGMP 601
Cdd:PLN02614  161 kiselfktcpnsteymktVVSFGgvsrEQKEEAETFGLviyawdEFLKLGEGkqyDLPIKK--KSDICTIMYTSGTTGDP 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   602 KGVMVEHRSVVNRLNWMQR-----RYPIGERDVLLQKTPVT--FDVSVWELFWWsfTGARLSLLppgaEKDPREMLRSIQ 674
Cdd:PLN02614  239 KGVMISNESIVTLIAGVIRllksaNAALTVKDVYLSYLPLAhiFDRVIEECFIQ--HGAAIGFW----RGDVKLLIEDLG 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   675 RDAVTVIHFVPSML------------------------------------------TPFLDLLDGDPTARAAASSLRLVF 712
Cdd:PLN02614  313 ELKPTIFCAVPRVLdrvysglqkklsdggflkkfvfdsafsykfgnmkkgqshveaSPLCDKLVFNKVKQGLGGNVRIIL 392

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   713 cSGEALAPLQVARFRRLFGdAVRLVNLYGPTEAtvdvsdheCASDNPTrVP--------IGRPIDN--LRLYVLDRaLRP 782
Cdd:PLN02614  393 -SGAAPLASHVESFLRVVA-CCHVLQGYGLTES--------CAGTFVS-LPdeldmlgtVGPPVPNvdIRLESVPE-MEY 460

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598523   783 QPLGAV--GELYIGGVGVARGYLNRPELNAERFLvdpfvaGGRLYrTGDLARWLADGNLEYLGRADDQVKI 851
Cdd:PLN02614  461 DALASTprGEICIRGKTLFSGYYKREDLTKEVLI------DGWLH-TGDVGEWQPNGSMKIIDRKKNIFKL 524
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 1612-1869 9.83e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 47.66  E-value: 9.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1612 DELAMLLFTSGSTGRPKGVELSHRmwanytqwqlRVASGVPGL---------------RTLQFAPLSFDMAF--QEIF-- 1672
Cdd:PTZ00216  264 DDLALIMYTSGTTGDPKGVMHTHG----------SLTAGILALedrlndligppeedeTYCSYLPLAHIMEFgvTNIFla 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1673 --STLCGGGELQLISN--RERMD-----PSALLHVLE-----RRQVQRVLLPFVALQR-------------LAEA----- 1720
Cdd:PTZ00216  334 rgALIGFGSPRTLTDTfaRPHGDltefrPVFLIGVPRifdtiKKAVEAKLPPVGSLKRrvfdhayqsrlraLKEGkdtpy 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1721 ------SNALGVRPGALRVVVSSGEQLriTEDVRAFCAAMPGLLLeNQYGPTETHQVTYHSLSGDpahypdLPP--IGRP 1792
Cdd:PTZ00216  414 wnekvfSAPRAVLGGRVRAMLSGGGPL--SAATQEFVNVVFGMVI-QGWGLTETVCCGGIQRTGD------LEPnaVGQL 484

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1793 LDGVEVQVLDA-----ALRPVPvgvTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWL 1867
Cdd:PTZ00216  485 LKGVEMKLLDTeeykhTDTPEP---RGEILLRGPFLFKGYYKQEELTREVLDEDGW------FHTGDVGSIAANGTLRII 555


                  ..
gi 15598523  1868 GR 1869
Cdd:PTZ00216  556 GR 557
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 1590-1887 2.20e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 46.63  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1590 RVLPVEELVAD--IEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGvPGLRTLQFAPLS--F 1664
Cdd:PLN02736  197 EIVTYSKLLAQgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGnLIANVAGSSLSTKFY-PSDVHISYLPLAhiY 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1665 DMAFQeIFSTLCG-------GGELQLISNRERMDPSALLHV--LERRQVQRVLLPFVA----LQRLAEAS-----NAL-- 1724
Cdd:PLN02736  276 ERVNQ-IVMLHYGvavgfyqGDNLKLMDDLAALRPTIFCSVprLYNRIYDGITNAVKEsgglKERLFNAAynakkQALen 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1725 GVRPGAL--RVVVSS-----GEQLR--------ITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGD--PAHypdlp 1787
Cdd:PLN02736  355 GKNPSPMwdRLVFNKikaklGGRVRfmssgaspLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDnlSGH----- 429

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1788 pIGRPLDGVEVQVLD-------AALRPVPvgvTGELYFGGDCLARGYHRAPKLTAERFVEHPWrpgarlYRTGDLGRILG 1860
Cdd:PLN02736  430 -VGSPNPACEVKLVDvpemnytSEDQPYP---RGEICVRGPIIFKGYYKDEVQTREVIDEDGW------LHTGDIGLWLP 499

                         330       340
                  ....*....|....*....|....*...
gi 15598523  1861 NGEIVWLGRADTQVKV-RGFRIEPAEVE 1887
Cdd:PLN02736  500 GGRLKIIDRKKNIFKLaQGEYIAPEKIE 527
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 921-1468 2.52e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 46.40  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  921 VRIDSLPLSANGKLDRRQLPAPP--EQVAAVAPRTATEAELAAVWADVLGVAEVGVHDDFYALGGDSILMLRIRAAAQRR 998
Cdd:COG3321  845 VPVDWSALYPGRGRRRVPLPTYPfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAA 924

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  999 GLGFELADLMRNPTVAGLAERLVRPLAERSYQPFELVSEVDKPRLEGLEDAFPTSRLSLGLLFHSRQRPDSSVYHDVFHY 1078
Cdd:COG3321  925 ALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALAL 1004

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1079 RFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASEPLQLVHTQARsepLILDLRGNPEAGTVLDEHIRQRRFHRYSLQQ 1158
Cdd:COG3321 1005 LAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAA---LAAAAAAAAALALALAALLLLAALAELALAA 1081

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1159 PGLFLFAAFVREDGLDLVFSFHHAILDGWSVANLIVALVAAYRGEPLPGPAPALACHVREELAALASPAAVGYWTGLLEG 1238
Cdd:COG3321 1082 AALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAA 1161

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1239 ARMTRLDGFGAHEPQAAQGPASHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPELP 1318
Cdd:COG3321 1162 ALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAA 1241

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1319 DADRMVGLFLNTVPVRSEIAgcswiEVADALFRQERDGHAHRRYPLSAIQQIVGDELSSAFNYVNLHVLEPLWQLRDFRV 1398
Cdd:COG3321 1242 AAAVAALAAAAAALLAALAA-----LALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAA 1316

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1399 WEETNFALLVNVIATPSDGMYLRIDSDGRGISRSQAALIGATFVELLWRLADHPDEAADFAFLAPRRDAA 1468
Cdd:COG3321 1317 AAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1580-1972 3.15e-04

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 45.93  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1580 PEHAHVAAAERVLpveelvaDIEPETFAAPQLDE--LAMLLFTSGSTGRPKGVELSHRmwANYTQWQlrvasgvpGLRTL 1657
Cdd:PRK05620  154 PEGIKVYSYEALL-------DGRSTVYDWPELDEttAAAICYSTGTTGAPKGVVYSHR--SLYLQSL--------SLRTT 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1658 QFAPLSFDMAFQ---EIFSTLCGGGELQ-------LISNRERMDPSALLHVLErrqvqrvllpfVALQRLAEASNALGVR 1727
Cdd:PRK05620  217 DSLAVTHGESFLccvPIYHVLSWGVPLAafmsgtpLVFPGPDLSAPTLAKIIA-----------TAMPRVAHGVPTLWIQ 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1728 pgaLRV--VVSSGEQLRITEdVRAFCAAMPGLLL---ENQYGPTETH--QVTYHSLSGDPAHypdlPPIG---------- 1790
Cdd:PRK05620  286 ---LMVhyLKNPPERMSLQE-IYVGGSAVPPILIkawEERYGVDVVHvwGMTETSPVGTVAR----PPSGvsgearwayr 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1791 ----RPLDGVEV------QVLDAALRPvpvgvTGELYFGGDCLARGYHRAPKLT----AERFVEHPWRPGARLY------ 1850
Cdd:PRK05620  358 vsqgRFPASLEYrivndgQVMESTDRN-----EGEIQVRGNWVTASYYHSPTEEgggaASTFRGEDVEDANDRFtadgwl 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1851 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQaerqPGLRGAAVVA-RERQGNDAFLAAFLLG---EPE 1926
Cdd:PRK05620  433 RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAA----PEVVECAVIGyPDDKWGERPLAVTVLApgiEPT 508

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 15598523  1927 AVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 1972
Cdd:PRK05620  509 RETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQH 554
prpE PRK10524
propionyl-CoA synthetase; Provisional
 471-945 5.68e-04

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 45.32  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGVQRAG-------GAYVpinpDHPL-------ERVR 536
Cdd:PRK10524   84 TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihsvvfGGFA----SHSLaariddaKPVL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   537 LLLEDCGAR---VV----LVDErAATLGESLGEtRVLHLERlpqstGDLPAANVAPGDL--------------------- 588
Cdd:PRK10524  160 IVSADAGSRggkVVpykpLLDE-AIALAQHKPR-HVLLVDR-----GLAPMARVAGRDVdyatlraqhlgarvpvewles 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   589 ---AYVIYTSGSTGMPKGVmvehrsvvnrlnwmqrrypigERDV------LLQKTPVTFDVSVWELFW------W----S 649
Cdd:PRK10524  233 nepSYILYTSGTTGKPKGV---------------------QRDTggyavaLATSMDTIFGGKAGETFFcasdigWvvghS 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   650 FT------GARLSLLPPG--AEKDPREMLRSIQRDAVTVIHFVPsmlTPFLDLLDGDPT--ARAAASSLRLVFCSGEala 719
Cdd:PRK10524  292 YIvyapllAGMATIMYEGlpTRPDAGIWWRIVEKYKVNRMFSAP---TAIRVLKKQDPAllRKHDLSSLRALFLAGE--- 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   720 PLQ--VARFrrlFGDA--VRLVNLYGPTEATVDV-SDHECASDNPTRV--PiGRPIDNLRLYVLDRAlRPQPLGAvGEly 792
Cdd:PRK10524  366 PLDepTASW---ISEAlgVPVIDNYWQTETGWPIlAIARGVEDRPTRLgsP-GVPMYGYNVKLLNEV-TGEPCGP-NE-- 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   793 iGGVGVARGYLNRPEL-----NAERFLVDPFVAGGRL-YRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLA 866
Cdd:PRK10524  438 -KGVLVIEGPLPPGCMqtvwgDDDRFVKTYWSLFGRQvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESIS 516

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   867 ALPGVRDAAVVARDSAVRGTHLVGYYVA--AAELDPGQLRAGLSA--------TLPDFMLPAFFVRIDSLPLSANGKLDR 936
Cdd:PRK10524  517 SHPAVAEVAVVGVKDALKGQVAVAFVVPkdSDSLADREARLALEKeimalvdsQLGAVARPARVWFVSALPKTRSGKLLR 596


                  ....*....
gi 15598523   937 RQLPAPPEQ 945
Cdd:PRK10524  597 RAIQAIAEG 605
PLN02654 PLN02654
acetate-CoA ligase
 1836-1963 5.69e-04

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 45.27  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  1836 ERFVEHPWRPGARLYRTGDLGRILGNGeIVWL-GRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARER---- 1910
Cdd:PLN02654  501 ERYETTYFKPFAGYYFSGDGCSRDKDG-YYWLtGRVDDVINVSGHRIGTAEVESALV----SHPQCAEAAVVGIEHevkg 575

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15598523  1911 QGNDAFLaAFLLGEPEAVDL-AELKQALRSELPEHMVPAHFAWVDGFALTPSGK 1963
Cdd:PLN02654  576 QGIYAFV-TLVEGVPYSEELrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGK 628
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
2072-2178 5.89e-04

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 43.84  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 2072 AGGSRPPLFLVHPLGGHVLCYLPLVRALP--------PDQPVYALQAAGTGQGSTPLAVLEDIAAsyLAAIRRVQPEGPY 2143
Cdd:COG2267   24 AGSPRGTVVLVHGLGEHSGRYAELAEALAaagyavlaFDLRGHGRSDGPRGHVDSFDDYVDDLRA--ALDALRARPGLPV 101

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15598523 2144 YLGGWSFGGFVAYEMArqlrALDPQAVAQLIVLDS 2178
Cdd:COG2267  102 VLLGHSMGGLIALLYA----ARYPDRVAGLVLLAP 132
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 585-612 8.48e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 44.70  E-value: 8.48e-04
                          10        20
                  ....*....|....*....|....*...
gi 15598523   585 PGDLAYVIYTSGSTGMPKGVMVEHRSVV 612
Cdd:PLN02736  220 PEDVATICYTSGTTGTPKGVVLTHGNLI 247
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 943-1022 1.02e-03

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: 39.93  E-value: 1.02e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     943 PEQVAAVAPRTATEAELAAVWADVLGVA---EVGVHDDFYALGGDSILMLRIRAAAQRR-GLGFELADLMRNPTVAGLAE 1018
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAE 80


                    ....
gi 15598523    1019 RLVR 1022
Cdd:smart00823   81 HLAA 84
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 471-621 1.13e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 44.20  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   471 TLSYAELDAKVQAVADALRAAGVRTDERVALLVARGPHLLPAILGV--QRAGGAYVPINpdhplervrlLLED------- 541
Cdd:PTZ00216  121 YITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsQSMVAATVYAN----------LGEDalayalr 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   542 --------CGARVVLVDERAATLGEsLGETRVLHLERLPQST----------------GDLPAANVAPG------DLAYV 591
Cdd:PTZ00216  191 eteckaivCNGKNVPNLLRLMKSGG-MPNTTIIYLDSLPASVdtegcrlvawtdvvakGHSAGSHHPLNipenndDLALI 269

                         170       180       190
                  ....*....|....*....|....*....|
gi 15598523   592 IYTSGSTGMPKGVMVEHRSVVNRLNWMQRR 621
Cdd:PTZ00216  270 MYTSGTTGDPKGVMHTHGSLTAGILALEDR 299
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1063-1339 1.43e-03

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: 43.62  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1063 SRQRPDSSVYHDVFHYRFDLAWDEAAFRHALDRVVAAYPALRSSFDLSGASePLQLVHTQARSEPlilDLRGNPEAGTVL 1142
Cdd:cd19546   18 ARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGD-VHQRILDADAARP---ELPVVPATEEEL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1143 DEHIRQRRFHRYSLQQPGLF---LFAAFVREDGLDLVFsfHHAILDGWSVANLIVALVAAY--RGE-------PLPGPAP 1210
Cdd:cd19546   94 PALLADRAAHLFDLTRETPWrctLFALSDTEHVLLLVV--HRIAADDESLDVLVRDLAAAYgaRREgraperaPLPLQFA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1211 ALACHVREELAALASPAAV-----GYWTGLLEGARMTRLDGFGAHEPQAAqgpaSHRE-----ALPDGLLERLKATAAQR 1280
Cdd:cd19546  172 DYALWERELLAGEDDRDSLigdqiAYWRDALAGAPDELELPTDRPRPVLP----SRRAgavplRLDAEVHARLMEAAESA 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15598523 1281 GLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPELPDADRMVGLFLNTVPVRSEIAG 1339
Cdd:cd19546  248 GATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEGDLEGMVGPFARPLALRTDLSG 306
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1207-1760 1.44e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.09  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1207 GPAPALACHVREELAALASPAAV-----------------------GY---WTGLLEGARMTRLD----GFGAHEPQAAQ 1256
Cdd:COG3321  798 GPGPVLTGLVRQCLAAAGDAVVLpslrrgedelaqlltalaqlwvaGVpvdWSALYPGRGRRRVPlptyPFQREDAAAAL 877

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1257 GPASHREALPDGLLERLKATAAQRGLPLKSLLLAAHCLTLHLFSRSDSVVTGAISNGRPELPDADRMVGLFLNTVPVRSE 1336
Cdd:COG3321  878 LAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALA 957

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1337 IAGCSWIEVADALFRQERDGHAHRRYPLSAIQQIVGDELSSAFNYVNLHVLEPLWQLRDFRVWEETNFALLVNVIATPSD 1416
Cdd:COG3321  958 AAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAA 1037

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1417 GMYLRIDSDGRGISRSQAALIGATFVELLWRLADHPDEAADFAFLAPRRDAASQPEPLVDVVSLFERQVEALPGSAALAF 1496
Cdd:COG3321 1038 AAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALAL 1117

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1497 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRV 1576
Cdd:COG3321 1118 AAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLL 1197

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1577 VAHPEHAHVAAAERVLPVEELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRT 1656
Cdd:COG3321 1198 AALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAA 1277

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1657 LQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVS 1736
Cdd:COG3321 1278 AAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAA 1357

                        570       580
                 ....*....|....*....|....
gi 15598523 1737 SGEQLRITEDVRAFCAAMPGLLLE 1760
Cdd:COG3321 1358 AAAAALAAAAGAAAAAAALALAAL 1381
PLN03051 PLN03051
acyl-activating enzyme; Provisional
 572-939 2.05e-03

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 43.27  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   572 PQSTGDLPAANVAPGD-LAYVIYTSGSTGMPKGVMVEHRSVVNRLNWMQRRYPIGERDVLLQKTPVTFDVSVWELFWWSF 650
Cdd:PLN03051  104 GSVGGNEYSPVYAPVEsVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPWLLYSAFL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   651 TGARLSLLppGAEKDPREMLRSIQRDAVTVIHFVPSMLTPFLDLLDGDpTARAAASSLRlVFCS-GEALAPLQVARFRRL 729
Cdd:PLN03051  184 NGATLALY--GGAPLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAFA-MEGLDWSKLR-VFAStGEASAVDDVLWLSSV 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   730 FGDAVRLVNLYGPTE-ATVDVSD---HECASDNPTRVPIGRpidnlRLYVLDRALRPQPlgaVGELYIGGVGVARGYLNR 805
Cdd:PLN03051  260 RGYYKPVIEYCGGTElASGYISStllQPQAPGAFSTASLGT-----RFVLLNDNGVPYP---DDQPCVGEVALAPPMLGA 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   806 PE--LNAERFLV----DPF--VAGGRLYRTGDLARWLADGNLEYLGRADDQVK---IRGNRVEPDEVRDRLAAlpGVRDA 874
Cdd:PLN03051  332 SDrlLNADHDKVyykgMPMygSKGMPLRRHGDIMKRTPGGYFCVQGRADDTMNlggIKTSSVEIERACDRAVA--GIAET 409

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598523   875 AVVARDSAVRGTHLVGYYVAAAEL-------DPGQLRAGLSATLPDFMLPAF---FVRID-SLPLSANGKLDRRQL 939
Cdd:PLN03051  410 AAVGVAPPDGGPELLVIFLVLGEEkkgfdqaRPEALQKKFQEAIQTNLNPLFkvsRVKIVpELPRNASNKLLRRVL 485
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 825-939 2.18e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 43.21  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   825 YRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVGYYV--AAAELDPgQ 902
Cdd:PRK00174  485 YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkGGEEPSD-E 563

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15598523   903 LRAGLSATL---------PDFMlpaFFVriDSLPLSANGKLDRRQL 939
Cdd:PRK00174  564 LRKELRNWVrkeigpiakPDVI---QFA--PGLPKTRSGKIMRRIL 604
PLN02654 PLN02654
acetate-CoA ligase
 811-939 2.54e-03

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 42.96  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   811 ERFLVDPFVAGGRLYRTGDLARWLADGNLEYLGRADDQVKIRGNRVEPDEVRDRLAALPGVRDAAVVARDSAVRGTHLVG 890
Cdd:PLN02654  501 ERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYA 580

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15598523   891 yYVAAAELDP--GQLRAGLSATLPD----FMLPAFFVRIDSLPLSANGKLDRRQL 939
Cdd:PLN02654  581 -FVTLVEGVPysEELRKSLILTVRNqigaFAAPDKIHWAPGLPKTRSGKIMRRIL 634
PRK12316 PRK12316
peptide synthase; Provisional
 8-309 2.76e-03

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 43.41  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523     8 PLSPYQRDIWvaAAQFPELDQYTIFSYDRFTGEVDTQALERALLQAARDTEAFRLRLGETDGTpyqWLDTDAEFEARH-V 86
Cdd:PRK12316 3640 LLLPIQQQFF--EEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGG---WTAEHLPVELGGaL 3714

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523    87 DLRADRDPEAAVRSWLRDAFRHAYPLDG---RSLVdLALLHSDQALYVYVrtHHIVSDAWGLQLFLSRVRAGYLGELgep 163
Cdd:PRK12316 3715 LWRAELDDAEELERLGEEAQRSLDLADGpllRALL-ATLADGSQRLLLVI--HHLVVDGVSWRILLEDLQQAYQQLL--- 3788

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   164 QAQMP-----TASLLAQLE-TDDYSGSEQYRGDRAYFAEALEGL-------EPALFTRRRPAGLRRTARHRLTLERTLLD 230
Cdd:PRK12316 3789 QGEAPrlpakTSSFKAWAErLQEHARGEALKAELAYWQEQLQGVsselpcdHPQGALQNRHAASVQTRLDRELTRRLLQQ 3868

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523   231 AIRDRGESPFLFLSAAVALYLARIHQNDDVVLGVPVLNR----ADRAAKQVVGHFANTLPLRIrtAPEQTVDEFLAQLRE 306
Cdd:PRK12316 3869 APAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGRedlfADIDLSRTVGWFTSLFPVRL--SPVEDLGASIKAIKE 3946


                  ...
gi 15598523   307 ATR 309
Cdd:PRK12316 3947 QLR 3949
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 2071-2173 3.88e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 41.85  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523  2071 RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQgSTPLAV---LEDIAASYLAAIRRVQPEgPYYLGG 2147
Cdd:PRK14875  126 LGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGA-SSKAVGagsLDELAAAVLAFLDALGIE-RAHLVG 203

                          90       100
                  ....*....|....*....|....*.
gi 15598523  2148 WSFGGFVAYEMARQlralDPQAVAQL 2173
Cdd:PRK14875  204 HSMGGAVALRLAAR----APQRVASL 225
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 1502-1711 5.70e-03

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: 41.95  E-value: 5.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1502 TYRDLD-HVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ---PFRVV 1577
Cdd:cd05905   16 TWGKLLsRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKvrvALTVE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598523 1578 A-HPEH-----AHVAAAERVLPV---EELVADIEPETFAAPQLD----------ELAMLLFTSGSTGRPKGVELSHRMWA 1638
Cdd:cd05905   96 AcLKGLpkkllKSKTAAEIAKKKgwpKILDFVKIPKSKRSKLKKwgphpptrdgDTAYIEYSFSSDGSLSGVAVSHSSLL 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598523 1639 NYTQwQLRVASGVPGLRTLqFAPLSFDMAFQEIFSTLCG---GGELQLISNRE-RMDPSALLHVLERRQVQRVLLPF 1711
Cdd:cd05905  176 AHCR-ALKEACELYESRPL-VTVLDFKSGLGLWHGCLLSvysGHHTILIPPELmKTNPLLWLQTLSQYKVRDAYVKL 250
 
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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