|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
62-1119 |
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: 888.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 62 DAATPGQNDIPPRNETCPPLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKG 141
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 142 VPKQTI-----SAACDAPFSVVEISPAAAAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTE 216
Cdd:COG1020 81 RPVQVIqpvvaAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 217 ILLKDLGAFYSAEVSGNATPEAELPIQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGEL 296
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 297 HDFTIEKETADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFG 376
Cdd:COG1020 241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 377 NFEKALRETHATLRQVISHQDMPFERIVDMVGVQRDPDSHPLFQIKFQLDAAPRERIRLPGLEMRRLARQDKVSRLDLCL 456
Cdd:COG1020 321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 457 DLRETEAGLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAGPQYFHE 536
Cdd:COG1020 401 TVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 537 LFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL 616
Cdd:COG1020 481 LFEAQAARTPDAVAVV----FGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPL 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 617 DPEYPAERIGAMLSDAGARLVVSHSSID--LP-KTANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVL 693
Cdd:COG1020 557 DPAYPAERLAYMLEDAGARLVLTQSALAarLPeLGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVM 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 694 VDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTP 773
Cdd:COG1020 637 VEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTP 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 774 S---ALLSLPVDDLLSLRTVLVGGEVPMPELIERWGK---TRRFINAYGPTETTVNASMVDMGGG---RAGLPVLRPAAN 844
Cdd:COG1020 717 SllrALLDAAPEALPSLRLVLVGGEALPPELVRRWRArlpGARLVNLYGPTETTVDSTYYEVTPPdadGGSVPIGRPIAN 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 845 KQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLADGRIHVSGRLDS 924
Cdd:COG1020 797 TRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPG--ARLYRTGDLARWLPDGNLEFLGRADD 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 925 QVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPDTFD 1004
Cdd:COG1020 875 QVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVP----EAGAAAAAALLRLALALLLPPYMVPAAVV 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1005 WLEALPLTMNGKIDPLKLPAPRAETDPDGRAPEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSLLATRFCAVAKDKF 1084
Cdd:COG1020 951 LLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLL 1030
|
1050 1060 1070
....*....|....*....|....*....|....*
gi 796556827 1085 GLDIGVIDLFNASTVEALANRLRTRDTGGSDDETL 1119
Cdd:COG1020 1031 LLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAA 1065
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
80-1106 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 830.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVVE 159
Cdd:PRK12467 51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 ISPAAAAMEDV-----IHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNA 234
Cdd:PRK12467 131 LANEQGRARESqieayINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGRE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 235 TPEAELPIQYGDFAAWQRERL-ATEIAGTLdAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIA 313
Cdd:PRK12467 211 PSLPALPIQYADYAIWQRSWLeAGERERQL-AYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 314 AAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVI 393
Cdd:PRK12467 290 QREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 394 SHQDMPFERIVDMVGVQRDPDSHPLFQIKF--QLDAA---PRERIRLPGLEMRRLARQDKVSRLDLCLDLRETEAGLSGT 468
Cdd:PRK12467 370 AHQDLPFEQLVEALQPERSLSHSPLFQVMFnhQNTATggrDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 469 IEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAgPQYFHELFEAHVARAPQA 548
Cdd:PRK12467 450 FTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYA-PDCVHQLIEAQARQHPER 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 549 AALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAM 628
Cdd:PRK12467 529 PALVF----GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYM 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 629 LSDAGARLVVSHSS----IDLPKTANRLNLDEdfPDDE----SADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLI 700
Cdd:PRK12467 605 LDDSGVRLLLTQSHllaqLPVPAGLRSLCLDE--PADLlcgySGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALA 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 701 NLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPS---ALL 777
Cdd:PRK12467 683 NYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPShlqALL 762
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 778 SLP-VDDLLSLRTVLVGGEVPMPELIERW---GKTRRFINAYGPTETTVNASMVDMGGGRA---GLPVLRPAANKQLYVL 850
Cdd:PRK12467 763 QASrVALPRPQRALVCGGEALQVDLLARVralGPGARLINHYGPTETTVGVSTYELSDEERdfgNVPIGQPLANLGLYIL 842
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 851 DDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRG 930
Cdd:PRK12467 843 DHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADG--GRLYRTGDLARYRADGVIEYLGRMDHQVKIRG 920
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 931 YRIEPGEIEARLLAHPAIVSATVAVRdDGRGGKRLAAYAVPQIDQDAATRP-TPSEIRAWLANRLPKFLVPDTFDWLEAL 1009
Cdd:PRK12467 921 FRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLVAYLVPAAVADGAEHQaTRDELKAQLRQVLPDYMVPAHLLLLDSL 999
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1010 PLTMNGKIDPLKLPAPRAETDPDG-RAPEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSLLATRFCAVAKDKFGLDI 1088
Cdd:PRK12467 1000 PLTPNGKLDRKALPKPDASAVQATfVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQV 1079
|
1050
....*....|....*...
gi 796556827 1089 GVIDLFNASTVEALANRL 1106
Cdd:PRK12467 1080 PLRTLFEHQTLAGFAQAV 1097
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
59-1117 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 814.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 59 AHADAATPGQNDIPprNETCPPLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYS 138
Cdd:PRK12467 1099 AQQQGAQPALPDVD--RDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 139 DKGVPKQTISAACDAPFSVVEISPAA---AAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWST 215
Cdd:PRK12467 1177 EDGRTRQVIHPVGSLTLEEPLLLAADkdeAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSM 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 216 EILLKDLGAFYSAEVSGNATPEAELPIQYGDFAAWQRERL-ATEIAGTLdAFWKQHLSQPRQTTQLVTDMARTAGHGHAG 294
Cdd:PRK12467 1257 QVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMdAGERARQL-AYWKAQLGGEQPVLELPTDRPRPAVQSHRG 1335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 295 ELHDFTIEKETADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDP 374
Cdd:PRK12467 1336 ARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDG 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 375 FGNFEKALRETHATLRQVISHQDMPFERIVDMVGVQRDPDSHPLFQIKF--QLDAAPRERiRLPGLEMRRLARQDKVSRL 452
Cdd:PRK12467 1416 QASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFnhQRDDHQAQA-QLPGLSVESLSWESQTAQF 1494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 453 DLCLDLRETEAGLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAGPQ 532
Cdd:PRK12467 1495 DLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLAR 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 533 YFHELFEAHVARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGA 612
Cdd:PRK12467 1575 LVHQLIEDQAAATPEAVALVF----GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGA 1650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 613 YLPLDPEYPAERIGAMLSDAGARLVVSHSSI----DLPKTANRLNLDE--DFPDDESADNLETVTHSSQLAYVIYTSGST 686
Cdd:PRK12467 1651 YVPLDPEYPRERLAYMIEDSGIELLLTQSHLqarlPLPDGLRSLVLDQedDWLEGYSDSNPAVNLAPQNLAYVIYTSGST 1730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 687 GKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHV 766
Cdd:PRK12467 1731 GRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQV 1810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 767 THLTMTPSALLSL-----PVDDLLSLRTVLVGGEVPMPELIERWG---KTRRFINAYGPTETTVN-----ASMVDMgGGR 833
Cdd:PRK12467 1811 TTLHFVPSMLQQLlqmdeQVEHPLSLRRVVCGGEALEVEALRPWLerlPDTGLFNLYGPTETAVDvthwtCRRKDL-EGR 1889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 834 AGLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLAD 913
Cdd:PRK12467 1890 DSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVG--SRLYRTGDLARYRAD 1967
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 914 GRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAiVSATVAVRDDGRGGKRLAAYAVPQ----IDQDAATRPTPSEIRAW 989
Cdd:PRK12467 1968 GVIEYLGRIDHQVKIRGFRIELGEIEARLREQGG-VREAVVIAQDGANGKQLVAYVVPTdpglVDDDEAQVALRAILKNH 2046
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 990 LANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPAPRA-ETDPDGRAPEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGG 1068
Cdd:PRK12467 2047 LKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDAsELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGG 2126
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 796556827 1069 HSLLATRFCAVAKDKfGLDIGVIDLFNASTVEALANRLRTRDTGGSDDE 1117
Cdd:PRK12467 2127 DSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDGTVSIDQ 2174
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-1103 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 761.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAacDAPFSVVE 159
Cdd:PRK12316 51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPL--DRPLEVEF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 ISPAA-------AAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSG 232
Cdd:PRK12316 129 EDCSGlpeaeqeARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 233 NATPEAELPIQYGDFAAWQRERL-ATEIAGTLdAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRK 311
Cdd:PRK12316 209 AEPGLPALPIQYADYALWQRSWLeAGEQERQL-EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 312 IAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQ 391
Cdd:PRK12316 288 TARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 392 VISHQDMPFERIVDMVGVQRDPDSHPLFQIKFQ---LDAAPRERIRLPGLEMRRLARQDKVSRLDLCLDLRETEAGLSGT 468
Cdd:PRK12316 368 AQAHQDLPFERLVEALKVERSLSHSPLFQVMYNhqpLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 469 IEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAGPQYFHELFEAHVARAPQA 548
Cdd:PRK12316 448 LTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEA 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 549 AALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAM 628
Cdd:PRK12316 528 PALAF----GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYM 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 629 LSDAGARLVVSHS----SIDLPKTANRLNLDED--FPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINL 702
Cdd:PRK12316 604 LEDSGVQLLLSQShlgrKLPLAAGVQVLDLDRPaaWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNR 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 703 TRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSALLSL--- 779
Cdd:PRK12316 684 LCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFlqd 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 780 -PVDDLLSLRTVLVGGEVPMPELIER-WGK--TRRFINAYGPTETTVNA---SMVDMGGGraGLPVLRPAANKQLYVLDD 852
Cdd:PRK12316 764 eDVASCTSLRRIVCSGEALPADAQEQvFAKlpQAGLYNLYGPTEAAIDVthwTCVEEGGD--SVPIGRPIANLACYILDA 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 853 NLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYR 932
Cdd:PRK12316 842 NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGER---MYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 918
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 933 IEPGEIEARLLAHPAIVSATVAVRDdgrgGKRLAAYAVPQidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLT 1012
Cdd:PRK12316 919 IELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLE----SEGGDWREALKAHLAASLPEYMVPAQWLALERLPLT 990
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1013 MNGKIDPLKLPAPRAETDPDGR-APEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSLLATRFCAVAKDKfGLDIGVI 1091
Cdd:PRK12316 991 PNGKLDRKALPAPEASVAQQGYvAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPR 1069
|
1050
....*....|..
gi 796556827 1092 DLFNASTVEALA 1103
Cdd:PRK12316 1070 DLFQHQTIRSLA 1081
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-1121 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 709.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVVE 159
Cdd:PRK12316 2604 PLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLED 2683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 -ISPAAAAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNATPEA 238
Cdd:PRK12316 2684 cAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLP 2763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 239 ELPIQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIAAAHGT 318
Cdd:PRK12316 2764 PLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGV 2843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 319 TLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVISHQDM 398
Cdd:PRK12316 2844 TLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDL 2923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 399 PFERIVDMVGVQRDPDSHPLFQIKFQLDAAPRERIRLPGLEMRRLARQDKVSRLDLCLDLRETEAGLSGTIEYKTALFRA 478
Cdd:PRK12316 2924 PFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDA 3003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 479 ETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAGPQYFHELFEAHVARAPQAAALimpqADA 558
Cdd:PRK12316 3004 RTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVAL----AFG 3079
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 559 DDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVV 638
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 639 SHSSIDLPKTANRLNLDEDF-PDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDC 717
Cdd:PRK12316 3160 SQSHLRLPLAQGVQVLDLDRgDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDR 3239
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 718 VLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPS----ALLSLPVDDLLSLRTVLVG 793
Cdd:PRK12316 3240 VLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSmlqaFLEEEDAHRCTSLKRIVCG 3319
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 794 GEVPMPELIERWGKTRRFINAYGPTETTVNASMVDMGG-GRAGLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGI 872
Cdd:PRK12316 3320 GEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEeGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGL 3399
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 873 ARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSAT 952
Cdd:PRK12316 3400 ARGYHNRPGLTAERFVPDPFVPGER---LYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAV 3476
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 953 VAVRDdgrgGKRLAAYAVPQIDQDAAtrptPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPAPRA-ETDP 1031
Cdd:PRK12316 3477 VLAVD----GRQLVAYVVPEDEAGDL----REALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAaLLQQ 3548
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1032 DGRAPEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSLLATRFCAVAKdKFGLDIGVIDLFNASTVEALANRLRTR-- 1109
Cdd:PRK12316 3549 DYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRAR-QAGIRFTPKDLFQHQTIQGLARVARVGgg 3627
|
1050
....*....|....*
gi 796556827 1110 ---DTGGSDDETLLL 1121
Cdd:PRK12316 3628 vavDQGPVSGETLLL 3642
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
80-1120 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 695.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDA-----P 154
Cdd:PRK05691 1730 PLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLrmdwqD 1809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 155 FSVVEISPAAAAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNA 234
Cdd:PRK05691 1810 FSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRE 1889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 235 TPEAELPIQYGDFAAWQRERL-ATEIAGTLDaFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIA 313
Cdd:PRK05691 1890 SPLEPLPVQYLDYSVWQRQWLeSGERQRQLD-YWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFN 1968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 314 AAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVI 393
Cdd:PRK05691 1969 AQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQ 2048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 394 SHQDMPFERIVDMVGVQRDPDSHPLFQI-------KFQldaAPRErirLPGLEMRRLARQDKVSRLDLCLDLRETEAGLS 466
Cdd:PRK05691 2049 SHQDLPFDHLVEALQPPRSAAYNPLFQVmcnvqrwEFQ---QSRQ---LAGMTVEYLVNDARATKFDLNLEVTDLDGRLG 2122
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 467 GTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAGPQYFHELFEAHVARAP 546
Cdd:PRK05691 2123 CCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTP 2202
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 547 QAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIG 626
Cdd:PRK05691 2203 QAPALTF----AGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLH 2278
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 627 AMLSDAGARLVVSHSSI-----DLPKTANRLNLDEDFP--DDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGL 699
Cdd:PRK05691 2279 YMIEDSGIGLLLSDRALfealgELPAGVARWCLEDDAAalAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEI 2358
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 700 INLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMslgagarllllpryATLPGA-------------ELADILRARHV 766
Cdd:PRK05691 2359 AMHCQAVIERFGMRADDCELHFYSINFDAASERLLV--------------PLLCGArvvlraqgqwgaeEICQLIREQQV 2424
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 767 THLTMTPS-----ALLSLPVDDLLSLRTVLVGGEVPMPELIERWGKT---RRFINAYGPTETTVN--ASMV--DMGGGRA 834
Cdd:PRK05691 2425 SILGFTPSygsqlAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAfapQLFFNAYGPTETVVMplACLApeQLEEGAA 2504
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 835 GLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLADG 914
Cdd:PRK05691 2505 SVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADG--GRLYRTGDLVRLRADG 2582
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 915 RIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDgRGGKRLAAYAV-PQIDQDAATRPTPSE-IRAWLAN 992
Cdd:PRK05691 2583 LVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDT-PSGKQLAGYLVsAVAGQDDEAQAALREaLKAHLKQ 2661
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 993 RLPKFLVPDTFDWLEALPLTMNGKIDPLKLPAPRAETD-PDGRAPEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSL 1071
Cdd:PRK05691 2662 QLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNrQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSI 2741
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 796556827 1072 LATRFCAVAKdKFGLDIGVIDLFNASTVEALAnRLRTRDTGGSDDETLL 1120
Cdd:PRK05691 2742 LSIQVVSRAR-QLGIHFSPRDLFQHQTVQTLA-AVATHSEAAQAEQGPL 2788
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
65-1124 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 689.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 65 TPGQNDIP--PRNETCPPlSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGV 142
Cdd:PRK05691 661 GAAQAAIArlPRGQALPQ-SLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGV 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 143 PKQTISAACDAPFSVVEIS--PAA---AAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEI 217
Cdd:PRK05691 740 ALQRIDAQGEFALQRIDLSdlPEAereARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNI 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 218 LLKDLGAFYSAEVSGNATPEAELPIQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELH 297
Cdd:PRK05691 820 LLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARY 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 298 DFTIEKETADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGN 377
Cdd:PRK05691 900 SLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLP 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 378 FEKALRETHATLRQVISHQDMPFERIVDMVGVQRDpdsHPLFQIKF---QLD-AAPReriRLPGLEMRRLARQDKVSRLD 453
Cdd:PRK05691 980 FTALLAQVRQATLGAQAHQDLPFEQLVEALPQARE---QGLFQVMFnhqQRDlSALR---RLPGLLAEELPWHSREAKFD 1053
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 454 LCLDLRETEAG-LSGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQrICDFNSTAQEHAgPQ 532
Cdd:PRK05691 1054 LQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQAPCAPA-QA 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 533 YFHELFEAHVARAPQAAALIMPQADADdimtYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGA 612
Cdd:PRK05691 1132 WLPELLNEQARQTPERIALVWDGGSLD----YAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGA 1207
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 613 YLPLDPEYPAERIGAMLSDAGARLVVSHSSI--DLPKTA-------NRLNLDeDFPDDESADNLetvtHSSQLAYVIYTS 683
Cdd:PRK05691 1208 YVPLDPDYPAERLAYMLADSGVELLLTQSHLleRLPQAEgvsaialDSLHLD-SWPSQAPGLHL----HGDNLAYVIYTS 1282
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 684 GSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPE----------LVMSLgagarllllpryatlP 753
Cdd:PRK05691 1283 GSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWEcfwplitgcrLVLAG---------------P 1347
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 754 G-----AELADILRARHVTHLTMTPSaLLSLPVDDLL-----SLRTVLVGGEVPMPELIERWGKTR---RFINAYGPTET 820
Cdd:PRK05691 1348 GehrdpQRIAELVQQYGVTTLHFVPP-LLQLFIDEPLaaactSLRRLFSGGEALPAELRNRVLQRLpqvQLHNRYGPTET 1426
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 821 TVNAS----MVDMGggrAGLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDG 896
Cdd:PRK05691 1427 AINVThwqcQAEDG---ERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDG 1503
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 897 RAgvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQD 976
Cdd:PRK05691 1504 AR--LYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEA 1581
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 977 AATRptpseIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPAPRAETDpDGRAPEGEMEGRIAGAFGHVLNIDQ 1056
Cdd:PRK05691 1582 EAER-----LKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQR-EHVEPRTELQQQIAAIWREVLGLPR 1655
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 796556827 1057 VAATDDFFTLGGHSLLATRFCAVAKDKFGLDIGVIDLFNASTVEALANRL-RTRDTGGSDDETLLLKRD 1124
Cdd:PRK05691 1656 VGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVaRIQAAGERNSQGAIARVD 1724
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-1116 |
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 796556827 80 PLSFAQERLwLIDQIYPGSALHHIC-IALEVRGaLDLDALKVALAGVMSRHTVLRARIY--SDKGVPKQTISAACDAPFS 156
Cdd:PRK12316 4104 PLSPMQQGM-LFHSLYEQEAGDYINqMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVwqGELGRPLQVVHKQVSLPFA 4181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 157 VVEISPAA---AAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEvsgn 233
Cdd:PRK12316 4182 ELDWRGRAdlqAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGR---- 4257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 234 atPEAELPIQYGDFAAWqrerLATEIAGTLDAFWKQHLSQPRQTTQLVTDMAR---TAGHGHAGELHDFtiEKETADALR 310
Cdd:PRK12316 4258 --PPAQPGGRYRDYIAW----LQRQDAAASEAFWREQLAALDEPTRLAQAIARadlRSANGYGEHVREL--DATATARLR 4329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 311 KIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPH--IETEDLVGLFVNPLPVRSLVDP---FGNFEKALRET 385
Cdd:PRK12316 4330 EFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAelPGIEGQIGLFINTLPVIATPRAqqsVVEWLQQVQRQ 4409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 386 HATLRQvisHQDMPFERIVDMVGVQRDPdshpLFQIKFQLDAAP----RERIRLPGLEMRRLARQDK-VSRLDLCLDLRE 460
Cdd:PRK12316 4410 NLALRE---HEHTPLYEIQRWAGQGGEA----LFDSLLVFENYPvseaLQQGAPGGLRFGEVTNHEQtNYPLTLAVGLGE 4482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 461 TeagLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAGPQYFHELFEA 540
Cdd:PRK12316 4483 T---LSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAE 4559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEY 620
Cdd:PRK12316 4560 RARMTPDAVAVVF----DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 621 PAERIGAMLSDAGARLVVSHS----SIDLPKTANRLNLDEDFP-DDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVD 695
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQShllqRLPIPDGLASLALDRDEDwEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVS 4715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 696 HSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRaRHVTHLTMTPSA 775
Cdd:PRK12316 4716 HGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHE-HRVTVLVFPPVY 4794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 776 LLSLPVD-----DLLSLRTVLVGGEVPMPELIERW---GKTRRFINAYGPTETTVNASMVDMGG----GRAGLPVLRPAA 843
Cdd:PRK12316 4795 LQQLAEHaerdgEPPSLRVYCFGGEAVAQASYDLAwraLKPVYLFNGYGPTETTVTVLLWKARDgdacGAAYMPIGTPLG 4874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 844 NKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLADGRIHVSGRLD 923
Cdd:PRK12316 4875 NRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPG--GRLYRTGDLARYRADGVIDYLGRVD 4952
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 924 SQVKIRGYRIEPGEIEARLLAHPAiVSATVAVRDDGRGGKRLAAYAVPQ----IDQDAATRPTPSEIRAWLANRLPKFLV 999
Cdd:PRK12316 4953 HQVKIRGFRIELGEIEARLREHPA-VREAVVIAQEGAVGKQLVGYVVPQdpalADADEAQAELRDELKAALRERLPEYMV 5031
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1000 PDTFDWLEALPLTMNGKIDPLKLPAPRAETDPDGR-APEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSLLATRFCA 1078
Cdd:PRK12316 5032 PAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYvAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTS 5111
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 796556827 1079 VAKDKFGLDIGVIDLFNASTVEALANRLRTRDTGGSDD 1116
Cdd:PRK12316 5112 RIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEK 5149
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
546-1023 |
0e+00 |
|
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: 647.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALIMPqadaDDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd17652 1 PDAPAVVFG----DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVvshssidlpktanrlnldedfpddesadnletVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRD 705
Cdd:cd17652 77 AYMLADARPALL--------------------------------LTTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 706 KIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSALLSLPVDDLL 785
Cdd:cd17652 125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 786 SLRTVLVGGEVPMPELIERWGKTRRFINAYGPTETTVNASMVDMGGGRAGLPVLRPAANKQLYVLDDNLELLPFGVPGEL 865
Cdd:cd17652 205 DLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGEL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 866 HIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAH 945
Cdd:cd17652 285 YIAGAGLARGYLNRPGLTAERFVADPFGAPG--SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEH 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 946 PAIVSATVAVRDDGRGGKRLAAYAVPQIDqdaaTRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLP 1023
Cdd:cd17652 363 PGVAEAVVVVRDDRPGDKRLVAYVVPAPG----AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
53-1106 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 639.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 53 LAFLNMAHADAATPGQNDIpprnETCPPLSFAQERLwLIDQIYPGSALHHI---CIALEvrgALDLDALKVALAGVMSRH 129
Cdd:PRK12467 2625 LAGLSQEQLDRLPVAVGDI----EDIYPLSPMQQGM-LFHTLYEGGAGDYInqmRVDVE---GLDVERFRTAWQAVIDRH 2696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 130 TVLRARIYSDKGV--PKQTISAACDAPFSVVEISPAA---AAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFT 204
Cdd:PRK12467 2697 EILRSGFLWDGELeePLQVVYKQARLPFSRLDWRDRAdleQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYT 2776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 205 LHHICADGWSTEILLKDLGAFYSaevsGNATPEAELpiQYGDFAAWqrerLATEIAGTLDAFWKQHLSQPRQTTQLVTDM 284
Cdd:PRK12467 2777 NHHILMDGWSGSQLLGEVLQRYF----GQPPPAREG--RYRDYIAW----LQAQDAEASEAFWKEQLAALEEPTRLARAL 2846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 285 ARTAGHGHAG-ELHDFTIEKETADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPH----IETEdlV 359
Cdd:PRK12467 2847 YPAPAEAVAGhGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAqlrgAEQQ--L 2924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 360 GLFVNPLPVRSLVDP----------FGNFEKALRE-THATLRQVISHQDMPFERIVDMVGV-QRDPDSHPLFQikfqldA 427
Cdd:PRK12467 2925 GLFINTLPVIASPRAeqtvsdwlqqVQAQNLALREfEHTPLADIQRWAGQGGEALFDSILVfENYPISEALKQ------G 2998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 428 APRerirlpGLEMRRLARQDKVSR-LDLCLDLRETeagLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATL 506
Cdd:PRK12467 2999 APS------GLRFGAVSSREQTNYpLTLAVGLGDT---LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGEL 3069
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 507 ALLTQEEQRQRICDFNSTAQEHAGPQYFHELFEAHVARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAE 586
Cdd:PRK12467 3070 PTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVF----GDQQLSYAELNRRANRLAHRLIAIGVGPD 3145
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 587 TVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSSI--DLPKTA--NRLNLDEDFPDDE 662
Cdd:PRK12467 3146 VLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLleQLPAPAgdTALTLDRLDLNGY 3225
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 663 SADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGAR 742
Cdd:PRK12467 3226 SENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGC 3305
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 743 LLLLPRYATLPgAELADILRARHVTHLTMTPSALLSLPVD----DLLSLRTVLVGGEVPMP---ELIERWGKTRRFINAY 815
Cdd:PRK12467 3306 LVVRDNDLWDP-EELWQAIHAHRISIACFPPAYLQQFAEDaggaDCASLDIYVFGGEAVPPaafEQVKRKLKPRGLTNGY 3384
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 816 GPTETTVNASMVDMGG----GRAGLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDP 891
Cdd:PRK12467 3385 GPTEAVVTVTLWKCGGdavcEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP 3464
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 892 FATDGraGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRdDGRGGKRLAAYAVP 971
Cdd:PRK12467 3465 FSGSG--GRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP 3541
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 972 QIDQDAATrptpSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPAPRAETDPDGRAPEGEMEGRIAGAFGHV 1051
Cdd:PRK12467 3542 ADPQGDWR----ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADV 3617
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 796556827 1052 LNIDQVAATDDFFTLGGHSLLATRFCAVAKDKFGLDIGVIDLFNASTVEALANRL 1106
Cdd:PRK12467 3618 LGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS 3672
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-1111 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 615.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLwLIDQIYPGSALHHIC-IALEVRGaLDLDALKVALAGVMSRHTVLRARIYSDKGV--PKQTISAACDAPFS 156
Cdd:PRK12316 1558 PLSPMQQGM-LFHSLYEQEAGDYINqLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGLeqPLQVIHKQVELPFA 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 157 VVEIS---PAAAAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEvsgn 233
Cdd:PRK12316 1636 ELDWRgreDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQ---- 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 234 atPEAELPIQYGDFAAW--QRERLATEiagtldAFWKQHLSQPRQTTQLVTDMARTAGHGHAGElHDFTIEKETADALRK 311
Cdd:PRK12316 1712 --PVAAPGGRYRDYIAWlqRQDAAASE------AFWKEQLAALEEPTRLAQAARTEDGQVGYGD-HQQLLDPAQTRALAE 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 312 IAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPH----IETEdlVGLFVNPLPVRSLVDP---FGNFEKALRE 384
Cdd:PRK12316 1783 FARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelpgIEQQ--IGLFINTLPVIAAPRPdqsVADWLQEVQA 1860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 385 THATLRQvisHQDMPFERIVDMVGVQRDP--DSHPLFQiKFQLDAAPRERIRlPGLEMRRLARQDKVSR-LDLCLDLRET 461
Cdd:PRK12316 1861 LNLALRE---HEHTPLYDIQRWAGQGGEAlfDSLLVFE-NYPVAEALKQGAP-AGLVFGRVSNHEQTNYpLTLAVTLGET 1935
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 462 eagLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAGPQYFHELFEAH 541
Cdd:PRK12316 1936 ---LSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQ 2012
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 542 VARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYP 621
Cdd:PRK12316 2013 AARAPEAIAVVF----GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYP 2088
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 622 AERIGAMLSDAGARLVVSHSSI--DLPKTANRLNLDEDfPDDESAD----NLETVTHSSQLAYVIYTSGSTGKAKGVLVD 695
Cdd:PRK12316 2089 AERLAYMLEDSGAALLLTQRHLleRLPLPAGVARLPLD-RDAEWADypdtAPAVQLAGENLAYVIYTSGSTGLPKGVAVS 2167
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 696 HSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGaELADILRARHVTHLTMTPSA 775
Cdd:PRK12316 2168 HGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPE-QLYDEMERHGVTILDFPPVY 2246
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 776 LLSLPVD-----DLLSLRTVLVGGEVPMPELIERWGK---TRRFINAYGPTETTVNASMVDM----GGGRAGLPVLRPAA 843
Cdd:PRK12316 2247 LQQLAEHaerdgRPPAVRVYCFGGEAVPAASLRLAWEalrPVYLFNGYGPTEAVVTPLLWKCrpqdPCGAAYVPIGRALG 2326
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 844 NKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLADGRIHVSGRLD 923
Cdd:PRK12316 2327 NRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASG--ERLYRTGDLARYRADGVVEYLGRID 2404
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 924 SQVKIRGYRIEPGEIEARLLAHPAIVSATVaVRDDGRGGKRLAAYAVPqidQDAATrPTPSEIRAWLANRLPKFLVPDTF 1003
Cdd:PRK12316 2405 HQVKIRGFRIELGEIEARLQAHPAVREAVV-VAQDGASGKQLVAYVVP---DDAAE-DLLAELRAWLAARLPAYMVPAHW 2479
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1004 DWLEALPLTMNGKIDPLKLPAPR-AETDPDGRAPEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSLLATRFCAVAKD 1082
Cdd:PRK12316 2480 VVLERLPLNPNGKLDRKALPKPDvSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQ 2559
|
1050 1060
....*....|....*....|....*....
gi 796556827 1083 KFGLDIGVIDLFNASTVEALANRLRTRDT 1111
Cdd:PRK12316 2560 DLGLEVPLRILFERPTLAAFAASLESGQT 2588
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
546-1018 |
3.11e-171 |
|
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: 520.93 E-value: 3.11e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd05930 1 PDAVAVV----DGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVVshssidlpktanrlnldedfpddesadnletvTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRD 705
Cdd:cd05930 77 AYILEDSGAKLVL--------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 706 KIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSALLSL----PV 781
Cdd:cd05930 125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLlqelEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 782 DDLLSLRTVLVGGEVPMPELIERWGKT---RRFINAYGPTETTVNASM--VDMGG-GRAGLPVLRPAANKQLYVLDDNLE 855
Cdd:cd05930 205 AALPSLRLVLVGGEALPPDLVRRWRELlpgARLVNLYGPTEATVDATYyrVPPDDeEDGRVPIGRPIPNTRVYVLDENLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 856 LLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEP 935
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGER---MYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 936 GEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNG 1015
Cdd:cd05930 362 GEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVP----DEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437
|
...
gi 796556827 1016 KID 1018
Cdd:cd05930 438 KVD 440
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
80-499 |
3.09e-162 |
|
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: 496.49 E-value: 3.09e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVVE 159
Cdd:cd19531 3 PLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 ISP-----AAAAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNA 234
Cdd:cd19531 83 LSGlpeaeREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 235 TPEAELPIQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIAA 314
Cdd:cd19531 163 SPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRALAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 315 AHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVIS 394
Cdd:cd19531 243 REGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 395 HQDMPFERIVDMVGVQRDPDSHPLFQIKFQLDAAPRERIRLPGLEMRRLARQDKVSRLDLCLDLRETEAGLSGTIEYKTA 474
Cdd:cd19531 323 HQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYNTD 402
|
410 420
....*....|....*....|....*
gi 796556827 475 LFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19531 403 LFDAATIERMAGHFQTLLEAIVADP 427
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
80-1106 |
8.11e-157 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 510.74 E-value: 8.11e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAAcdAPFSVVE 159
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPA--LTFPLPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 I-------SPAAAAMeDVIHAETSRPFDLAAEPPI-RLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVS 231
Cdd:PRK10252 87 IidlrtqpDPHAAAQ-ALMQADLQQDLRVDSGKPLvFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 232 GNATPEAELP---------IQYGDFAAWQRERlateiagtldAFWKQHLSQPRQTTQLVTdmARTAGHGHAGELHDFTIE 302
Cdd:PRK10252 166 GEPTPASPFTpfadvveeyQRYRASEAWQRDA----------AFWAEQRRQLPPPASLSP--APLPGRSASADILRLKLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 303 KETADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKAL 382
Cdd:PRK10252 234 FTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 383 RETHATLRQVISHQDMPFERIV-DM--VGVQRdPDSHPLFQIK-FQldaaprERIRLPGLEMR--RLArQDKVSRLDLCL 456
Cdd:PRK10252 314 TRLAAQLKKMRRHQRYDAEQIVrDSgrAAGDE-PLFGPVLNIKvFD------YQLDFPGVQAQthTLA-TGPVNDLELAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 457 DLRETeAGLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEqRQRICDFNSTAqeHAGPQY-FH 535
Cdd:PRK10252 386 FPDEH-GGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGE-YAQLAQVNATA--VEIPETtLS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALimpqADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:PRK10252 462 ALVAQQAAKTPDAPAL----ADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLVVSHSSiDLPKTANRLNLDEDFPDDESADNLETVTHSSQ---LAYVIYTSGSTGKAKGV 692
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTAD-QLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQphhTAYIIFTSGSTGRPKGV 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 693 LVDHSGLIN---LTRDKIRacdVTADDCVLQFFSFSFDASIPE----------LVMSlgagarllllPRYATLPGAELAD 759
Cdd:PRK10252 617 MVGQTAIVNrllWMQNHYP---LTADDVVLQKTPCSFDVSVWEffwpfiagakLVMA----------EPEAHRDPLAMQQ 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 760 ILRARHVTHLTMTPS---ALLSLP-----VDDLLSLRTVLVGGEVPMPELIERWGKT--RRFINAYGPTETTVN-----A 824
Cdd:PRK10252 684 FFAEYGVTTTHFVPSmlaAFVASLtpegaRQSCASLRQVFCSGEALPADLCREWQQLtgAPLHNLYGPTEAAVDvswypA 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 825 SMVDMGGGR-AGLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYR 903
Cdd:PRK10252 764 FGEELAAVRgSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGER---MYR 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 904 TGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHP----AIVSATVAVRDDGRGG--KRLAAYAVPQIDQ-- 975
Cdd:PRK10252 841 TGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGdaRQLVGYLVSQSGLpl 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 976 DAATrptpseIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPAPRAETDPDGRAPEGEMEGRIAGAFGHVLNID 1055
Cdd:PRK10252 921 DTSA------LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCD 994
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 796556827 1056 QVAATDDFFTLGGHSLLATRFCAVAKDKFGLDIGVIDLFNASTVEALANRL 1106
Cdd:PRK10252 995 VVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLL 1045
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
536-1025 |
1.32e-156 |
|
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: 484.14 E-value: 1.32e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVF----EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLVVSHSSIDlPKTANR---LNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGV 692
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHLQ-PPIAFIgliDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 693 LVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMT 772
Cdd:cd17655 156 MIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 773 PSALLSLPVDDL---LSLRTVLVGGEVPMPELIERWGKT----RRFINAYGPTETTVNASM--VDMGGGRAG-LPVLRPA 842
Cdd:cd17655 236 PAHLKLLDAADDsegLSLKHLIVGGEALSTELAKKIIELfgtnPTITNAYGPTETTVDASIyqYEPETDQQVsVPIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 843 ANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRL 922
Cdd:cd17655 316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGER---MYRTGDLARWLPDGNIEFLGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 923 DSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqiDQDAatrpTPSEIRAWLANRLPKFLVPDT 1002
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVS--EKEL----PVAQLREFLARELPDYMIPSY 466
|
490 500
....*....|....*....|...
gi 796556827 1003 FDWLEALPLTMNGKIDPLKLPAP 1025
Cdd:cd17655 467 FIKLDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
536-1018 |
1.20e-151 |
|
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: 470.53 E-value: 1.20e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:cd12117 1 ELFEEQAARTPDAVAVV----YGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLVVSHssidlPKTANRLNLDE------DFPDDESADNLETVTHSSQLAYVIYTSGSTGKA 689
Cdd:cd12117 77 LDPELPAERLAFMLADAGAKVLLTD-----RSLAGRAGGLEvavvidEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 690 KGVLVDHSGLINLTRDKiRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHL 769
Cdd:cd12117 152 KGVAVTHRGVVRLVKNT-NYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 770 TMTpSALLSLPVDD----LLSLRTVLVGGEVPMPELIERW---GKTRRFINAYGPTETTVNA---SMVDMGGGRAGLPVL 839
Cdd:cd12117 231 WLT-AALFNQLADEdpecFAGLRELLTGGEVVSPPHVRRVlaaCPGLRLVNGYGPTENTTFTtshVVTELDEVAGSIPIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 840 RPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVS 919
Cdd:cd12117 310 RPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGER---LYRTGDLARWLPDGRLEFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 920 GRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVpqidqdAATRPTPSEIRAWLANRLPKFLV 999
Cdd:cd12117 387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV------AEGALDAAELRAFLRERLPAYMV 460
|
490
....*....|....*....
gi 796556827 1000 PDTFDWLEALPLTMNGKID 1018
Cdd:cd12117 461 PAAFVVLDELPLTANGKVD 479
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
1145-1506 |
1.31e-148 |
|
thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.
Pssm-ID: 273787 [Multi-domain] Cd Length: 367 Bit Score: 457.65 E-value: 1.31e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1145 HVFLTGATGFLGTYLLHELLRD-PERKVTCLVRGDD---GMSRLRQAFRQYDLPQSVLT-ERVTIVTGELSKPGLGLAAA 1219
Cdd:TIGR01746 1 TVLLTGATGFLGAYLLEELLRRsTRAKVICLVRADSeehAMERLREALRSYRLWHENLAmERIEVVAGDLSKPRLGLSDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1220 DYDNIVRNADCIFHNGAEVHHLHRYERLRETNVLGIREILQLACAGEGRHVHYISTLSALTPRRGSGGdprPVCELESVE 1299
Cdd:TIGR01746 81 EWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTG---VTEDDATVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1300 GFVPPAGGYNRSKWVAEHLVNEAGRRGLPVTIYRPGAISGDSVTGAFNGSDILCRLVQAYLYTGTAPEGERLLD-MLPVD 1378
Cdd:TIGR01746 158 PYPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSDILWRMVKGCLALGAYPQSPELTEdLTPVD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1379 HVARAIVHLSGKPAS--AGQVFHLIHSSPVSSARLFEACELEGIELKRVSQREWQDMLGDVARGTPDHPLYPLLGLLRSP 1456
Cdd:TIGR01746 238 FVARAIVALSSRPAAsaGGIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFDEWLQRLEDSDTAKRDSRRYPLLPLLHFT 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 796556827 1457 SAAGKSDEKQTRNFDCHLTQAALSDAPFREPALTFELLRTYLRAFAKANF 1506
Cdd:TIGR01746 318 GDAFESDETDTRNLDSRSTAEALEGDGIREPSITAPLLHLYLQYLKEIGF 367
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
535-1018 |
1.53e-147 |
|
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: 459.82 E-value: 1.53e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYL 614
Cdd:cd17646 1 HALVAEQAARTPDAPAVV----DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 615 PLDPEYPAERIGAMLSDAGARLVVSHSSID--LPKTANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGV 692
Cdd:cd17646 77 PLDPGYPADRLAYMLADAGPAVVLTTADLAarLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 693 LVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPEL---VMSLgagarllllpryATL----PGAE-----LADI 760
Cdd:cd17646 157 MVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELfwpLVAG------------ARLvvarPGGHrdpayLAAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 761 LRARHVTHLTMTPSAL---LSLP-VDDLLSLRTVLVGGEVPMPELIERWGKT--RRFINAYGPTETTVNAS--MVDMGGG 832
Cdd:cd17646 225 IREHGVTTCHFVPSMLrvfLAEPaAGSCASLRRVFCSGEALPPELAARFLALpgAELHNLYGPTEAAIDVThwPVRGPAE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 833 RAGLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLA 912
Cdd:cd17646 305 TPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSR---MYRTGDLARWRP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 913 DGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidQDAATRPTPSEIRAWLAN 992
Cdd:cd17646 382 DGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVP---AAGAAGPDTAALRAHLAE 458
|
490 500
....*....|....*....|....*.
gi 796556827 993 RLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd17646 459 RLPEYMVPAAFVVLDALPLTANGKLD 484
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
538-1023 |
9.86e-142 |
|
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: 444.48 E-value: 9.86e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 538 FEAHVARAPQAAALIMPQAdaddIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLD 617
Cdd:cd17651 1 FERQAARTPDAPALVAEGR----RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 618 PEYPAERIGAMLSDAGARLVVSHS--SIDLPKTANRLNLDEDFPDDESADNLETV-THSSQLAYVIYTSGSTGKAKGVLV 694
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPalAGELAVELVAVTLLDQPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 695 DHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPS 774
Cdd:cd17651 157 PHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 775 ALLSL------PVDDLLSLRTVLVGGE-VPMPELIERWGKT---RRFINAYGPTETTVNASMV---DMGGGRAGLPVLRP 841
Cdd:cd17651 237 ALRALaehgrpLGVRLAALRYLLTGGEqLVLTEDLREFCAGlpgLRLHNHYGPTETHVVTALSlpgDPAAWPAPPPIGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 842 AANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGR 921
Cdd:cd17651 317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGAR---MYRTGDLARWLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 922 LDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPD 1001
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVG----DPEAPVDAAELRAALATHLPEYMVPS 469
|
490 500
....*....|....*....|..
gi 796556827 1002 TFDWLEALPLTMNGKIDPLKLP 1023
Cdd:cd17651 470 AFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
535-1023 |
6.25e-140 |
|
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: 438.41 E-value: 6.25e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYL 614
Cdd:cd17644 3 HQLFEEQVERTPDAVAVV----FEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 615 PLDPEYPAERIGAMLSDAGARLVvshssidlpktanrlnldedfpddesadnletVTHSSQLAYVIYTSGSTGKAKGVLV 694
Cdd:cd17644 79 PLDPNYPQERLTYILEDAQISVL--------------------------------LTQPENLAYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 695 DHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPs 774
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 775 ALLSLPVDDLL--------SLRTVLVGGEVPMPELIERWGKTR----RFINAYGPTETTVNASMVDM----GGGRAGLPV 838
Cdd:cd17644 206 AYWHLLVLELLlstidlpsSLRLVIVGGEAVQPELVRQWQKNVgnfiQLINVYGPTEATIAATVCRLtqltERNITSVPI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 839 LRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFA--TDGRagvLYRTGDRAVLLADGRI 916
Cdd:cd17644 286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESER---LYKTGDLARYLPDGNI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 917 HVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDaatrPTPSEIRAWLANRLPK 996
Cdd:cd17644 363 EYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEES----PSTVELRQFLKAKLPD 438
|
490 500
....*....|....*....|....*..
gi 796556827 997 FLVPDTFDWLEALPLTMNGKIDPLKLP 1023
Cdd:cd17644 439 YMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
563-953 |
2.14e-139 |
|
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: 434.77 E-value: 2.14e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLR-RKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHS 641
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 SI-----DLPKTANRLNLDEDFPDDESADN--LETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTA 714
Cdd:TIGR01733 81 ALasrlaGLVLPVILLDPLELAALDDAPAPppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 715 DDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARH-VTHLTMTPS---ALLSLPVDDLLSLRTV 790
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSllaLLAAALPPALASLRLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 791 LVGGEVPMPELIERW---GKTRRFINAYGPTETTVNASM----VDMGGGRAGLPVLRPAANKQLYVLDDNLELLPFGVPG 863
Cdd:TIGR01733 241 ILGGEALTPALVDRWrarGPGARLINLYGPTETTVWSTAtlvdPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 864 ELHIGGCGIARGYHDRAALTAERFVPDPFATDGRAgVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLL 943
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGA-RLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
|
410
....*....|
gi 796556827 944 AHPAIVSATV 953
Cdd:TIGR01733 400 RHPGVREAVV 409
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
546-1018 |
1.66e-138 |
|
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: 434.80 E-value: 1.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALimpqADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd12116 1 PDATAV----RDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVVSHSSIDLPKTANRLNLDEDFPDDESA-DNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTR 704
Cdd:cd12116 77 RYILEDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAApAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 705 DKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPS---ALLSLPV 781
Cdd:cd12116 157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPAtwrMLLDAGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 782 DDLLSLrTVLVGGEVPMPELIERW-GKTRRFINAYGPTETTVNASMVDMGGGRAGLPVLRPAANKQLYVLDDNLELLPFG 860
Cdd:cd12116 237 QGRAGL-TALCGGEALPPDLAARLlSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 861 VPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEA 940
Cdd:cd12116 316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPG--SRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 941 RLLAHPAIVSATVAVRDDGrGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd12116 394 ALAAHPGVAQAAVVVREDG-GDRRLVAYVVL----KAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
546-1023 |
2.89e-138 |
|
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: 433.33 E-value: 2.89e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd17649 1 PDAVALVF----GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVVSHssidlpktanrlnldedfpddesadnletvtHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRD 705
Cdd:cd17649 77 RYMLEDSGAGLLLTH-------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 706 KIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSAL-------LS 778
Cdd:cd17649 126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLqqlaeeaDR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 779 LPVDDLLSLRTVLVGGEVPMPELIERWGKTR-RFINAYGPTETTVNASM--VDMGGGRAG--LPVLRPAANKQLYVLDDN 853
Cdd:cd17649 206 TGDGRPPSLRLYIFGGEALSPELLRRWLKAPvRLFNAYGPTEATVTPLVwkCEAGAARAGasMPIGRPLGGRSAYILDAD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 854 LELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGraGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRI 933
Cdd:cd17649 286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPG--SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 934 EPGEIEARLLAHPAIVSATVAVRdDGRGGKRLAAYAVPQidQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTM 1013
Cdd:cd17649 364 ELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLR--AAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTP 440
|
490
....*....|
gi 796556827 1014 NGKIDPLKLP 1023
Cdd:cd17649 441 NGKLDRKALP 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
546-1018 |
1.78e-136 |
|
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: 428.65 E-value: 1.78e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd17643 1 PEAVAVV----DEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVvshssidlpktanrlnldedfpddesadnletVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRD 705
Cdd:cd17643 77 AFILADSGPSLL--------------------------------LTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 706 KIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSALLSL------ 779
Cdd:cd17643 125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLveaadr 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 780 PVDDLLSLRTVLVGGEVPMPELIERWGKTR-----RFINAYGPTETTVNASM----VDMGGGRAGLPVLRPAANKQLYVL 850
Cdd:cd17643 205 DGRDPLALRYVIFGGEALEAAMLRPWAGRFgldrpQLVNMYGITETTVHVTFrpldAADLPAAAASPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 851 DDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdGRAGV-LYRTGDRAVLLADGRIHVSGRLDSQVKIR 929
Cdd:cd17643 285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF---GGPGSrMYRTGDLARRLPDGELEYLGRADEQVKIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 930 GYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEAL 1009
Cdd:cd17643 362 GFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVA----DDGAAADIAELRALLKELLPDYMVPARYVPLDAL 437
|
....*....
gi 796556827 1010 PLTMNGKID 1018
Cdd:cd17643 438 PLTVNGKLD 446
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
266-1450 |
2.44e-133 |
|
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: 447.97 E-value: 2.44e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 266 FWKQHLSQPrQTTQLVTDMARTAGHGHAGELHDFTIEKETAdalrkiAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGT 345
Cdd:TIGR03443 1 RWSERLDNP-TLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 346 PVASRPhietedlvglfvNPLPVRSLVDPFGNFEKALRETHATLRQVISHQDMPFERIVDMVGVQRDPDSHP-LFQIKFQ 424
Cdd:TIGR03443 74 SSNKSG------------RPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAFQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 425 ldaapreriRLPGLEMRRLArqdKVSRLDLCLDLRETEAGLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVA 504
Cdd:TIGR03443 142 ---------DAPDNQQTTYS---TGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 505 TLALLTqEEQRQRI---------CDFNstaqehaGPqyFHELFEAHVARAPQAAALIMPQADADD-----IMTYGELNAR 570
Cdd:TIGR03443 210 KVSLIT-PSQKSLLpdptkdldwSGFR-------GA--IHDIFADNAEKHPDRTCVVETPSFLDPssktrSFTYKQINEA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 571 ANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLS-----------DAG--ARLV 637
Cdd:TIGR03443 280 SNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSvakpralivieKAGtlDQLV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 638 VSH--SSIDLPKTANRLNLDED------FPDDESADNLETVTH-SSQLAYVI----------YTSGSTGKAKGVLVDHSG 698
Cdd:TIGR03443 360 RDYidKELELRTEIPALALQDDgslvggSLEGGETDVLAPYQAlKDTPTGVVvgpdsnptlsFTSGSEGIPKGVLGRHFS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 699 L----------INLT-RDKIRACDVTADDCVLQ--FFSFSFDASIpeLVmslgagarllllpryatlPGAE-------LA 758
Cdd:TIGR03443 440 LayyfpwmakrFGLSeNDKFTMLSGIAHDPIQRdmFTPLFLGAQL--LV------------------PTADdigtpgrLA 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 759 DILRARH--VTHLTMTPSALLSLPVDDLL-SLRTVLVGGEVpmpeLIER-------WGKTRRFINAYGPTET-------- 820
Cdd:TIGR03443 500 EWMAKYGatVTHLTPAMGQLLSAQATTPIpSLHHAFFVGDI----LTKRdclrlqtLAENVCIVNMYGTTETqravsyfe 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 821 --------TVNASMVDMgggragLPVLRPAANKQLYVLDDNLELLPFGVP--GELHIGGCGIARGYHDRAALTAERFVPD 890
Cdd:TIGR03443 576 ipsrssdsTFLKNLKDV------MPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNN 649
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 891 PFATD-------------------GRAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSA 951
Cdd:TIGR03443 650 WFVDPshwidldkennkperefwlGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREN 729
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 952 TVAVRDDGRGGKRLAAYAVPQIDQDA----------------------ATRPTPSEIRAWLANRLPKFLVPDTFDWLEAL 1009
Cdd:TIGR03443 730 VTLVRRDKDEEPTLVSYIVPQDKSDEleefksevddeessdpvvkgliKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKL 809
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1010 PLTMNGKIDPLKLPAPRA---ETDPDGRAPEG------EMEGRIAGAFGHVL-NI-DQVAATDDFFTLGGHSLLATRFCA 1078
Cdd:TIGR03443 810 PLNPNGKVDKPALPFPDTaqlAAVAKNRSASAadeeftETEREIRDLWLELLpNRpATISPDDSFFDLGGHSILATRMIF 889
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1079 VAKDKFGLDI--GVIdlFNASTVEALAN---RLRTRD------TGGSDDETLLLKRDI-----KLDDAIR---PSATAKA 1139
Cdd:TIGR03443 890 ELRKKLNVELplGLI--FKSPTIKGFAKevdRLKKGEeladegDSEIEEEETVLELDYakdakTLVDSLPksyPSRKELD 967
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1140 TSGTDHVFLTGATGFLGTYLLHELL---RDPERKVTCLVRGDD---GMSRLRQAFRQYDLPQSVLTERVTIVTGELSKPG 1213
Cdd:TIGR03443 968 ASTPITVFLTGATGFLGSFILRDLLtrrSNSNFKVFAHVRAKSeeaGLERLRKTGTTYGIWDEEWASRIEVVLGDLSKEK 1047
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1214 LGLAAADYDNIVRNADCIFHNGAEVHHLHRYERLRETNVLGIREILQLACAGEGRHVHYISTLSALTPRR---------- 1283
Cdd:TIGR03443 1048 FGLSDEKWSDLTNEVDVIIHNGALVHWVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVSSTSALDTEYyvnlsdelvq 1127
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1284 -GSGGDPrpvcELESVEGFVPPAG-GYNRSKWVAEHLVNEAGRRGLPVTIYRPGAISGDSVTGAFNGSDILCRLVQAYLY 1361
Cdd:TIGR03443 1128 aGGAGIP----ESDDLMGSSKGLGtGYGQSKWVAEYIIREAGKRGLRGCIVRPGYVTGDSKTGATNTDDFLLRMLKGCIQ 1203
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1362 TGTAPEGERLLDMLPVDHVARAIVHLSGKPASAGQ--VFHLIHSSPVSSARLFEACELEGIELKRVSQREWQDMLGD-VA 1438
Cdd:TIGR03443 1204 LGLIPNINNTVNMVPVDHVARVVVAAALNPPKESElaVAHVTGHPRIRFNDFLGTLKTYGYDVEIVDYVHWRKSLERfVI 1283
|
1370
....*....|..
gi 796556827 1439 RGTPDHPLYPLL 1450
Cdd:TIGR03443 1284 ERSEDNALFPLL 1295
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
53-1107 |
4.51e-127 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 440.37 E-value: 4.51e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 53 LAFLNMAHADAATpgqndIPPRN-ETCPPLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTV 131
Cdd:PRK05691 3236 LAQLTQAQLDALP-----VPAAEiEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEA 3310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 132 LRARIYSDKGVPK-QTISAACDAPFSVVEISPAAAA-----MEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTL 205
Cdd:PRK05691 3311 LRASFSWNAGETMlQVIHKPGRTPIDYLDWRGLPEDgqeqrLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSN 3390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 206 HHICADGWSTEILLKDLGAFYSAEVSGNatpEAELPI--QYGDFAAW-QRERLATEiagtlDAFWKQHLSQPRQTTQLVT 282
Cdd:PRK05691 3391 HHILIDAWCRSLLMNDFFEIYTALGEGR---EAQLPVppRYRDYIGWlQRQDLAQA-----RQWWQDNLRGFERPTPIPS 3462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 283 DmaRTAGHGHAGE-----LHDFTIEKETADA--LRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRP--HI 353
Cdd:PRK05691 3463 D--RPFLREHAGDsggmvVGDCYTRLDAADGarLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvsMP 3540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 354 ETEDLVGLFVNPLPVRSLVDPFG------NFEKALRETHATLRQvisHQDMPferIVDMVGVQRDPDSHPLFQIKFQLDA 427
Cdd:PRK05691 3541 QMQRTVGLFINSIALRVQLPAAGqrcsvrQWLQGLLDSNMELRE---YEYLP---LVAIQECSELPKGQPLFDSLFVFEN 3614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 428 APRErirlpglemrrlarqdkVSRLDLCLDLRET-EAGLSGT-----------------IEYKTALFRAETIGLFASHFQ 489
Cdd:PRK05691 3615 APVE-----------------VSVLDRAQSLNASsDSGRTHTnfpltavcypgddlglhLSYDQRYFDAPTVERLLGEFK 3677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 490 QLLKSIAADPCLPVATLALLTQEEQRQRICDFNSTAQEHAGPQYFHELFEAHVARAPQ-AAALIMPQAdaddiMTYGELN 568
Cdd:PRK05691 3678 RLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQrIAASCLDQQ-----WSYAELN 3752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 569 ARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVV--------SH 640
Cdd:PRK05691 3753 RAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVcsaacreqAR 3832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 641 SSIDLPKTANRLNLD--EDFPDDESAD-NLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDC 717
Cdd:PRK05691 3833 ALLDELGCANRPRLLvwEEVQAGEVAShNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADV 3912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 718 VLQFFSFSFDASIPELVMSLGAGARLLLLPR-YATLPGAELADIlRARHVTHLTMTPS---ALLSLPVDDLLSLRTVLVG 793
Cdd:PRK05691 3913 IAQTASQSFDISVWQFLAAPLFGARVEIVPNaIAHDPQGLLAHV-QAQGITVLESVPSliqGMLAEDRQALDGLRWMLPT 3991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 794 GEVPMPELIERWgkTRRF-----INAYGPTETTVNASM--VDMGGGRAG-LPVLRPAANKQLYVLDDNLELLPFGVPGEL 865
Cdd:PRK05691 3992 GEAMPPELARQW--LQRYpqiglVNAYGPAECSDDVAFfrVDLASTRGSyLPIGSPTDNNRLYLLDEALELVPLGAVGEL 4069
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 866 HIGGCGIARGYHDRAALTAERFVPDPFATDGRAgvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAH 945
Cdd:PRK05691 4070 CVAGTGVGRGYVGDPLRTALAFVPHPFGAPGER--LYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQ 4147
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 946 PAIVSATVAVRdDGRGGKRLAAYAVPqidQDAATRPTP--SEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLP 1023
Cdd:PRK05691 4148 AEVREAAVAVQ-EGVNGKHLVGYLVP---HQTVLAQGAllERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALP 4223
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1024 APR--AETDPDGRAPEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSLLATRFCAVAKDKFGLDIGVIDLFNASTVEA 1101
Cdd:PRK05691 4224 ALDigQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEE 4303
|
....*.
gi 796556827 1102 LANRLR 1107
Cdd:PRK05691 4304 LAEYIE 4309
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
535-1018 |
3.18e-123 |
|
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: 392.45 E-value: 3.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVARAPQAAALIMPQADaddiMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYL 614
Cdd:cd12115 2 HDLVEAQAARTPDAIALVCGDES----LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 615 PLDPEYPAERIGAMLSDAGARLVVshssidlpktanrlnldedfpddesadnletvTHSSQLAYVIYTSGSTGKAKGVLV 694
Cdd:cd12115 78 PLDPAYPPERLRFILEDAQARLVL--------------------------------TDPDDLAYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 695 DHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELvmslgagarllllprYATLP-GAE---------LADILRAR 764
Cdd:cd12115 126 EHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFEL---------------FGPLAtGGKvvladnvlaLPDLPAAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 765 HVTHLTMTPSALLSLPVDDLL--SLRTVLVGGEVPMPELIER-WGKT--RRFINAYGPTETTV--NASMVDMGGGRAgLP 837
Cdd:cd12115 191 EVTLINTVPSAAAELLRHDALpaSVRVVNLAGEPLPRDLVQRlYARLqvERVVNLYGPSEDTTysTVAPVPPGASGE-VS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 838 VLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIH 917
Cdd:cd12115 270 IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGAR---LYRTGDLVRWRPDGLLE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 918 VSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKF 997
Cdd:cd12115 347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVA----EPGAAGLVEDLRRHLGTRLPAY 422
|
490 500
....*....|....*....|.
gi 796556827 998 LVPDTFDWLEALPLTMNGKID 1018
Cdd:cd12115 423 MVPSRFVRLDALPLTPNGKID 443
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
546-1018 |
6.82e-122 |
|
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: 389.13 E-value: 6.82e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd17650 1 PDAIAVS----DATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVVSHssidlpktanrlnldedfPDDesadnletvthssqLAYVIYTSGSTGKAKGVLVDHSGLIN--LT 703
Cdd:cd17650 77 QYMLEDSGAKLLLTQ------------------PED--------------LAYVIYTSGTTGKPKGVMVEHRNVAHaaHA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 704 RDKIRACDVTADDcVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSalLSLPV-- 781
Cdd:cd17650 125 WRREYELDSFPVR-LLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPA--LIRPVma 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 782 ------DDLLSLRTVLVGGEVPMPE----LIERWGKTRRFINAYGPTETTVNASMVDMGGGRAG----LPVLRPAANKQL 847
Cdd:cd17650 202 yvyrngLDLSAMRLLIVGSDGCKAQdfktLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGdsanVPIGRPLPNTAM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 848 YVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRLDSQVK 927
Cdd:cd17650 282 YVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGER---MYRTGDLARWRADGNVELLGRVDHQVK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 928 IRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqdaATRPTPSEIRAWLANRLPKFLVPDTFDWLE 1007
Cdd:cd17650 359 IRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVA------AATLNTAELRAFLAKELPSYMIPSYYVQLD 432
|
490
....*....|.
gi 796556827 1008 ALPLTMNGKID 1018
Cdd:cd17650 433 ALPLTPNGKVD 443
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
535-1023 |
1.24e-119 |
|
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: 382.67 E-value: 1.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYL 614
Cdd:cd17645 1 HQLFEEQVERTPDHVAVV----DRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 615 PLDPEYPAERIGAMLSDAGARLVVSHssidlpktanrlnldedfPDDesadnletvthssqLAYVIYTSGSTGKAKGVLV 694
Cdd:cd17645 77 PIDPDYPGERIAYMLADSSAKILLTN------------------PDD--------------LAYVIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 695 DHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVThLTMTPS 774
Cdd:cd17645 125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 775 ALLSLPVD-DLLSLRTVLVGGEVpmPELIERwgKTRRFINAYGPTETTVNASMVDMGGGRAGLPVLRPAANKQLYVLDDN 853
Cdd:cd17645 204 GAAEQFMQlDNQSLRVLLTGGDK--LKKIER--KGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 854 LELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRI 933
Cdd:cd17645 280 LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGER---MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 934 EPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDaatrptPSEIRAWLANRLPKFLVPDTFDWLEALPLTM 1013
Cdd:cd17645 357 EPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIP------HEELREWLKNDLPDYMIPTYFVHLKALPLTA 430
|
490
....*....|
gi 796556827 1014 NGKIDPLKLP 1023
Cdd:cd17645 431 NGKVDRKALP 440
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
535-1018 |
5.10e-116 |
|
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: 374.19 E-value: 5.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVARAPQAAALimpqaDADDI-MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAY 613
Cdd:cd05918 2 HDLIEERARSQPDAPAV-----CAWDGsLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 614 LPLDPEYPAERIGAMLSDAGARLVVSHSsidlpktanrlnldedfPDDesadnletvthssqLAYVIYTSGSTGKAKGVL 693
Cdd:cd05918 77 VPLDPSHPLQRLQEILQDTGAKVVLTSS-----------------PSD--------------AAYVIFTSGSTGKPKGVV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 694 VDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELvmslgagarllllprYATL--------PGAE-----LADI 760
Cdd:cd05918 126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEI---------------FTTLaaggclciPSEEdrlndLAGF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 761 LRARHVTHLTMTPSALLSLPVDDLLSLRTVLVGGEVPMPELIERWGKTRRFINAYGPTETTVNASMVDMGGGRAGLPVLR 840
Cdd:cd05918 191 INRLRVTWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 841 PAANkQLYVLD--DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPF----ATDGRAGVLYRTGDRAVLLADG 914
Cdd:cd05918 271 PLGA-TCWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqEGSGRGRRLYRTGDLVRYNPDG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 915 RIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPA---IVSATVAVRDDGRGGKRLAAYAVPQIDQDAA------------- 978
Cdd:cd05918 350 SLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPgakEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSgdgdslflepsde 429
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 796556827 979 TRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd05918 430 FRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKID 469
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
79-499 |
3.41e-114 |
|
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: 367.13 E-value: 3.41e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 79 PPLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVV 158
Cdd:cd19540 2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 159 EISPAAAAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNAtPE- 237
Cdd:cd19540 82 VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA-PDw 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 238 AELPIQYGDFAAWQRERLATE------IAGTLDaFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRK 311
Cdd:cd19540 161 APLPVQYADYALWQRELLGDEddpdslAARQLA-YWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 312 IAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQ 391
Cdd:cd19540 240 LAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 392 VISHQDMPFERIVDMVGVQRDPDSHPLFQIKFQLDAAPRERIRLPGLEMRRLARQDKVSRLDLCLDLRE------TEAGL 465
Cdd:cd19540 320 AFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGL 399
|
410 420 430
....*....|....*....|....*....|....
gi 796556827 466 SGTIEYKTALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19540 400 TGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
79-499 |
4.62e-114 |
|
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: 366.70 E-value: 4.62e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 79 PPLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDK-GVPKQTISAACDAPFSV 157
Cdd:cd19539 2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 158 VEISPA----AAAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGN 233
Cdd:cd19539 82 RDLSDPdsdrERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 234 ATPEAELPIQYGDFAAWQRERLATEIAGTLDAFWKQHLsQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIA 313
Cdd:cd19539 162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRL-RGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 314 AAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVI 393
Cdd:cd19539 241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 394 SHQDMPFERIVDMVGVQRDPDSHPLFQIKFQLDAAPRERIRLPG-LEMRRLARQDKVSRLDLCLDLRETEAGLSGTIEYK 472
Cdd:cd19539 321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGgLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYA 400
|
410 420
....*....|....*....|....*..
gi 796556827 473 TALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19539 401 TSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
536-1022 |
1.14e-113 |
|
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: 365.86 E-value: 1.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALimpqADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:cd17653 1 DAFERIAAAHPDAVAV----ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLVVSHSSidlpktanrlnldedfPDDesadnletvthssqLAYVIYTSGSTGKAKGVLVD 695
Cdd:cd17653 77 LDAKLPSARIQAILRTSGATLLLTTDS----------------PDD--------------LAYIIFTSGSTGIPKGVMVP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 696 HSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGagarllllpRYATL----PGAELADIlrARHVTHLTM 771
Cdd:cd17653 127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLC---------NGGTLvladPSDPFAHV--ARTVDALMS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 772 TPSALLSLPVDDLLSLRTVLVGGEVPMPELIERWGKTRRFINAYGPTETTVNASMVDMgggRAGLPVL--RPAANKQLYV 849
Cdd:cd17653 196 TPSILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTEL---LPGQPVTigKPIPNSTCYI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 850 LDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRLDSQVKIR 929
Cdd:cd17653 273 LDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSR---MYRTGDYGRWTEDGGLEFLGREDNQVKVR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 930 GYRIEPGEIEARLLAHPAIVSATVAVRDDGrggkRLAAYAVPQ-IDQDAatrptpseIRAWLANRLPKFLVPDTFDWLEA 1008
Cdd:cd17653 350 GFRINLEEIEEVVLQSQPEVTQAAAIVVNG----RLVAFVTPEtVDVDG--------LRSELAKHLPSYAVPDRIIALDS 417
|
490
....*....|....
gi 796556827 1009 LPLTMNGKIDPLKL 1022
Cdd:cd17653 418 FPLTANGKVDRKAL 431
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
546-1023 |
3.31e-112 |
|
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: 362.49 E-value: 3.31e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALImpqaDADDIMTYGELNARANRLARLLRRKG-VSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAER 624
Cdd:cd17648 1 PDRVAVV----YGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 625 IGAMLSDAGARLVvshssidlpktanrlnldedfpddesadnletVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTR 704
Cdd:cd17648 77 IQFILEDTGARVV--------------------------------ITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 705 DKIRACDV--TADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSALLSLPVD 782
Cdd:cd17648 125 SLSERYFGrdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 783 DLLSLRTVLVGGEvpmpELIE-RWGKTR-----RFINAYGPTETTV-NASMVDMGGGRAGLPVLRPAANKQLYVLDDNLE 855
Cdd:cd17648 205 RLPHLKRVDAAGE----EFTApVFEKLRsrfagLIINAYGPTETTVtNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMK 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 856 LLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATD-----GRAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRG 930
Cdd:cd17648 281 RVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEqerarGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 931 YRIEPGEIEARLLAHPAIVSATVAVRDD-----GRGGKRLAAYAVPqidqDAATRPTpSEIRAWLANRLPKFLVPDTFDW 1005
Cdd:cd17648 361 QRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYLP----EPGHVPE-SDLLSFLRAKLPRYMVPARLVR 435
|
490
....*....|....*...
gi 796556827 1006 LEALPLTMNGKIDPLKLP 1023
Cdd:cd17648 436 LEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
546-1023 |
1.80e-111 |
|
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: 361.79 E-value: 1.80e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd17656 2 PDAVAVV----FENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVVS--HSSIDLPKTANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLT 703
Cdd:cd17656 78 IYIMLDSGVRVVLTqrHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 704 RDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILrARHVTHLTMTPSALLSLpvdd 783
Cdd:cd17656 158 HFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLV-KRHNIEVVFLPVAFLKF---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 784 LLSLRT-----------VLVGGEV-----PMPELIERWGKTrrFINAYGPTET-TVNASMVDMGGGRAGLPVL-RPAANK 845
Cdd:cd17656 233 IFSEREfinrfptcvkhIITAGEQlvitnEFKEMLHEHNVH--LHNHYGPSEThVVTTYTINPEAEIPELPPIgKPISNT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 846 QLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRLDSQ 925
Cdd:cd17656 311 WIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNER---MYRTGDLARYLPDGNIEFLGRADHQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 926 VKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIdqdaatRPTPSEIRAWLANRLPKFLVPDTFDW 1005
Cdd:cd17656 388 VKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ------ELNISQLREYLAKQLPEYMIPSFFVP 461
|
490
....*....|....*...
gi 796556827 1006 LEALPLTMNGKIDPLKLP 1023
Cdd:cd17656 462 LDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
546-1018 |
6.82e-110 |
|
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: 356.97 E-value: 6.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd12114 1 PDATAVI----CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVVSHSSIDLPK-TANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTR 704
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDvAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 705 DKIRACDVTADDCVLQFFSFSFDASI----------PELVMSLGAGARLLllpryatlpgAELADILRARHVTHLTMTPs 774
Cdd:cd12114 157 DINRRFAVGPDDRVLALSSLSFDLSVydifgalsagATLVLPDEARRRDP----------AHWAELIERHGVTLWNSVP- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 775 ALLSLPVD-------DLLSLRTVLVGGEVPMPELIERWGKTR---RFINAYGPTETTV--NA-SMVDMGGGRAGLPVLRP 841
Cdd:cd12114 226 ALLEMLLDvleaaqaLLPSLRLVLLSGDWIPLDLPARLRALApdaRLISLGGATEASIwsIYhPIDEVPPDWRSIPYGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 842 AANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPfatDGRAgvLYRTGDRAVLLADGRIHVSGR 921
Cdd:cd12114 306 LANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGER--LYRTGDLGRYRPDGTLEFLGR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 922 LDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDgRGGKRLAAYAVPqidQDAATRPTPSEIRAWLANRLPKFLVPD 1001
Cdd:cd12114 381 RDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGD-PGGKRLAAFVVP---DNDGTPIAPDALRAFLAQTLPAYMIPS 456
|
490
....*....|....*..
gi 796556827 1002 TFDWLEALPLTMNGKID 1018
Cdd:cd12114 457 RVIALEALPLTANGKVD 473
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
80-499 |
5.75e-106 |
|
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: 344.63 E-value: 5.75e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDA--PFSV 157
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEAtpKLEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 158 VEISPAAaaMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNATPE 237
Cdd:cd19538 83 KEVDEEE--LESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 238 AELPIQYGDFAAWQRERLATEIAGTLD-----AFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKI 312
Cdd:cd19538 161 APLPVQYADYALWQQELLGDESDPDSLiarqlAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 313 AAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRslVDPFGN--FEKALRETHATLR 390
Cdd:cd19538 241 AKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLR--TDTSGNpsFRELLERVKETNL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 391 QVISHQDMPFERIVDMVGVQRDPDSHPLFQIKFQLDAAPRERIRLPGLEMRRLARQDKVSRLDLCLDLRE-----TEAGL 465
Cdd:cd19538 319 EAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREqyndgTPNGI 398
|
410 420 430
....*....|....*....|....*....|....
gi 796556827 466 SGTIEYKTALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19538 399 EGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
1145-1407 |
1.07e-102 |
|
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 442549 [Multi-domain] Cd Length: 265 Bit Score: 328.71 E-value: 1.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1145 HVFLTGATGFLGTYLLHELLRDPERKVTCLVRGDD---GMSRLRQAFRQYDLPQSVLTERVTIVTGELSKPGLGLAAADY 1221
Cdd:COG3320 2 TVLLTGATGFLGAHLLRELLRRTDARVYCLVRASDeaaARERLEALLERYGLWLELDASRVVVVAGDLTQPRLGLSEAEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1222 DNIVRNADCIFHNGAEVHHLHRYERLRETNVLGIREILQLACAGEGRHVHYISTLSALTPRRGSGgdprpVCE---LESV 1298
Cdd:COG3320 82 QELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSG-----VFEeddLDEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1299 EGFvppAGGYNRSKWVAEHLVNEAGRRGLPVTIYRPGAISGDSVTGAFNGSDILCRLVQAYLYTGTAPE-GERLLDMLPV 1377
Cdd:COG3320 157 QGF---ANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKDDGFYRLLKGLLRLGAAPGlGDARLNLVPV 233
|
250 260 270
....*....|....*....|....*....|
gi 796556827 1378 DHVARAIVHLSGKPASAGQVFHLIHSSPVS 1407
Cdd:COG3320 234 DYVARAIVHLSRQPEAAGRTFHLTNPQPLS 263
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
534-1018 |
1.65e-96 |
|
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: 318.68 E-value: 1.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 534 FHELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAY 613
Cdd:COG0318 1 LADLLRRAAARHPDRPALV----FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 614 LPLDPEYPAERIGAMLSDAGARLVVShssidlpktanrlnldedfpddesadnletvthssqlAYVIYTSGSTGKAKGVL 693
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVT-------------------------------------ALILYTSGTTGRPKGVM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 694 VDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDAS-IPELVMSLGAGARLLLLPRYAtlpGAELADILRARHVTHLTMT 772
Cdd:COG0318 120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPRFD---PERVLELIERERVTVLFGV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 773 PS---ALLSLPV---DDLLSLRTVLVGGEvPMP-ELIERWGKT--RRFINAYGPTETTVNASM--VDMGGGRAGlPVLRP 841
Cdd:COG0318 197 PTmlaRLLRHPEfarYDLSSLRLVVSGGA-PLPpELLERFEERfgVRIVEGYGLTETSPVVTVnpEDPGERRPG-SVGRP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 842 AANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVpdpfatDGragvLYRTGDRAVLLADGRIHVSGR 921
Cdd:COG0318 275 LPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR------DG----WLRTGDLGRLDEDGYLYIVGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 922 LDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPD 1001
Cdd:COG0318 345 KKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVL----RPGAELDAEELRAFLRERLARYKVPR 420
|
490
....*....|....*..
gi 796556827 1002 TFDWLEALPLTMNGKID 1018
Cdd:COG0318 421 RVEFVDELPRTASGKID 437
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
80-516 |
2.50e-96 |
|
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: 318.51 E-value: 2.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDK-GVPKQTISAACDAPFSVV 158
Cdd:pfam00668 6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQEnGEPVQVILEERPFELEII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 159 EISPAAA-----AMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGN 233
Cdd:pfam00668 86 DISDLSEseeeeAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 234 ATPEAELPiQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIA 313
Cdd:pfam00668 166 PLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 314 AAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVI 393
Cdd:pfam00668 245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 394 SHQDMPFERIVDMVGVQRDPDSHPLFQIKFQLDAAPrerIRLPGLEMRRLARQD--------KVSRLDLCLDLRETEAGL 465
Cdd:pfam00668 325 PHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYL---GQDSQEEEFQLSELDlsvssvieEEAKYDLSLTASERGGGL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 796556827 466 SGTIEYKTALFRAETIGLFASHFQQLLKSIAADPCLPVATLALLTQEEQRQ 516
Cdd:pfam00668 402 TIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQK 452
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
542-1022 |
1.59e-93 |
|
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: 310.33 E-value: 1.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 542 VARAPQAAALimpqADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYP 621
Cdd:cd05945 1 AAANPDRPAV----VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 622 AERIGAMLSDAGARLVVShssidlpktanrlnldedFPDDesadnletvthssqLAYVIYTSGSTGKAKGVLVDHSGLIN 701
Cdd:cd05945 77 AERIREILDAAKPALLIA------------------DGDD--------------NAYIIFTSGSTGRPKGVQISHDNLVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 702 LTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSALLSLPV 781
Cdd:cd05945 125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 782 DDLL------SLRTVLVGGEV-PMP---ELIERWGKTRrFINAYGPTETTVNASMVDM----GGGRAGLPVLRPAANKQL 847
Cdd:cd05945 205 SPTFtpeslpSLRHFLFCGEVlPHKtarALQQRFPDAR-IYNTYGPTEATVAVTYIEVtpevLDGYDRLPIGYAKPGAKL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 848 YVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDpfatDGRAGvlYRTGDRAVLLADGRIHVSGRLDSQVK 927
Cdd:cd05945 284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD----EGQRA--YRTGDLVRLEADGLLFYRGRLDFQVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 928 IRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLE 1007
Cdd:cd05945 358 LNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVP---KPGAEAGLTKAIKAELAERLPPYMIPRRFVYLD 434
|
490
....*....|....*
gi 796556827 1008 ALPLTMNGKIDPLKL 1022
Cdd:cd05945 435 ELPLNANGKIDRKAL 449
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
1145-1430 |
1.85e-89 |
|
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187546 [Multi-domain] Cd Length: 290 Bit Score: 292.63 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1145 HVFLTGATGFLGTYLLHELLRDP-ERKVTCLVRG---DDGMSRLRQAFRQYDLPQSVL--TERVTIVTGELSKPGLGLAA 1218
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELLKRKnVSKIYCLVRAkdeEAALERLIDNLKEYGLNLWDEleLSRIKVVVGDLSKPNLGLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1219 ADYDNIVRNADCIFHNGAEVHHLHRYERLRETNVLGIREILQLACAGEGRHVHYISTLSALtprrGSGGDPRPVCELES- 1297
Cdd:cd05235 81 DDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVF----SAEEYNALDDEESDd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1298 -VEGFVPPAGGYNRSKWVAEHLVNEAGRRGLPVTIYRPGAISGDSVTGAFNGSDILCRLVQAYLYTGTAPEGERLLDMLP 1376
Cdd:cd05235 157 mLESQNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTDDFFWRLLKGCLQLGIYPISGAPLDLSP 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 796556827 1377 VDHVARAIVHLSGKPASAGQVFHLIHSSPVSSARLFEACELEGIELKRVSQREW 1430
Cdd:cd05235 237 VDWVARAIVKLALNESNEFSIYHLLNPPLISLNDLLDALEEKGYSIKEVSYEEW 290
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
538-929 |
2.14e-86 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 288.83 E-value: 2.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 538 FEAHVARAPQAAALIMpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLD 617
Cdd:pfam00501 1 LERQAARTPDKTALEV---GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 618 PEYPAERIGAMLSDAGARLVVSHSS---------------------IDLPKTANRLNLDEDFPDDESADNLETVTHSSQL 676
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDAlkleellealgklevvklvlvLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 677 AYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACD----VTADDCVLQFFSFSFDASIPELVMSLGAG-ARLLLLPRYAT 751
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAgATVVLPPGFPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 752 LPGAELADILRARHVTHLTMTPSAL------LSLPVDDLLSLRTVLVGGEVPMPELIERWGKT--RRFINAYGPTETTVN 823
Cdd:pfam00501 238 LDPAALLELIERYKVTVLYGVPTLLnmlleaGAPKRALLSSLRLVLSGGAPLPPELARRFRELfgGALVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 824 ASMVDMGGGRAGLP--VLRPAANKQLYVLDDN-LELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragv 900
Cdd:pfam00501 318 VTTPLPLDEDLRSLgsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW-------- 389
|
410 420
....*....|....*....|....*....
gi 796556827 901 lYRTGDRAVLLADGRIHVSGRLDSQVKIR 929
Cdd:pfam00501 390 -YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
1148-1384 |
3.30e-76 |
|
Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.
Pssm-ID: 462334 [Multi-domain] Cd Length: 257 Bit Score: 253.30 E-value: 3.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1148 LTGATGFLGTYLLHELLRDPE--RKVTCLVR---GDDGMSRLRQAFRQYDLPQSVL---TERVTIVTGELSKPGLGLAAA 1219
Cdd:pfam07993 1 LTGATGFLGKVLLEKLLRSTPdvKKIYLLVRakdGESALERLRQELEKYPLFDALLkeaLERIVPVAGDLSEPNLGLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1220 DYDNIVRNADCIFHNGAEVHHLHRYERLRETNVLGIREILQLACAGEG-RHVHYISTlSALTPRRGSGGDPRPVCELESV 1298
Cdd:pfam07993 81 DFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQlKPFHHVST-AYVNGERGGLVEEKPYPEGEDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1299 EGFV--------PPAGGYNRSKWVAEHLVNEAGRRGLPVTIYRPGAISGDSVTGAFNGSDILCRLVQAYLYTGTAPEG-- 1368
Cdd:pfam07993 160 MLLDedepallgGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWINNFDFGPRGLLGGIGKGVLPSIlg 239
|
250
....*....|....*...
gi 796556827 1369 --ERLLDMLPVDHVARAI 1384
Cdd:pfam07993 240 dpDAVLDLVPVDYVANAI 257
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
81-321 |
1.01e-70 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 237.24 E-value: 1.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 81 LSFAQERLWLIDqiyPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVVEI 160
Cdd:COG4908 1 LSPAQKRFLFLE---PGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 161 SPAA-----AAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNAT 235
Cdd:COG4908 78 SALPepereAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 236 PEAELPIQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIAAA 315
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237
|
....*.
gi 796556827 316 HGTTLF 321
Cdd:COG4908 238 HGATVN 243
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
80-498 |
1.04e-69 |
|
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: 241.40 E-value: 1.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVVE 159
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 ISPAA---AAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNatP 236
Cdd:cd20483 83 LSEAAdpeAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGR--D 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 237 EAELP---IQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQL----------VTDMARTaghghageLHDFTIEK 303
Cdd:cd20483 161 LATVPpppVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKLlpfakaerppVKDYERS--------TVEATLDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 304 ETADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALR 383
Cdd:cd20483 233 ELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 384 ETHATLRQVISHQDMPFERIVDMVGVQRDPdSH-PLFQIKF--QLDAAPRErIRLPGLEMRRLARQDKVSRLDLCLDLRE 460
Cdd:cd20483 313 STKTTCLEAYEHSAVPFDYIVDALDVPRST-SHfPIGQIAVnyQVHGKFPE-YDTGDFKFTDYDHYDIPTACDIALEAEE 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 796556827 461 T-EAGLSGTIEYKTALFRAETIGLFASHFQQLLKSIAAD 498
Cdd:cd20483 391 DpDGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
80-499 |
3.89e-68 |
|
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: 236.54 E-value: 3.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTIS-AACDAPFSVV 158
Cdd:cd19066 3 PLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLdKTVRFRIEII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 159 EISPAA---AAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNAT 235
Cdd:cd19066 83 DLRNLAdpeARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 236 PeAELPIQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIAAA 315
Cdd:cd19066 163 L-PPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 316 HGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVISH 395
Cdd:cd19066 242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 396 QDMPFERIVDMVGVQRDPDSHPLFQIKFQLDAAPRERIRLPGL-EMRRLARQDKVSRLDLCLDLRE-TEAGLSGTIEYKT 473
Cdd:cd19066 322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFiFTTPVYTSSEGTVFDLDLEASEdPDGDLLLRLEYSR 401
|
410 420
....*....|....*....|....*.
gi 796556827 474 ALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19066 402 GVYDERTIDRFAERYMTALRQLIENP 427
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
80-499 |
9.99e-68 |
|
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: 235.84 E-value: 9.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPfSVVE 159
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAAR-PELP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 ISPAAAA-MEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNATPEA 238
Cdd:cd19546 85 VVPATEEeLPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPERA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 239 ELPIQYGDFAAWQRERLATE-----IAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIA 313
Cdd:cd19546 165 PLPLQFADYALWERELLAGEddrdsLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 314 AAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTpVASRP--HIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQ 391
Cdd:cd19546 245 ESAGATMFTVVQAALAMLLTRLGAGTDVTVGT-VLPRDdeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVRE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 392 VISHQDMPFERIVDMVGVQRDPDSHPLFQIKFQL---DAAPRERIRLPGLEMRRLARQDKVSRLDLCLDLRETEA----- 463
Cdd:cd19546 324 ARRHQDVPFERLAELLALPPSADRHPVFQVALDVrddDNDPWDAPELPGLRTSPVPLGTEAMELDLSLALTERRNddgdp 403
|
410 420 430
....*....|....*....|....*....|....*..
gi 796556827 464 -GLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19546 404 dGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
675-1018 |
1.32e-64 |
|
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: 223.32 E-value: 1.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 675 QLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRyatLPG 754
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 755 AELADILRARHVTHLTMTPSALLSL------PVDDLLSLRTVLVGGEVPMPELIERWGKTR--RFINAYGPTETTVNASM 826
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEEAPgiKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 827 --VDMGGGRAGlPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVpdpfatDGragvLYRT 904
Cdd:cd04433 158 gpPDDDARKPG-SVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDE------DG----WYRT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 905 GDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPS 984
Cdd:cd04433 227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVL----RPGADLDAE 302
|
330 340 350
....*....|....*....|....*....|....
gi 796556827 985 EIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd04433 303 ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
80-499 |
1.66e-62 |
|
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: 220.02 E-value: 1.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDK--GVPKQTISAACDAPFSV 157
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPedGEPMQGVLASSPLRLEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 158 VEISPAAAAmEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYsaevsgNATPE 237
Cdd:cd19532 83 VQISDEAEV-EEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY------NGQPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 238 AELPIQYGDFAAWQRERLATeiaGTLD---AFWKQHLSQPRQTTQLVtDMARTA--------GHGHAgelhDFTIEKETA 306
Cdd:cd19532 156 LPPPLQYLDFAARQRQDYES---GALDedlAYWKSEFSTLPEPLPLL-PFAKVKsrppltryDTHTA----ERRLDAALA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 307 DALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETH 386
Cdd:cd19532 228 ARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 387 ATLRQVISHQDMPFERIVDMVGVQRDPDSHPLFQIKFQLDAAPRERIRLPGLEMRRLARQDkvSRL--DLCLDLRETEAG 464
Cdd:cd19532 308 DKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEGEEFED--ARTpyDLSLDIIDNPDG 385
|
410 420 430
....*....|....*....|....*....|....*..
gi 796556827 465 lSGTIEYKT--ALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19532 386 -DCLLTLKVqsSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
559-1018 |
3.03e-62 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 222.08 E-value: 3.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 559 DDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVV 638
Cdd:PRK04813 25 GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLII 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 639 SHSSIDLPKTANRLNLDEDFPDDESADNLETVTHSSQL---AYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTAD 715
Cdd:PRK04813 105 ATEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGddnYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 716 DCVLQFFSFSFDASipelVMSLGagarllllPRYAT------LPGAELADI------LRARHVTHLTMTPS----ALL-- 777
Cdd:PRK04813 185 PQFLNQAPYSFDLS----VMDLY--------PTLASggtlvaLPKDMTANFkqlfetLPQLPINVWVSTPSfadmCLLdp 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 778 SLPVDDLLSLRTVLVGGEVpMP-----ELIERWGKTRRFiNAYGPTETTVNASMV----DMGGGRAGLPVLRPAANKQLY 848
Cdd:PRK04813 253 SFNEEHLPNLTHFLFCGEE-LPhktakKLLERFPSATIY-NTYGPTEATVAVTSIeitdEMLDQYKRLPIGYAKPDSPLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 849 VLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFvpdpFATDG-RAgvlYRTGDRAVLlADGRIHVSGRLDSQVK 927
Cdd:PRK04813 331 IIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGqPA---YHTGDAGYL-EDGLLFYQGRIDFQIK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 928 IRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLE 1007
Cdd:PRK04813 403 LNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKFIYRD 482
|
490
....*....|.
gi 796556827 1008 ALPLTMNGKID 1018
Cdd:PRK04813 483 SLPLTPNGKID 493
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
80-499 |
5.56e-61 |
|
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: 215.53 E-value: 5.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLW---LIDqiyPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRAR-IYSDKGVPKQTISAACDAPF 155
Cdd:cd19543 3 PLSPMQEGMLfhsLLD---PGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSfVWEGLGEPLQVVLKDRKLPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 156 SVVEISPAAAAM-EDVIHA----ETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEV 230
Cdd:cd19543 80 RELDLSHLSEAEqEAELEAlaeeDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 231 SGNAtPEAELPIQYGDFAAW--QRERLATEiagtldAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADA 308
Cdd:cd19543 160 EGQP-PSLPPVRPYRDYIAWlqRQDKEAAE------AYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 309 LRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPH----IETedLVGLFVNPLPVRSLVDP---FGNFEKA 381
Cdd:cd19543 233 LQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAelpgIET--MVGLFINTLPVRVRLDPdqtVLELLKD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 382 LRETHATLRQvisHQDMPFERIvdmvgvQR-DPDSHPLFQ--IKFQ---LDAAPRERIRLPGLEMRRLARQDKVSrLDLC 455
Cdd:cd19543 311 LQAQQLELRE---HEYVPLYEI------QAwSEGKQALFDhlLVFEnypVDESLEEEQDEDGLRITDVSAEEQTN-YPLT 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 796556827 456 LDLRETEaGLSGTIEYKTALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19543 381 VVAIPGE-ELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
535-1017 |
2.53e-59 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 214.98 E-value: 2.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVARAPQAAALIMPQADADD-IMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAY 613
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEErTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 614 LPLDPEYPAERIGAMLSDAGARLVVSHSS-------IDLPKTA----------------NRLNLDEDFPDD--------E 662
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADGglrggkvIDLKEKVdealeelpslehvivvGRTGADVPMEGDldwdellaA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 663 SADNLETV-THSSQLAYVIYTSGSTGKAKGVLVDHSG-LINLTRDKIRACDVTADD---CV-----------LQFFSFSF 726
Cdd:COG0365 172 ASAEFEPEpTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDvfwCTadigwatghsyIVYGPLLN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 727 DASIpelVMslgagarLLLLPRYATlPGAeLADILrARH-VTHLTMTPSALLSL------PVD--DLLSLRTVLVGGEVP 797
Cdd:COG0365 252 GATV---VL-------YEGRPDFPD-PGR-LWELI-EKYgVTVFFTAPTAIRALmkagdePLKkyDLSSLRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 798 MPELIERWGKT--RRFINAYGPTETTVNasmvdMGGGRAGLPVlRP-AANKQLY-----VLDDNLELLPFGVPGELHIGG 869
Cdd:COG0365 319 NPEVWEWWYEAvgVPIVDGWGQTETGGI-----FISNLPGLPV-KPgSMGKPVPgydvaVVDEDGNPVPPGEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 870 --CGIARGYHDRAALTAERFVpdpfatDGRAGVlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPA 947
Cdd:COG0365 393 pwPGMFRGYWNDPERYRETYF------GRFPGW-YRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 796556827 948 IV-SATVAVRDDGRgGKRLAAYAV--PQIDQDAATRptpSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:COG0365 466 VAeAAVVGVPDEIR-GQVVKAFVVlkPGVEPSDELA---KELQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
79-499 |
2.71e-59 |
|
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: 211.02 E-value: 2.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 79 PPLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVV 158
Cdd:cd20484 2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 159 EISPAAAamEDV---IHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNAT 235
Cdd:cd20484 82 DISSLKE--SEIiayLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 236 PEAELPIQYGDFAAWQRERLATEIAGTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIAAA 315
Cdd:cd20484 160 TLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 316 HGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVISH 395
Cdd:cd20484 240 QSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 396 QDMPFERIVDMVGVQRDPDSHPLFQIKFQ----LDAAPRERIRLP-----GLEMRRLARQDkvSRLDLCLDLRETEAGLS 466
Cdd:cd20484 320 AAYPFPAMVRDLNIPRSQANSPVFQVAFFyqnfLQSTSLQQFLAEyqdvlSIEFVEGIHQE--GEYELVLEVYEQEDRFT 397
|
410 420 430
....*....|....*....|....*....|...
gi 796556827 467 GTIEYKTALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd20484 398 LNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
541-1018 |
1.32e-55 |
|
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: 200.53 E-value: 1.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEY 620
Cdd:cd17631 4 RARRHPDRTALV----FGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 621 PAERIGAMLSDAGARLVVshssidlpktanrlnldedfpDDesadnletvthssqLAYVIYTSGSTGKAKGVLVDHSGLI 700
Cdd:cd17631 80 TPPEVAYILADSGAKVLF---------------------DD--------------LALLMYTSGTTGRPKGAMLTHRNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 701 NLTRDKIRACDVTADD---CVLQFFSFSFD--ASIPELVmslgagarllllpRYATL-------PGAELADILRARhVTH 768
Cdd:cd17631 125 WNAVNALAALDLGPDDvllVVAPLFHIGGLgvFTLPTLL-------------RGGTVvilrkfdPETVLDLIERHR-VTS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 769 LTMTPS---ALLSLPV---DDLLSLRTVLVGGEvPMPE-LIERW-GKTRRFINAYGPTETTVNASMVDMGG-----GRAG 835
Cdd:cd17631 191 FFLVPTmiqALLQHPRfatTDLSSLRAVIYGGA-PMPErLLRALqARGVKFVQGYGMTETSPGVTFLSPEDhrrklGSAG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 836 lpvlRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVpdpfatDGragvLYRTGDRAVLLADGR 915
Cdd:cd17631 270 ----RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR------DG----WFHTGDLGRLDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 916 IHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQidqdAATRPTPSEIRAWLANRLP 995
Cdd:cd17631 336 LYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR----PGAELDEDELIAHCRERLA 411
|
490 500
....*....|....*....|...
gi 796556827 996 KFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd17631 412 RYKIPKSVEFVDALPRNATGKIL 434
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
546-1022 |
1.12e-53 |
|
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: 195.38 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALIMPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd17654 1 PDRPALIIDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGA-RLVVSHSSIDLPKTANRLNLDEDFPDDESadnletvthssqLAYVIYTSGSTGKAKGVLVDHSGLINLTR 704
Cdd:cd17654 81 LTVMKKCHVsYLLQNKELDNAPLSFTPEHRHFNIRTDEC------------LAYVIHTSGTTGTPKIVAVPHKCILPNIQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 705 DKIRACDVTADDcVLQFFSF-SFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARH-VTHLTMTPSALLSLPVD 782
Cdd:cd17654 149 HFRSLFNITSED-ILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRRFGSQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 783 DLL--------SLRTVLVGGEvPMPEL--IERW---GKTRRFINAYGPTETTVNASMVDMGGGRAGLPVLRPAANKQLYV 849
Cdd:cd17654 228 SIKstvlsatsSLRVLALGGE-PFPSLviLSSWrgkGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 850 LDDNlellPFGVPGELHIGgcGIARGYhdraaltaerFVPDPfaTDGRAGVLYRTGDRaVLLADGRIHVSGRLDSQVKIR 929
Cdd:cd17654 307 RDQN----GSEGTGQVFLG--GLNRVC----------ILDDE--VTVPKGTMRATGDF-VTVKDGELFFLGRKDSQIKRR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 930 GYRIEPGEIEARLLAHPAIVSATVAVRDDgrggKRLAAYAVPQIDQDaatrPTPSEIRAWLanrLPKFLVPDTFDWLEAL 1009
Cdd:cd17654 368 GKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGESSSS----RIHKELQLTL---LSSHAIPDTFVQIDKL 436
|
490
....*....|...
gi 796556827 1010 PLTMNGKIDPLKL 1022
Cdd:cd17654 437 PLTSHGKVDKSEL 449
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
536-1018 |
1.07e-51 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 190.08 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALIMPqadaDDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:cd05936 3 DLLEEAARRFPDKTALIFM----GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGAR-LVVSHSSIDLPKTANRLNLD-EDFPDDesadnletvthssqLAYVIYTSGSTGKAKGVL 693
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKaLIVAVSFTDLLAAGAPLGERvALTPED--------------VAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 694 VDHSGLI-NLTRDKIRACDV-TADD---CVLQFF-SFSFDASipeLVMSLGAGARLLLLPRYAtlPGAELADILRARhVT 767
Cdd:cd05936 145 LTHRNLVaNALQIKAWLEDLlEGDDvvlAALPLFhVFGLTVA---LLLPLALGATIVLIPRFR--PIGVLKEIRKHR-VT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 768 HLTMTP---SALLSLPVD---DLLSLRTVLVGGeVPMP-ELIERWGK-TR-RFINAYGPTET----TVNASMVDMGGGRA 834
Cdd:cd05936 219 IFPGVPtmyIALLNAPEFkkrDFSSLRLCISGG-APLPvEVAERFEElTGvPIVEGYGLTETspvvAVNPLDGPRKPGSI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 835 GLPVLrpaaNKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVpdpfatDGRagvlYRTGDRAVLLADG 914
Cdd:cd05936 298 GIPLP----GTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV------DGW----LRTGDIGYMDEDG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 915 RIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIV-SATVAVRDDgRGGKRLAAYAVPQIDQDaatrPTPSEIRAWLANR 993
Cdd:cd05936 364 YFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAeAAVVGVPDP-YSGEAVKAFVVLKEGAS----LTEEEIIAFCREQ 438
|
490 500
....*....|....*....|....*
gi 796556827 994 LPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd05936 439 LAGYKVPRQVEFRDELPKSAVGKIL 463
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
536-1017 |
9.88e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 179.72 E-value: 9.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:PRK07656 9 ELLARAARRFGDKEAYV----FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLV--------VSHSSIDLPKTANRLNLDEDFPDDESADNLETVT---------------H 672
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALfvlglflgVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTdflaagdpaerapevD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 673 SSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADD---CVLQFF-SFSFDAS-----------IPELVMSL 737
Cdd:PRK07656 165 PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylAANPFFhVFGYKAGvnaplmrgatiLPLPVFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 738 gagarllllpryatlpgAELADILRARHVTHL----TMTPSaLLSLP---VDDLLSLRTVLVGGEVPMPELIERWGKTRR 810
Cdd:PRK07656 245 -----------------DEVFRLIETERITVLpgppTMYNS-LLQHPdrsAEDLSSLRLAVTGAASMPVALLERFESELG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 811 F---INAYGPTETTVNASMVDMGGGRAGLP--VLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAE 885
Cdd:PRK07656 307 VdivLTGYGLSEASGVTTFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 886 RFVPDpfatdgraGVLYrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRL 965
Cdd:PRK07656 387 AIDAD--------GWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 796556827 966 AAYAVPQidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK07656 458 KAYVVLK----PGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKV 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
556-1017 |
1.03e-47 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 178.95 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 556 ADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGAR 635
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 636 LVVSHSSI---------------------DLPKTANRLNLDEDFPDDESADNLETV--THSSQLAYVIYTSGSTGKAKGV 692
Cdd:cd05911 85 VIFTDPDGlekvkeaakelgpkdkiivldDKPDGVLSIEDLLSPTLGEEDEDLPPPlkDGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 693 LVDHSGLIN---LTRDKIRACDvTADDCVLQFFSFSFDASIPELVMSLGAGArllllPRYaTLPGAELADILRA---RHV 766
Cdd:cd05911 165 CLSHRNLIAnlsQVQTFLYGND-GSNDVILGFLPLYHIYGLFTTLASLLNGA-----TVI-IMPKFDSELFLDLiekYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 767 THLTMTPSALLSL------PVDDLLSLRTVLVGGEvP----MPELIERWGKTRRFINAYGPTETTVNASMV---DMGGGR 833
Cdd:cd05911 238 TFLYLVPPIAAALakspllDKYDLSSLRVILSGGA-PlskeLQELLAKRFPNATIKQGYGMTETGGILTVNpdgDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 834 AGlpvlRPAANKQLYVLDDNL-ELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLA 912
Cdd:cd05911 317 VG----RLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW---------LHTGDIGYFDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 913 DGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAatrpTPSEIRAWLAN 992
Cdd:cd05911 384 DGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKL----TEKEVKDYVAK 459
|
490 500
....*....|....*....|....*..
gi 796556827 993 RLP--KFLVPDTFdWLEALPLTMNGKI 1017
Cdd:cd05911 460 KVAsyKQLRGGVV-FVDEIPKSASGKI 485
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
80-499 |
4.46e-47 |
|
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: 175.25 E-value: 4.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVVE 159
Cdd:cd19533 3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 ISPAAAAM---EDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNATP 236
Cdd:cd19533 83 LSGDPDPEgaaQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 237 EAELP---------IQYGDFAAWQRERlateiagtldAFWKQHLSQPRQTTQLVTdmaRTAGHGHAGELHDFTIEKETAD 307
Cdd:cd19533 163 PAPFGsfldlveeeQAYRQSERFERDR----------AFWTEQFEDLPEPVSLAR---RAPGRSLAFLRRTAELPPELTR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 308 ALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHA 387
Cdd:cd19533 230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 388 TLRQVISHQDMPFERIVDMVGVQRdpDSHPLFQIKFQLDAAPRE-RIRLPGLEMRRLArQDKVSRLDLCLDLRETEAGLS 466
Cdd:cd19533 310 ELRSLLRHQRYRYEDLRRDLGLTG--ELHPLFGPTVNYMPFDYGlDFGGVVGLTHNLS-SGPTNDLSIFVYDRDDESGLR 386
|
410 420 430
....*....|....*....|....*....|...
gi 796556827 467 GTIEYKTALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19533 387 IDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
563-1017 |
4.95e-47 |
|
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: 175.17 E-value: 4.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVshss 642
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 IDLpktanrlnldedfpddesadnletvthssqlAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADD-CVLQF 721
Cdd:cd05934 81 VDP-------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDvYLTVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 722 FSFSFDASIPELVMSLGAGARLLLLPRYAtlPGAELADILRARH-VTH-LTMTPSALLSLPVDDLLS---LRTVLVGGEV 796
Cdd:cd05934 130 PLFHINAQAVSVLAALSVGATLVLLPRFS--ASRFWSDVRRYGAtVTNyLGAMLSYLLAQPPSPDDRahrLRAAYGAPNP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 797 PM--PELIERWGKtrRFINAYGPTETTVnASMVDMGGGRAGLPVLRPAANKQLYVLDDNLELLPFGVPGELHI---GGCG 871
Cdd:cd05934 208 PElhEEFEERFGV--RLLEGYGMTETIV-GVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 872 IARGYHDRAALTAERFvpdpfatdgrAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIV-S 950
Cdd:cd05934 285 FFKGYYNMPEATAEAM----------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVReA 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 951 ATVAVRDDGRGGKRLAAYAVPQidqdaATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05934 355 AVVAVPDEVGEDEVKAVVVLRP-----GETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
1146-1405 |
4.36e-46 |
|
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187573 [Multi-domain] Cd Length: 293 Bit Score: 168.31 E-value: 4.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDpERKVTCLVRGDDGmSRLRQAFRQYDLPQsvltERVTIVTGELSKPGLGLAAADYDNIV 1225
Cdd:cd05263 1 VFVTGGTGFLGRHLVKRLLEN-GFKVLVLVRSESL-GEAHERIEEAGLEA----DRVRVLEGDLTQPNLGLSAAASRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNADCIFHNGAEVHHLHRYERLRETNVLGIREILQLACAGEGRHVHYISTLSALTPRRGSGGdprpVCELESVEGFVppa 1305
Cdd:cd05263 75 GKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAGNREGNIR----ETELNPGQNFK--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1306 GGYNRSKWVAEHLVNEAGRRgLPVTIYRPGAISGDSVTGAFNGSDILCRLVQAYLYTGTAP-----EGERLlDMLPVDHV 1380
Cdd:cd05263 148 NPYEQSKAEAEQLVRAAATQ-IPLTVYRPSIVVGDSKTGRIEKIDGLYELLNLLAKLGRWLpmpgnKGARL-NLVPVDYV 225
|
250 260
....*....|....*....|....*
gi 796556827 1381 ARAIVHLSGKPASAGQVFHLIHSSP 1405
Cdd:cd05263 226 ADAIVYLSKKPEANGQIFHLTDPTP 250
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
527-1018 |
5.95e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 171.52 E-value: 5.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 527 EHAGPQYFHELFEAHVARAPQAAALIMPqadaDDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAV 606
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFD----GRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 607 WKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSSI---------DLP-------------KTANRLNLD-EDFPDDES 663
Cdd:PRK06187 77 PKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFvpllaailpQLPtvrtvivegdgpaAPLAPEVGEyEELLAAAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 664 ADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVL----QFFSFSFDASipelVMSLGA 739
Cdd:PRK06187 157 DTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLP----YLALMA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 740 GARLLLLPRYatlPGAELADILRARHVTHLTMTPS---ALLSLPV---DDLLSLRTVLVGGEvPMPE-LIERWGKT--RR 810
Cdd:PRK06187 233 GAKQVIPRRF---DPENLLDLIETERVTFFFAVPTiwqMLLKAPRayfVDFSSLRLVIYGGA-ALPPaLLREFKEKfgID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 811 FINAYGPTETTVNASMV-----DMGG----GRAGlpvlRPAANKQLYVLDDNLELLP--FGVPGELHIGGCGIARGYHDR 879
Cdd:PRK06187 309 LVQGYGMTETSPVVSVLppedqLPGQwtkrRSAG----RPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 880 AALTAERFVPDpfatdgragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATV-AVRDD 958
Cdd:PRK06187 385 PEATAETIDGG----------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAViGVPDE 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 959 gRGGKRLAAYAVPQIDQDaatrPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:PRK06187 455 -KWGERPVAVVVLKPGAT----LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKIL 509
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
562-1017 |
2.21e-44 |
|
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: 167.66 E-value: 2.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHS 641
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 SIDlpktanrlnldedfpddesadnletvthssQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQF 721
Cdd:cd05935 82 ELD------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILAC 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 722 FSFSFDASIPELVMSlgagarllllPRYAtlpGAE-----------LADILRARHVTHLTMTPSALLSLPVD------DL 784
Cdd:cd05935 132 LPLFHVTGFVGSLNT----------AVYV---GGTyvlmarwdretALELIEKYKVTFWTNIPTMLVDLLATpefktrDL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 785 LSLRtVLVGGEVPMPE-LIERWGKTR--RFINAYGPTETTVNASMVDMGggRAGLPVLR-PAANKQLYVLD-DNLELLPF 859
Cdd:cd05935 199 SSLK-VLTGGGAPMPPaVAEKLLKLTglRFVEGYGLTETMSQTHTNPPL--RPKLQCLGiP*FGVDARVIDiETGRELPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 860 GVPGELHIGGCGIARGYHDRAALTAERFVPDpfatDGRAgvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIE 939
Cdd:cd05935 276 NEVGEIVVRGPQIFKGYWNRPEETEESFIEI----KGRR--FFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 940 ARLLAHPAIVSATVAVRDDGRGGKRLAAYAVpqIDQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05935 350 AKLYKHPAI*EVCVISVPDERVGEEVKAFIV--LRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
563-1022 |
1.01e-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: 165.63 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVshss 642
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 idLPKTANRLNLDEDfPDDesadnletvthssqLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVL--- 719
Cdd:cd05903 79 --VPERFRQFDPAAM-PDA--------------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLvas 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 ---QFFSFSFDASIPeLVMSLGAGARLLLLPRYAtlpgaelADILRARHVTHLTMTPSALLSL------PVDDLLSLRTV 790
Cdd:cd05903 142 pmaHQTGFVYGFTLP-LLLGAPVVLQDIWDPDKA-------LALMREHGVTFMMGATPFLTDLlnaveeAGEPLSRLRTF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 791 LVGGEVPMPELIER-WGKTRRFI-NAYGPTET-TVNASMVDMGGGRAGLPVLRPAANKQLYVLDDNLELLPFGVPGELHI 867
Cdd:cd05903 214 VCGGATVPRSLARRaAELLGAKVcSAYGSTECpGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 868 GGCGIARGYHDRAALTAErfvpdpFATDGragvLYRTGDRAVLLADGRIHVSGRlDSQVKIR-GYRIEPGEIEARLLAHP 946
Cdd:cd05903 294 RGPSVFLGYLDRPDLTAD------AAPEG----WFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLEVEDLLLGHP 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 947 AIVSATVAVRDDGRGGKRLAAYAVPQidqdAATRPTPSEIRAWL-ANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:cd05903 363 GVIEAAVVALPDERLGERACAVVVTK----SGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
546-1022 |
1.80e-42 |
|
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: 163.64 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALIMPQADADdiMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:cd05926 1 PDAPALVVPGSTPA--LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVVSHSSIDLP--KTANRLNL-----------------DEDFP---DDESADNLETVTHSSQLAYVIYTS 683
Cdd:cd05926 79 EFYLADLGSKLVLTPKGELGPasRAASKLGLailelaldvgvlirapsAESLSnllADKKNAKSEGVPLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 684 GSTGKAKGVLVDHSGLINLTRDKIRACDVTADD---CVLQFFsfsfdaSIPELVMSlgagarlLLLPRYA----TLPGAE 756
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNITNTYKLTPDDrtlVVMPLF------HVHGLVAS-------LLSTLAAggsvVLPPRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 757 LA----DILRARHVTHLTMTP---SALL----SLPVDDLLSLRTVLVGGEvPMPELIERwGKTRRF----INAYGPTETT 821
Cdd:cd05926 226 SAstfwPDVRDYNATWYTAVPtihQILLnrpePNPESPPPKLRFIRSCSA-SLPPAVLE-ALEATFgapvLEAYGMTEAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 822 --VNASMVDMGG---GRAGLPVlrpaaNKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdg 896
Cdd:cd05926 304 hqMTSNPLPPGPrkpGSVGKPV-----GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW---- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 897 ragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSA-TVAVRDDgRGGKRLAAYAVPQidq 975
Cdd:cd05926 375 -----FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAvAFGVPDE-KYGEEVAAAVVLR--- 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 796556827 976 dAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:cd05926 446 -EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
569-1018 |
1.21e-41 |
|
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: 160.30 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 569 ARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGA----YLPLDPEYPAERIGAMLSDAGARLVVSHSS-- 642
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 --IDLPKTANR---LNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDC 717
Cdd:cd05922 81 drLRDALPASPdpgTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 718 VLQFFSFSFDASIPELVMSLGAGARLLLLPRYatLPGAELADILRARHVTHLTMTPSA---LLSLPVDD--LLSLRTVL- 791
Cdd:cd05922 161 ALTVLPLSYDYGLSVLNTHLLRGATLVLTNDG--VLDDAFWEDLREHGATGLAGVPSTyamLTRLGFDPakLPSLRYLTq 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 792 VGGEVPmPELIERW---GKTRRFINAYGPTE-----TTVNASMVDMGGGRAGLPVlrpaANKQLYVLDDNLELLPFGVPG 863
Cdd:cd05922 239 AGGRLP-QETIARLrelLPGAQVYVMYGQTEatrrmTYLPPERILEKPGSIGLAI----PGGEFEILDDDGTPTPPGEPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 864 ELHIGGCGIARGYHDRAaltaerfvPDPFATDGRAGVLYrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLL 943
Cdd:cd05922 314 EIVHRGPNVMKGYWNDP--------PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAAR 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 796556827 944 AHPAIVSAtVAVRDDGRGGKRLAAYAVpqidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd05922 385 SIGLIIEA-AAVGLPDPLGEKLALFVT------APDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
557-1018 |
1.73e-41 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 159.38 E-value: 1.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 557 DADDIMTYGELNARANRLARLLRRKGVSAE-TVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGAR 635
Cdd:cd05941 7 DDGDSITYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 636 LVVshssidlpktanrlnldedfpddesadnletvthssQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTAD 715
Cdd:cd05941 87 LVL------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 716 DCVLQF------------------------FSFSFDASIPELVMSLGAGARLLLLP----RYATLPGAELADILRARHVT 767
Cdd:cd05941 131 DVLLHVlplhhvhglvnallcplfagasveFLPKFDPKEVAISRLMPSITVFMGVPtiytRLLQYYEAHFTDPQFARAAA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 768 ----HLTMTPSALLSLPVDDLLSLRTvlvgGEVpmpeLIERwgktrrfinaYGPTETTVNASMVDMGGGRAGlPVLRPAA 843
Cdd:cd05941 211 aerlRLMVSGSAALPVPTLEEWEAIT----GHT----LLER----------YGMTEIGMALSNPLDGERRPG-TVGMPLP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 844 NKQLYVLDDN-LELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRL 922
Cdd:cd05941 272 GVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW---------FKTGDLGVVDEDGYYWILGRS 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 923 -DSQVKIRGYRIEPGEIEARLLAHPAIV-SATVAVRDDGRgGKRLAAYAVPqidQDAATRPTPSEIRAWLANRLPKFLVP 1000
Cdd:cd05941 343 sVDIIKSGGYKVSALEIERVLLAHPGVSeCAVIGVPDPDW-GERVVAVVVL---RAGAAALSLEELKEWAKQRLAPYKRP 418
|
490
....*....|....*...
gi 796556827 1001 DTFDWLEALPLTMNGKID 1018
Cdd:cd05941 419 RRLILVDELPRNAMGKVN 436
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
563-1018 |
2.39e-41 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 158.77 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSS 642
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 IDLpKTANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDC---VL 719
Cdd:TIGR01923 81 LEE-KDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNwllSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 QFFSFSFDASIPELVMSLgagarllllpryATL----PGAELADILRARHVTHLTMTPSALLSLPVDDL--LSLRTVLVG 793
Cdd:TIGR01923 160 PLYHISGLSILFRWLIEG------------ATLrivdKFNQLLEMIANERVTHISLVPTQLNRLLDEGGhnENLRKILLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 794 GE-VPMPeLIERwGKTRRF--INAYGPTET--TVNASMVDMGGGRAGlpVLRPAANKQLYVLDDNLEllpfgVPGELHIG 868
Cdd:TIGR01923 228 GSaIPAP-LIEE-AQQYGLpiYLSYGMTETcsQVTTATPEMLHARPD--VGRPLAGREIKIKVDNKE-----GHGEIMVK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 869 GCGIARGYHDRAALTAERFVPDPFatdgragvlyRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAI 948
Cdd:TIGR01923 299 GANLMKGYLYQGELTPAFEQQGWF----------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGI 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 949 VSATVAVRDDGRGGKRLAAYAVPQIDQDAAtrptpsEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:TIGR01923 369 QEAVVVPKPDAEWGQVPVAYIVSESDISQA------KLIAYLTEKLAKYKVPIAFEKLDELPYNASGKIL 432
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
80-498 |
3.76e-41 |
|
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: 156.96 E-value: 3.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISaacdapfsvvE 159
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYS----------S 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 160 ISPAAAAMEDV-IHAETSRPFDLAAEPPIRLLVAKCddghhVLVFTLHHICADGWSTEILLKDLGAFYSaevsGNATPEA 238
Cdd:cd19537 73 SPPRVQRVDTLdVWKEINRPFDLEREDPIRVFISPD-----TLLVVMSHIICDLTTLQLLLREVSAAYN----GKLLPPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 239 ELpiQYGDFAAWQRERLATEIAgtldaFWKQHLSQPrqttQLVTDMARTAGHGHAGELHDFTIEKETADALRKIAAAHGT 318
Cdd:cd19537 144 RR--EYLDSTAWSRPASPEDLD-----FWSEYLSGL----PLLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 319 TLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIETEDLVGLFVNPLPVRSLVDPFGNFEKA--LRETHATLRQVISHQ 396
Cdd:cd19537 213 TLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPSSSDASAAdfLRAVRRSSQAALAHA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 397 dMPFERIVDMVGVQRDPDSHPLFQI--KFQLDAAPRERIRLPGLEMRRL--------------ARQDKvsrldlCLDLRe 460
Cdd:cd19537 293 -IPWHQLLEHLGLPPDSPNHPLFDVmvTFHDDRGVSLALPIPGVEPLYTwaegakfplmfeftALSDD------SLLLR- 364
|
410 420 430
....*....|....*....|....*....|....*...
gi 796556827 461 teaglsgtIEYKTALFRAETIGLFASHFQQLLKSIAAD 498
Cdd:cd19537 365 --------LEYDTDCFSEEEIDRIESLILAALELLVEG 394
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
80-499 |
1.51e-40 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 156.07 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRAR-IYSDKGVPKQTISAACDAPFSVV 158
Cdd:cd19536 3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSfIEDGLGQPVQVVHRQAQVPVTEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 159 EISP---AAAAMEDVIHAETSRPFDLAAEPPIRL-LVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGna 234
Cdd:cd19536 83 DLTPleeQLDPLRAYKEETKIRRFDLGRAPLVRAaLVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEY-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 235 TPEAELPIQ-YGDFAAWQRERLATEiagTLDAFWKQHLSQPRQTTQLVTDMARTAGHGHAGELhDFTIEKETadALRKIA 313
Cdd:cd19536 161 KPLSLPPAQpYRDFVAHERASIQQA---ASERYWREYLAGATLATLPALSEAVGGGPEQDSEL-LVSVPLPV--RSRSLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 314 AAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASRPHIET--EDLVGLFVNPLPVRsLVDPFGNFEKALRETHATLRQ 391
Cdd:cd19536 235 KRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTgaERLLGLFLNTLPLR-VTLSEETVEDLLKRAQEQELE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 392 VISHQDMPFERIvdmvgvQRDPDSHPLFQIKFQL------DAAPrERIRLPGLEMRRLARQDKvSRLDLCLDLRETEAGL 465
Cdd:cd19536 314 SLSHEQVPLADI------QRCSEGEPLFDSIVNFrhfdldFGLP-EWGSDEGMRRGLLFSEFK-SNYDVNLSVLPKQDRL 385
|
410 420 430
....*....|....*....|....*....|....
gi 796556827 466 SGTIEYKTALFRAETIGLFASHFQQLLKSIAADP 499
Cdd:cd19536 386 ELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
563-1022 |
4.33e-40 |
|
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: 154.80 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVshss 642
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 idlpktanrlnldedfpddesadnletvTHSSQLAYVIYTSGSTGKAKGVLVDHS----------GLINLTRDKIRACdv 712
Cdd:cd05972 78 ----------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSyplghiptaaYWLGLRPDDIHWN-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 713 TADDCVLQFFSFSFDAsipelVMSLGAGARLLLLPRYAtlpgAELA-DILRARHVTHLTMTPSAL-----LSLPVDDLLS 786
Cdd:cd05972 128 IADPGWAKGAWSSFFG-----PWLLGATVFVYEGPRFD----AERIlELLERYGVTSFCGPPTAYrmlikQDLSSYKFSH 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 787 LRTVLVGGEVPMPELIERW----GKTRRfiNAYGPTETTV---NASMVDMGGGRAGlpvlRPAANKQLYVLDDNLELLPF 859
Cdd:cd05972 199 LRLVVSAGEPLNPEVIEWWraatGLPIR--DGYGQTETGLtvgNFPDMPVKPGSMG----RPTPGYDVAIIDDDGRELPP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 860 GVPGEL--HIGGCGIARGYHDRAALTAERFVPDpfatdgragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGE 937
Cdd:cd05972 273 GEEGDIaiKLPPPGLFLGYVGDPEKTEASIRGD----------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 938 IEARLLAHPAIV-SATVAVRDDGRgGKRLAAYAVPQiDQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGK 1016
Cdd:cd05972 343 VESALLEHPAVAeAAVVGSPDPVR-GEVVKAFVVLT-SGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGK 420
|
....*.
gi 796556827 1017 IDPLKL 1022
Cdd:cd05972 421 IRRVEL 426
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
549-1022 |
2.22e-39 |
|
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: 154.45 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 549 AALIMPQadadDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAM 628
Cdd:cd05959 21 TAFIDDA----GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 629 LSDAGARLVVSHSSIdLPKTANRLNLDE----------------------DFPDDESADNLETVTHSSQLAYVIYTSGST 686
Cdd:cd05959 97 LEDSRARVVVVSGEL-APVLAAALTKSEhtlvvlivsggagpeagalllaELVAAEAEQLKPAATHADDPAFWLYSSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 687 GKAKGVLVDHSGLINLTRDKIR-ACDVTADDCVLQ--------------FFSFSFDASIpeLVMslgagarllllPRYAT 751
Cdd:cd05959 176 GRPKGVVHLHADIYWTAELYARnVLGIREDDVCFSaaklffayglgnslTFPLSVGATT--VLM-----------PERPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 752 lPGAELADILRARhvthltmtPSALLSLPV-------------DDLLSLRTVLVGGEvPMPELI-ERWgkTRRF----IN 813
Cdd:cd05959 243 -PAAVFKRIRRYR--------PTVFFGVPTlyaamlaapnlpsRDLSSLRLCVSAGE-ALPAEVgERW--KARFgldiLD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 814 AYGPTEttvnasMV---------DMGGGRAGLPVlrpaANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTA 884
Cdd:cd05959 311 GIGSTE------MLhiflsnrpgRVRYGTTGKPV----PGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 885 ERFVpdpfatdgraGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKR 964
Cdd:cd05959 381 DTFQ----------GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTK 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 796556827 965 LAAYAVP---QIDQDAATRptpsEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:cd05959 451 PKAFVVLrpgYEDSEALEE----ELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
535-1017 |
1.03e-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: 154.27 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVARAPQAAALIMPQADADDIMT--YGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGA 612
Cdd:cd17634 56 ANALDRHLRENGDRTAIIYEGDDTSQSRTisYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 613 YLPLDPEYPAERIGAMLSDAGARLVVSHS-------SIDLPKTANR-LNLD---------------------------ED 657
Cdd:cd17634 136 HSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrSVPLKKNVDDaLNPNvtsvehvivlkrtgsdidwqegrdlwwRD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 658 FPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSG-LINLTRDKIRACDVTADDCVLQFFSFSFDASIPELV-- 734
Cdd:cd17634 216 LIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLyg 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 735 --MSLGAGARLLLLPRYATlPGAeLADILRARHVTHLTMTPSALLSL-PVD-------DLLSLRTVLVGGEVPMPE---- 800
Cdd:cd17634 296 plACGATTLLYEGVPNWPT-PAR-MWQVVDKHGVNILYTAPTAIRALmAAGddaiegtDRSSLRILGSVGEPINPEayew 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 801 LIERWGKTRR-FINAYGPTETtvNASMVDMGGG----RAGLPVlRPAANKQLYVLDDNLELLPFGVPGELHIGGC--GIA 873
Cdd:cd17634 374 YWKKIGKEKCpVVDTWWQTET--GGFMITPLPGaielKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQT 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 874 RGYHDRAaltaERFVPDPFAT-DGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIV-SA 951
Cdd:cd17634 451 RTLFGDH----ERFEQTYFSTfKG----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAeAA 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 796556827 952 TVAVRDDGRgGKRLAAYAVPQidqdAATRPTP---SEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd17634 523 VVGIPHAIK-GQAPYAYVVLN----HGVEPSPelyAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
562-1017 |
4.14e-38 |
|
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: 149.21 E-value: 4.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHS 641
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 sidlpktANRLNLDEDfpddesadnletvthssqLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDcvlQF 721
Cdd:cd05973 81 -------ANRHKLDSD------------------PFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED---SF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 722 FSFS--------FDASIPELVMSLGAGArllllprYATLPGAELA-DILRARHVTHLTMTPSALLSL-------PVDDLL 785
Cdd:cd05973 133 WNAAdpgwayglYYAITGPLALGHPTIL-------LEGGFSVESTwRVIERLGVTNLAGSPTAYRLLmaagaevPARPKG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 786 SLRTVLVGGEVPMPELIeRWGKTRRFI---NAYGPTE--TTVN-----ASMVDMGGGRAGLPVLRPAankqlyVLDDNLE 855
Cdd:cd05973 206 RLRRVSSAGEPLTPEVI-RWFDAALGVpihDHYGQTElgMVLAnhhalEHPVHAGSAGRAMPGWRVA------VLDDDGD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 856 LLPFGVPGELHIggcgiargyhDRAALTAERF----VPDPFATDGRagvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGY 931
Cdd:cd05973 279 ELGPGEPGRLAI----------DIANSPLMWFrgyqLPDTPAIDGG---YYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 932 RIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQidqdAATRPTPS---EIRAWLANRLPKFLVPDTFDWLEA 1008
Cdd:cd05973 346 RIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLR----GGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDE 421
|
....*....
gi 796556827 1009 LPLTMNGKI 1017
Cdd:cd05973 422 LPKTPSGKI 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
542-993 |
5.19e-38 |
|
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: 150.46 E-value: 5.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 542 VARAPQAAALImpQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYP 621
Cdd:cd05904 15 ASAHPSRPALI--DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 622 AERIGAMLSDAGARLVVSHSSI--DLPKTANRLNLDEDFPDDESADNLETVT-----------HSSQLAYVIYTSGSTGK 688
Cdd:cd05904 93 PAEIAKQVKDSGAKLAFTTAELaeKLASLALPVVLLDSAEFDSLSFSDLLFEadeaeppvvviKQDDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 689 AKGVLVDHSGLINLTR--DKIRACDVTADD---CVLQFF---SFSF------DASIPELVMslgagarllllPRYatlpg 754
Cdd:cd05904 173 SKGVMLTHRNLIAMVAqfVAGEGSNSDSEDvflCVLPMFhiyGLSSfalgllRLGATVVVM-----------PRF----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 755 aELADILRA--RH-VTHLTMTPSALLSLP----VD--DLLSLRTVLVGGEVPMPELIERWGK---TRRFINAYGPTETTV 822
Cdd:cd05904 237 -DLEELLAAieRYkVTHLPVVPPIVLALVkspiVDkyDLSSLRQIMSGAAPLGKELIEAFRAkfpNVDLGQGYGMTESTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 823 NASMVD---MGGGRAGlPVLRPAANKQLYVLD-DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDpfatdgra 898
Cdd:cd05904 316 VVAMCFapeKDRAKYG-SVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE-------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 899 GVLyRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAa 978
Cdd:cd05904 387 GWL-HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSL- 464
|
490
....*....|....*
gi 796556827 979 trpTPSEIRAWLANR 993
Cdd:cd05904 465 ---TEDEIMDFVAKQ 476
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
96-499 |
1.79e-37 |
|
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: 146.30 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 96 PGSALHHIciALEVRGALDLDALKVALAGVMSRHTVLRARIY--SDKGVPKQTISAACDAPFSVVEISpaaaamEDVIHA 173
Cdd:cd19542 19 PGLYFNHF--VFDLDSSVDVERLRNAWRQLVQRHDILRTVFVesSAEGTFLQVVLKSLDPPIEEVETD------EDSLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 174 ETSRPFD---LAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNATPeaelpiqYGDFAAW 250
Cdd:cd19542 91 LTRDLLDdptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPP-------FSDYISY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 251 QRERLATEIAgtldAFWKQHLsqprQTTQLVTDMARTAGHGHAGELHdftIEKETADALRKIAAAHGTTLFTALFTAFNL 330
Cdd:cd19542 164 LQSQSQEESL----QYWRKYL----QGASPCAFPSLSPKRPAERSLS---STRRSLAKLEAFCASLGVTLASLFQAAWAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 331 LIHRYTGQTDLVIGTPVASR--PHIETEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLRQVISHQDMPFERIVDMVG 408
Cdd:cd19542 233 VLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 409 VQRdpdSHPLFQ--IKFQLDAAPRERIRLPGLEMRRLARQDKVSrLDLCLDLRETEAGLSGTIEYKTALFRAETIGLFAS 486
Cdd:cd19542 313 LWP---SGTLFNtlVSYQNFEASPESELSGSSVFELSAAEDPTE-YPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLE 388
|
410
....*....|...
gi 796556827 487 HFQQLLKSIAADP 499
Cdd:cd19542 389 QFDDILEALLANP 401
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
534-1018 |
3.37e-37 |
|
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: 148.37 E-value: 3.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 534 FHELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSA-ETVVaISLPRSFDMIVAWLAVWKAGGA 612
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVV----DGERRLSYAELDRRADRLAAGLLALGLRPgDRVV-VQLPNVAEFVIVFFALFRAGAI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 613 ylpldPEY--PAER---IGAMLSDAGARLVV---SHSSIDLPKTANRLNldEDFP--------------------DDESA 664
Cdd:COG1021 102 -----PVFalPAHRraeISHFAEQSEAVAYIipdRHRGFDYRALARELQ--AEVPslrhvlvvgdageftsldalLAAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 665 DNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADD---CVLQFfSFSFDASIP---------- 731
Cdd:COG1021 175 DLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTvylAALPA-AHNFPLSSPgvlgvlyagg 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 732 ELVMSLGagarllllpryatlPGAELADILRARH-VTHLTMTPSALL----SLPVD--DLLSLRTVLVGGEVPMPELIER 804
Cdd:COG1021 254 TVVLAPD--------------PSPDTAFPLIERErVTVTALVPPLALlwldAAERSryDLSSLRVLQVGGAKLSPELARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 805 WGKTR--RFINAYG-------------PTETTVNASmvdmgggraGLPVlrpAANKQLYVLDDNLELLPFGVPGELHIGG 869
Cdd:COG1021 320 VRPALgcTLQQVFGmaeglvnytrlddPEEVILTTQ---------GRPI---SPDDEVRIVDEDGNPVPPGEVGELLTRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 870 CGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRLDSQVkIR-GYRIEPGEIEARLLAHPAI 948
Cdd:COG1021 388 PYTIRGYYRAPEHNARAFTPDGF---------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 796556827 949 VSAT-VAVRDDgRGGKRLAAYAVPQidqdaATRPTPSEIRAWLANR-LPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:COG1021 458 HDAAvVAMPDE-YLGERSCAFVVPR-----GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKID 523
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
557-1022 |
1.02e-36 |
|
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: 144.91 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 557 DADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARL 636
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 637 VvshssidlpktanrlnldedfpddesadnletVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIR-ACDVTAD 715
Cdd:cd05919 86 V--------------------------------VTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAReALGLTPG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 716 DCVLQ----FFSFSFDASI--PELVMSLGAGArllllpryATLPGAELADILRARHvthltmTPSALLSLPV-------- 781
Cdd:cd05919 134 DRVFSsakmFFGYGLGNSLwfPLAVGASAVLN--------PGWPTAERVLATLARF------RPTVLYGVPTfyanllds 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 782 -----DDLLSLRTVLVGGEvPMPE-LIERWGKT--RRFINAYGPTETT---VNASMVDMGGGRAGLPVlrPAAnkQLYVL 850
Cdd:cd05919 200 cagspDALRSLRLCVSAGE-ALPRgLGERWMEHfgGPILDGIGATEVGhifLSNRPGAWRLGSTGRPV--PGY--EIRLV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 851 DDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFvpdpfatdgrAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRG 930
Cdd:cd05919 275 DEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF----------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 931 YRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAV---PQIDQDAATRptpsEIRAWLANRLPKFLVPDTFDWLE 1007
Cdd:cd05919 345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVlksPAAPQESLAR----DIHRHLLERLSAHKVPRRIAFVD 420
|
490
....*....|....*
gi 796556827 1008 ALPLTMNGKIDPLKL 1022
Cdd:cd05919 421 ELPRTATGKLQRFKL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
563-1017 |
1.90e-35 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 141.42 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVShss 642
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 idlpktanrlnldeDFPDDEsadnletvthssqlAYVIYTSGSTGKAKG------VLVDHSGLINLTRDKI-RACDV--- 712
Cdd:cd05971 85 --------------DGSDDP--------------ALIIYTSGTTGPPKGalhahrVLLGHLPGVQFPFNLFpRDGDLywt 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 713 TAD--------DCVLQFFSFSfdasIPELVMSLGAGArllllpryatlPGAELAdiLRARH-VTHLTMTPSALLSL---- 779
Cdd:cd05971 137 PADwawiggllDVLLPSLYFG----VPVLAHRMTKFD-----------PKAALD--LMSRYgVTTAFLPPTALKMMrqqg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 780 -PVDDL-LSLRTVLVGGEVPMPELIErWGKtRRF---IN-AYGPTETTV----NASMVDMGGGRAGlpvlRPAANKQLYV 849
Cdd:cd05971 200 eQLKHAqVKLRAIATGGESLGEELLG-WAR-EQFgveVNeFYGQTECNLvignCSALFPIKPGSMG----KPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 850 LDDNLELLPFGVPGELHIG-GCGIAR-GYHDRAALTAERFvpdpfatdgrAGVLYRTGDRAVLLADGRIHVSGRLDSQVK 927
Cdd:cd05971 274 VDDNGTPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKM----------AGDWLLTGDLGRKDSDGYFWYVGRDDDVIT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 928 IRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAV---PQIDQDAATRptpsEIRAWLANRLPKFLVPDTFD 1004
Cdd:cd05971 344 SSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpGETPSDALAR----EIQELVKTRLAAHEYPREIE 419
|
490
....*....|...
gi 796556827 1005 WLEALPLTMNGKI 1017
Cdd:cd05971 420 FVNELPRTATGKI 432
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
523-1022 |
2.47e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 143.27 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 523 STAQEHAGPQYFHELFEAHVARAPQAAALIMPQADADDI--MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMI 600
Cdd:PRK13295 15 SIAAGHWHDRTINDDLDACVASCPDKTAVTAVRLGTGAPrrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 601 VAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVV--------SHSSI------DLPKTANRLNLDEDFPDD----- 661
Cdd:PRK13295 95 VLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVvpktfrgfDHAAMarrlrpELPALRHVVVVGGDGADSfeall 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 662 -----ESADNLETVTHSSQ-----LAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVL------QFFSFS 725
Cdd:PRK13295 175 itpawEQEPDAPAILARLRpgpddVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILmaspmaHQTGFM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 726 FDASIPeLVMSLGAGARLLLLPryatlpgAELADILRARHVThLTMTPSALLS-------LPVDDLLSLRTVLVGGEVPM 798
Cdd:PRK13295 255 YGLMMP-VMLGATAVLQDIWDP-------ARAAELIRTEGVT-FTMASTPFLTdltravkESGRPVSSLRTFLCAGAPIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 799 PELIERwgKTRRF----INAYGPTE-----TTVNASMVDMGGGRAGLPVlrPAAnkQLYVLDDNLELLPFGVPGELHIGG 869
Cdd:PRK13295 326 GALVER--ARAALgakiVSAWGMTEngavtLTKLDDPDERASTTDGCPL--PGV--EVRVVDADGAPLPAGQIGRLQVRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 870 CGIARGYHDRAALTAErfvpdpfATDGragvLYRTGDRAVLLADGRIHVSGRlDSQVKIRG-YRIEPGEIEARLLAHPAI 948
Cdd:PRK13295 400 CSNFGGYLKRPQLNGT-------DADG----WFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAI 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 796556827 949 VSATVAVRDDGRGGKRLAAYAVPqidqdaatRP----TPSEIRAWL-ANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK13295 468 AQVAIVAYPDERLGERACAFVVP--------RPgqslDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
531-1018 |
1.67e-34 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 139.38 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 531 PQYFHELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGV-SAETVVaISLPRSFDMIVAWLAVWKA 609
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVV----DGDRRLTYRELDRRADRLAAGLRGLGIrPGDRVV-VQLPNVAEFVVLFFALLRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 610 GGAYLPLDPEYPAERIGAMLSDAGARLVVSHssidlpktanrlnlDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKA 689
Cdd:cd05920 89 GAVPVLALPSHRRSELSAFCAHAEAVAYIVP--------------DRHAGFDHRALARELAESIPEVALFLLSGGTTGTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 690 KGVLVDHSGLINLTRDKIRACDVTADD---CVLQFfSFSFDASIPELVMSLGAGARLLLLPRyatlPGAELADILRARH- 765
Cdd:cd05920 155 KLIPRTHNDYAYNVRASAEVCGLDQDTvylAVLPA-AHNFPLACPGVLGTLLAGGRVVLAPD----PSPDAAFPLIEREg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 766 VTHLTMTPsALLSLPVD-------DLLSLRTVLVGGEVPMPELIERWGKTR--RFINAYGPTETTVNASMVDMGGGRAGL 836
Cdd:cd05920 230 VTVTALVP-ALVSLWLDaaasrraDLSSLRLLQVGGARLSPALARRVPPVLgcTLQQVFGMAEGLLNYTRLDDPDEVIIH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 837 PVLRPA-ANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGR 915
Cdd:cd05920 309 TQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF---------YRTGDLVRRTPDGY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 916 IHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQidqdaATRPTPSEIRAWLANR-L 994
Cdd:cd05920 380 LVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-----DPPPSAAQLRRFLRERgL 454
|
490 500
....*....|....*....|....
gi 796556827 995 PKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd05920 455 AAYKLPDRIEFVDSLPLTAVGKID 478
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
563-1025 |
2.77e-34 |
|
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: 139.58 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGAR-LVVShs 641
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRgLIVI-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 sidlpktanrlnldedfpddESADnleTVTHSSQLAYVIYTSGSTGKAKGVLVDHSGL----------INLT-RDKIRAC 710
Cdd:cd17647 100 --------------------RAAG---VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLayyfpwmakrFNLSeNDKFTML 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 711 DVTADDCVLQ--FFSFSFDASIpeLVMSLGAGARllllpryatlPGaELADILrARH---VTHLTMTPSALLS------L 779
Cdd:cd17647 157 SGIAHDPIQRdmFTPLFLGAQL--LVPTQDDIGT----------PG-RLAEWM-AKYgatVTHLTPAMGQLLTaqattpF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 780 P-------VDDLLSLRTVLvggevpmpeLIERWGKTRRFINAYGPTETTVNASMVDMGGGRAG----------LPVLRPA 842
Cdd:cd17647 223 PklhhaffVGDILTKRDCL---------RLQTLAENVRIVNMYGTTETQRAVSYFEVPSRSSDptflknlkdvMPAGRGM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 843 ANKQLYVLD--DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRAGV-------------------L 901
Cdd:cd17647 294 LNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHWNYldkdnnepwrqfwlgprdrL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 902 YRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAAT-- 979
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDEsf 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 980 ---------------------RPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPAP 1025
Cdd:cd17647 454 aqedvpkevstdpivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
537-1018 |
4.86e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 136.17 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 537 LFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL 616
Cdd:PRK07798 8 LFEAVADAVPDRVALV----CGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 617 DPEYPAERIGAMLSDAGARLVVSHSSIDlPKTANRLnldEDFP--------DDESADNLET--VTHSSQLA--------- 677
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALVYEREFA-PRVAEVL---PRLPklrtlvvvEDGSGNDLLPgaVDYEDALAagsperdfg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 678 -------YVIYTSGSTGKAKGVLVDHSglinltrDKIRACDVTADdcvlqFFSFSFDASIPELVMSLGAGARLLLLP--- 747
Cdd:PRK07798 160 erspddlYLLYTGGTTGMPKGVMWRQE-------DIFRVLLGGRD-----FATGEPIEDEEELAKRAAAGPGMRRFPapp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 748 ------------------RYATLPGAEL--ADILR--ARH-VTHLTMTPSALLSLPVD--------DLLSLRTVLVGGEV 796
Cdd:PRK07798 228 lmhgagqwaafaalfsgqTVVLLPDVRFdaDEVWRtiEREkVNVITIVGDAMARPLLDaleargpyDLSSLFAIASGGAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 797 PMPELIERWGK---TRRFINAYGPTETTVNAS-MVDMGGGRAGLPVLRPAANKQlyVLDDNLELLPfgvPGElhiGGCG- 871
Cdd:PRK07798 308 FSPSVKEALLEllpNVVLTDSIGSSETGFGGSgTVAKGAVHTGGPRFTIGPRTV--VLDEDGNPVE---PGS---GEIGw 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 872 IAR------GYHDRAALTAERFvpdpFATDGRAGVLyrTGDRAVLLADGRIHVSGRlDSQVkIR--GYRIEPGEIEARLL 943
Cdd:PRK07798 380 IARrghiplGYYKDPEKTAETF----PTIDGVRYAI--PGDRARVEADGTITLLGR-GSVC-INtgGEKVFPEEVEEALK 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 796556827 944 AHPAIVSATVAVRDDGRGGKRLAayAVPQIDQDAatRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:PRK07798 452 AHPDVADALVVGVPDERWGQEVV--AVVQLREGA--RPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
563-1022 |
3.32e-32 |
|
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: 133.14 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLV----- 637
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVfvdrd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 638 -------------------VSHSSIDLPKTANRLNLD-EDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHS 697
Cdd:cd12119 107 flplleaiaprlptvehvvVMTDDAAMPEPAGVGVLAyEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 698 GLI-----NLTRDkirACDVTADDCVL---QFF-----SFSFDASI--PELVMSLgagarllllpRYatLPGAELADILR 762
Cdd:cd12119 187 SLVlhamaALLTD---GLGLSESDVVLpvvPMFhvnawGLPYAAAMvgAKLVLPG----------PY--LDPASLAELIE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 763 ARHVTHLTMTPSALLSL------PVDDLLSLRTVLVGGEVPMPELIERW-GKTRRFINAYGPTETTVNASMVDMGGGRAG 835
Cdd:cd12119 252 REGVTFAAGVPTVWQGLldhleaNGRDLSSLRRVVIGGSAVPRSLIEAFeERGVRVIHAWGMTETSPLGTVARPPSEHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 836 LPVL----------RPAANKQLYVLDDNLELLPF--GVPGELHIGGCGIARGYHDRAALTAERFVpdpfatDGragvLYR 903
Cdd:cd12119 332 LSEDeqlalrakqgRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTE------DG----WLR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 904 TGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDaatrPTP 983
Cdd:cd12119 402 TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAT----VTA 477
|
490 500 510
....*....|....*....|....*....|....*....
gi 796556827 984 SEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
530-1015 |
3.32e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 133.72 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 530 GPQYFHELFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKA 609
Cdd:PRK06164 8 RADTLASLLDAHARARPDAVALI----DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 610 GGAYLPLDPEYPAERIGAMLSDAGARLVV---SHSSIDLPKTANRLNLDE---------------DFPDD---------- 661
Cdd:PRK06164 84 GATVIAVNTRYRSHEVAHILGRGRARWLVvwpGFKGIDFAAILAAVPPDAlpplraiavvddaadATPAPapgarvqlfa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 662 -----ESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMS 736
Cdd:PRK06164 164 lpdpaPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 737 LGAGARLLLLPRYatlPGAELADILRARHVTHlTMTPSALLSLPVD------DLLSLRTVLVGGEVP-MPELIErWGKTR 809
Cdd:PRK06164 244 LAGGAPLVCEPVF---DAARTARALRRHRVTH-TFGNDEMLRRILDtageraDFPSARLFGFASFAPaLGELAA-LARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 810 RFINA--YGPTETTVNASMVDM---------GGGRaglpVLRPAAnkQLYVLD-DNLELLPFGVPGELHIGGCGIARGYH 877
Cdd:PRK06164 319 GVPLTglYGSSEVQALVALQPAtdpvsvrieGGGR----PASPEA--RVRARDpQDGALLPDGESGEIEIRAPSLMRGYL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 878 DRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVaVRD 957
Cdd:PRK06164 393 DNPDATARALTDDGY---------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQV-VGA 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 958 DGRGGKRLAAYAVPQidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNG 1015
Cdd:PRK06164 463 TRDGKTVPVAFVIPT----DGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
1145-1416 |
1.20e-31 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 126.25 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1145 HVFLTGATGFLGTYLLHELLRDPERkVTCLVRGDDGMSRLRQAfrqydlpqsvltERVTIVTGELSKPGlGLAAAdydni 1224
Cdd:COG0451 1 RILVTGGAGFIGSHLARRLLARGHE-VVGLDRSPPGAANLAAL------------PGVEFVRGDLRDPE-ALAAA----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1225 VRNADCIFHNGAEVHH-LHRYERLRETNVLGIREILQLACAGEGRHVHYISTLSALtprrgsGGDPRPVCELESVEgfvp 1303
Cdd:COG0451 62 LAGVDAVVHLAAPAGVgEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVY------GDGEGPIDEDTPLR---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1304 PAGGYNRSKWVAEHLVNEAGRR-GLPVTIYRPGAISGDSVTGAFNgsdilcRLVQAYLYTGTAP---EGERLLDMLPVDH 1379
Cdd:COG0451 132 PVSPYGASKLAAELLARAYARRyGLPVTILRPGNVYGPGDRGVLP------RLIRRALAGEPVPvfgDGDQRRDFIHVDD 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 796556827 1380 VARAIVHLSGKPASAGQVFHLIHSSPVSSARLFEACE 1416
Cdd:COG0451 206 VARAIVLALEAPAAPGGVYNVGGGEPVTLRELAEAIA 242
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
1144-1417 |
2.50e-31 |
|
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187547 [Multi-domain] Cd Length: 320 Bit Score: 126.26 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1144 DHVFLTGATGFLGTYLLHELLRD-PE-RKVTCLVRGDDGMS---RLRQ-----AFRQYDLPQSVLTERVTIVTGELSKPG 1213
Cdd:cd05236 1 KSVLITGATGFLGKVLLEKLLRScPDiGKIYLLIRGKSGQSaeeRLREllkdkLFDRGRNLNPLFESKIVPIEGDLSEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1214 LGLAAADYDNIVRNADCIFHNGAEVHHLHRYERLRETNVLGIREILQLA--CAGEGRHVHyISTLSALTPRRG------- 1284
Cdd:cd05236 81 LGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAkrCKKLKAFVH-VSTAYVNGDRQLieekvyp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1285 SGGDPRPVCELES------VEGFVPPAGG-----YNRSKWVAEHLVNEAgRRGLPVTIYRPGAISG----------DSVT 1343
Cdd:cd05236 160 PPADPEKLIDILElmddleLERATPKLLGghpntYTFTKALAERLVLKE-RGNLPLVIVRPSIVGAtlkepfpgwiDNFN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1344 GAFN-----GSDILCRLVQaylytgtapEGERLLDMLPVDHVARAIV-----HLSGKPAsAGQVFHlIHSSPVSSARLFE 1413
Cdd:cd05236 239 GPDGlflayGKGILRTMNA---------DPNAVADIIPVDVVANALLaaaaySGVRKPR-ELEVYH-CGSSDVNPFTWGE 307
|
....
gi 796556827 1414 ACEL 1417
Cdd:cd05236 308 AEEL 311
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
563-1017 |
7.88e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 128.39 E-value: 7.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVShss 642
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 iDLPKTANRLNlDEDFPD-DESADNLETVTHSS----QLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDC 717
Cdd:PRK09088 101 -DDAVAAGRTD-VEDLAAfIASADALEPADTPSippeRVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 718 VL----QFFSFSFDASI-PELVMSLGAGARLLLLPRyATLpgAELADIlrARHVTHLTMTP---SALLSLPVDDLLSLR- 788
Cdd:PRK09088 179 FLcdapMFHIIGLITSVrPVLAVGGSILVSNGFEPK-RTL--GRLGDP--ALGITHYFCVPqmaQAFRAQPGFDAAALRh 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 789 -TVLVGGEVPMPELIERW--GKTRRFINAYGPTET------TVNASMVDMGGGRAGLPvlrpAANKQLYVLDDNLELLPF 859
Cdd:PRK09088 254 lTALFTGGAPHAAEDILGwlDDGIPMVDGFGMSEAgtvfgmSVDCDVIRAKAGAAGIP----TPTVQTRVVDDQGNDCPA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 860 GVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIE 939
Cdd:PRK09088 330 GVPGELLLRGPNLSPGYWRRPQATARAFTGDGW---------FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 940 ARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK09088 401 AVLADHPGIRECAVVGMADAQWGEVGYLAIVPA----DGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
681-1022 |
2.45e-30 |
|
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: 123.93 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 681 YTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADD---CVLQFFSfSFDASIPELVMSLGAGARLLLLPRYAtlPGAEL 757
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDrlcIPVPLFH-CFGSVLGVLACLTHGATMVFPSPSFD--PLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 758 ADILRARhVTHLTMTPS---ALLSLPVD---DLLSLRT-VLVGGEVP---MPELIERWGKTRRFInAYGPTETT--VNAS 825
Cdd:cd05917 86 EAIEKEK-CTALHGVPTmfiAELEHPDFdkfDLSSLRTgIMAGAPCPpelMKRVIEVMNMKDVTI-AYGMTETSpvSTQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 826 MVDMGGGRAGLPVLRPAANKQLYVLD-DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRT 904
Cdd:cd05917 164 RTDDSIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGW---------LHT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 905 GDRAVLLADGRIHVSGRLDSQVkIRG-YRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQdaatRPTP 983
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGA----ELTE 309
|
330 340 350
....*....|....*....|....*....|....*....
gi 796556827 984 SEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:cd05917 310 EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
563-1022 |
5.67e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 126.79 E-value: 5.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLV----- 637
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFfaptl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 638 ---VSHSSI------DLPKTANRLNLDEDFPDDeSADNLETV------------THSSQLAYVIYTSGSTGKAKGVLVDH 696
Cdd:PRK06087 131 fkqTRPVDLilplqnQLPQLQQIVGVDKLAPAT-SSLSLSQIiadyeplttaitTHGDELAAVLFTSGTEGLPKGVMLTH 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 697 SGLINLTRDKIRACDVTADDCVL------QFFSFSFDASIPELVMSLGAGARLLLlpryatlPGAELADILRARHVTHLT 770
Cdd:PRK06087 210 NNILASERAYCARLNLTWQDVFMmpaplgHATGFLHGVTAPFLIGARSVLLDIFT-------PDACLALLEQQRCTCMLG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 771 MTP------SALLSLPVdDLLSLRTVLVGGeVPMPELIER--WGKTRRFINAYGPTETTVNAsMVDMG------GGRAGl 836
Cdd:PRK06087 283 ATPfiydllNLLEKQPA-DLSALRFFLCGG-TTIPKKVARecQQRGIKLLSVYGSTESSPHA-VVNLDdplsrfMHTDG- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 837 pvlRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAeRFVPDpfatDGragvLYRTGDRAVLLADGRI 916
Cdd:PRK06087 359 ---YAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RALDE----EG----WYYSGDLCRMDEAGYI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 917 HVSGRlDSQVKIR-GYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidQDAATRPTPSEIRAWLA-NRL 994
Cdd:PRK06087 427 KITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVL---KAPHHSLTLEEVVAFFSrKRV 502
|
490 500
....*....|....*....|....*...
gi 796556827 995 PKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK06087 503 AKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
526-1017 |
9.33e-30 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 126.24 E-value: 9.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 526 QEHAGPQYFHELFEAHVARAPqAAALIMPQAD-ADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWL 604
Cdd:cd05906 4 RPEGAPRTLLELLLRAAERGP-TKGITYIDADgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 605 AVWKAGGAYLPLDP----EYPAERIG------AMLSDAgarLVVSHSSI-----DLPKTANRLNLDEDFPDDESADNLET 669
Cdd:cd05906 83 ACVLAGFVPAPLTVpptyDEPNARLRklrhiwQLLGSP---VVLTDAELvaefaGLETLSGLPGIRVLSIEELLDTAADH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 670 VTHSSQ---LAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPEL-VMSLGAGARLLL 745
Cdd:cd05906 160 DLPQSRpddLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 746 LPryatlPGAELADILR-----ARHVTHLTMTPSALLSLPVD----------DLLSLRTVLVGGE-------VPMPELIE 803
Cdd:cd05906 240 VP-----TEEILADPLRwldliDRYRVTITWAPNFAFALLNDlleeiedgtwDLSSLRYLVNAGEavvaktiRRLLRLLE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 804 RWG-KTRRFINAYGPTETT--VNASMVDMGGGRAGLPVL----RPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGY 876
Cdd:cd05906 315 PYGlPPDAIRPAFGMTETCsgVIYSRSFPTYDHSQALEFvslgRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 877 HDRAALTAERFVPDPFatdgragvlYRTGDRAvLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVS---ATV 953
Cdd:cd05906 395 YNNPEANAEAFTEDGW---------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAF 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 954 AVRDDGRGGKRLAAYAVPQIDQDAATRPTPSEIRAWLANRL---PKFLVPDTfdwLEALPLTMNGKI 1017
Cdd:cd05906 465 AVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVgvsPAYLIPLP---KEEIPKTSLGKI 528
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
531-1028 |
1.68e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 125.54 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 531 PQYFH------ELFEAHVARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWL 604
Cdd:PRK06178 26 PEYPHgerpltEYLRAWARERPQRPAIIF----YGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 605 AVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVS-------------------------------HSSIDLPK--TANR 651
Cdd:PRK06178 102 GILKLGAVHVPVSPLFREHELSYELNDAGAEVLLAldqlapvveqvraetslrhvivtsladvlpaEPTLPLPDslRAPR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 652 LnLDEDFPDDESAdnLETVTHSSQ--------LAYVIYTSGSTGKAKGVLVDHsglinltRDKI----RACDVT----AD 715
Cdd:PRK06178 182 L-AAAGAIDLLPA--LRACTAPVPlpppaldaLAALNYTGGTTGMPKGCEHTQ-------RDMVytaaAAYAVAvvggED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 716 DCVLQFFsfsfdasiPELVMSLGAGARLLLLPRYATL-------PGAELADILRARhVTHLTMT-PSA--LLSLP---VD 782
Cdd:PRK06178 252 SVFLSFL--------PEFWIAGENFGLLFPLFSGATLvllarwdAVAFMAAVERYR-VTRTVMLvDNAveLMDHPrfaEY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 783 DLLSLRTVLVGGEVPM--PELIERW----GKTRRFInAYGPTET-TVNASMVDMGGGR---------AGLPVlrPAAnkQ 846
Cdd:PRK06178 323 DLSSLRQVRVVSFVKKlnPDYRQRWraltGSVLAEA-AWGMTEThTCDTFTAGFQDDDfdllsqpvfVGLPV--PGT--E 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 847 LYVLD-DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVpdpfatDGragvLYRTGDRAVLLADGRIHVSGRLDSQ 925
Cdd:PRK06178 398 FKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR------DG----WLHTGDIGKIDEQGFLHYLGRRKEM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 926 VKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAatrpTPSEIRAWLANRLPKFLVPdTFDW 1005
Cdd:PRK06178 468 LKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADL----TAAALQAWCRENMAVYKVP-EIRI 542
|
570 580
....*....|....*....|...
gi 796556827 1006 LEALPLTMNGKIDPLKLpAPRAE 1028
Cdd:PRK06178 543 VDALPMTATGKVRKQDL-QALAE 564
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
549-1017 |
2.62e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 124.25 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 549 AALIMpqADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAM 628
Cdd:PRK08276 1 PAVIM--APSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 629 LSDAGARLVVSHSSID---------LPKTANRLNLD----------EDFPDDESADNLETVTHSSQLAYviyTSGSTGKA 689
Cdd:PRK08276 79 VDDSGAKVLIVSAALAdtaaelaaeLPAGVPLLLVVagpvpgfrsyEEALAAQPDTPIADETAGADMLY---SSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 690 KGVL-------VDHSGLINLTRDKIRACdvTADDCV------------LQFFSFSFDASIPELVMslgagarllllPRYA 750
Cdd:PRK08276 156 KGIKrplpgldPDEAPGMMLALLGFGMY--GGPDSVylspaplyhtapLRFGMSALALGGTVVVM-----------EKFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 751 tlPGAELADILRARhVTHLTMTPSA---LLSLPVD-----DLLSLRTVLVGGeVPMPE-----LIERWGKTrrFINAYGP 817
Cdd:PRK08276 223 --AEEALALIERYR-VTHSQLVPTMfvrMLKLPEEvraryDVSSLRVAIHAA-APCPVevkraMIDWWGPI--IHEYYAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 818 TE----TTVNASMVDMGGGRAGLPVLrpaanKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFA 893
Cdd:PRK08276 297 SEgggvTVITSEDWLAHPGSVGKAVL-----GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 894 TdgragvlyrTGDRAVLLADGRIHVSGRlDSQVKIRG-YRIEPGEIEARLLAHPAIVSATV-AVRDDGRGGKRLAAyaVP 971
Cdd:PRK08276 372 T---------VGDVGYLDEDGYLYLTDR-KSDMIISGgVNIYPQEIENLLVTHPKVADVAVfGVPDEEMGERVKAV--VQ 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 796556827 972 QIDQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK08276 440 PADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
541-1017 |
2.76e-29 |
|
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: 124.66 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALIMPQADADDI--MTYGELNARANRLARLLRRKGVSAETVVAIsLPRSFDMIVAWLAVWKAGG----AYL 614
Cdd:cd05931 2 RAAARPDRPAYTFLDDEGGREetLTYAELDRRARAIAARLQAVGKPGDRVLLL-APPGLDFVAAFLGCLYAGAiavpLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 615 PLDPEYpAERIGAMLSDAGARLVVSHSSI--DLPKTANRLNLDEDF--------PDDESADNLETVTHSSQLAYVIYTSG 684
Cdd:cd05931 81 PTPGRH-AERLAAILADAGPRVVLTTAAAlaAVRAFAASRPAAGTPrllvvdllPDTSAADWPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 685 STGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFD------------ASIPELVMSlgagarllllpryatl 752
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmgligglltplySGGPSVLMS---------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 753 PGAELADILR-----ARHVTHLT-------------MTPSALLSLpvdDLLSLRTVLVGGEVPMPELIERWGKT------ 808
Cdd:cd05931 224 PAAFLRRPLRwlrliSRYRATISaapnfaydlcvrrVRDEDLEGL---DLSSWRVALNGAEPVRPATLRRFAEAfapfgf 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 809 RR--FINAYGPTETTVNASMVDMG----------------------GGRAGLPVL---RPAANKQLYVLDDN-LELLPFG 860
Cdd:cd05931 301 RPeaFRPSYGLAEATLFVSGGPPGtgpvvlrvdrdalagravavaaDDPAARELVscgRPLPDQEVRIVDPEtGRELPDG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 861 VPGELHIGGCGIARGYHDRAALTAERFVPDpfaTDGRAGVLYRTGDRAVlLADGRIHVSGRLDSQVKIRGYRIEPGEIEA 940
Cdd:cd05931 381 EVGEIWVRGPSVASGYWGRPEATAETFGAL---AATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 941 RL-LAHPAIVSATVAV--RDDGRGGKRLAAYAVPQIDQDAATRPTPSEIRAWLANRlpkF-LVPDTFDWLE--ALPLTMN 1014
Cdd:cd05931 457 TAeEAHPALRPGCVAAfsVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVARE---HgVAPADVVLVRpgSIPRTSS 533
|
...
gi 796556827 1015 GKI 1017
Cdd:cd05931 534 GKI 536
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
537-1024 |
7.28e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 123.50 E-value: 7.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 537 LFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL 616
Cdd:PRK07788 54 LVAHAARRAPDRAALI----DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 617 DPEYPAERIGAMLSDAGARLVV---------SHSSIDLPK-TANRLNLDEDFPDDESADNLETV--THSSQLA------- 677
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVyddeftdllSALPPDLGRlRAWGGNPDDDEPSGSTDETLDDLiaGSSTAPLpkppkpg 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 678 -YVIYTSGSTGKAKGVLVDH-SGLIN----LTRDKIRACDVTADDCVLqFFSFSFDASIPELVMSlgagarllllpryAT 751
Cdd:PRK07788 210 gIVILTSGTTGTPKGAPRPEpSPLAPlaglLSRVPFRAGETTLLPAPM-FHATGWAHLTLAMALG-------------ST 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 752 L-------PGAELADIlrARH-VTHLTMTP---SALLSLPVD-----DLLSLRTVLVGGEVPMPELIERwgKTRRF---- 811
Cdd:PRK07788 276 VvlrrrfdPEATLEDI--AKHkATALVVVPvmlSRILDLGPEvlakyDTSSLKIIFVSGSALSPELATR--ALEAFgpvl 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 812 INAYGPTETTVN--ASMVDMGggRAGLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDraaltaerfVP 889
Cdd:PRK07788 352 YNLYGSTEVAFAtiATPEDLA--EAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD---------GR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 890 DPFATDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYA 969
Cdd:PRK07788 421 DKQIIDG----LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 796556827 970 VPQidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPA 1024
Cdd:PRK07788 497 VKA----PGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
1147-1407 |
9.01e-29 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 124.29 E-value: 9.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1147 FLTGATGFLGTYLLHELL-RDPERKVTCLVRgDDGMSRLRQAFRQYDlpqsvlTERVTIVTGELSKPGLGLAAADYDNIV 1225
Cdd:PRK07201 4 FVTGGTGFIGRRLVSRLLdRRREATVHVLVR-RQSLSRLEALAAYWG------ADRVVPLVGDLTEPGLGLSEADIAELG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 rNADCIFHNGAeVHHLH-RYERLRETNVLGIREILQLACAGEGRHVHYISTLSAltprrgsGGDPRPVC---ELESVEGF 1301
Cdd:PRK07201 77 -DIDHVVHLAA-IYDLTaDEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAV-------AGDYEGVFredDFDEGQGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1302 VPPaggYNRSKWVAEHLVNEAGrrGLPVTIYRPGAISGDSVTGAFNGSD-------ILCRLVQAYLYTGTA-PEGERlLD 1373
Cdd:PRK07201 148 PTP---YHRTKFEAEKLVREEC--GLPWRVYRPAVVVGDSRTGEMDKIDgpyyffkVLAKLAKLPSWLPMVgPDGGR-TN 221
|
250 260 270
....*....|....*....|....*....|....
gi 796556827 1374 MLPVDHVARAIVHLSGKPASAGQVFHLIHSSPVS 1407
Cdd:PRK07201 222 IVPVDYVADALDHLMHKDGRDGQTFHLTDPKPQR 255
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
675-1018 |
9.64e-29 |
|
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: 118.59 E-value: 9.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 675 QLAYVIYTSGSTGKAKGVLVDHSGLinltrdkiracdVTADDCVLQFfsFSFDASIPELV----------MSLGAGARLL 744
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANL------------LASAAGLHSR--LGFGGGDSWLLslplyhvgglAILVRSLLAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 745 LLPRYATLPGAELADILRARhVTHLTMTPSALLSL-----PVDDLLSLRTVLVGGEVPMPELIERwGKTRRF--INAYGP 817
Cdd:cd17630 67 AELVLLERNQALAEDLAPPG-VTHVSLVPTQLQRLldsgqGPAALKSLRAVLLGGAPIPPELLER-AADRGIplYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 818 TET--TVNASMVDmGGGRAGLPVLRPAAnkQLYVLDDnlellpfgvpGELHIGGCGIARGYHDRAaltaerfVPDPFATD 895
Cdd:cd17630 145 TETasQVATKRPD-GFGRGGVGVLLPGR--ELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEFNED 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 896 GragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidq 975
Cdd:cd17630 205 G----WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG---- 276
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 796556827 976 daATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd17630 277 --RGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVD 317
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
535-1017 |
1.56e-28 |
|
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: 122.98 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVARAPQAAALI-MPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAY 613
Cdd:cd05968 64 EQLLDKWLADTRTRPALRwEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 614 LPLDPEYPAERIGAMLSDAGARL----------------------------------VVSHSSIDLPKTanrlNLDEDFP 659
Cdd:cd05968 144 VPIFSGFGKEAAATRLQDAEAKAlitadgftrrgrevnlkeeadkacaqcptvekvvVVRHLGNDFTPA----KGRDLSY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 660 DD--ESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGL-INLTRDKIRACDVTADDCVLQFFSFSFDASiPELVM- 735
Cdd:cd05968 220 DEekETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFg 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 736 SLGAGARLLLLPRYATLPGAE-LADILRARHVTHLTMTPSALLSL------PVD--DLLSLRTVLVGGEVPMPE----LI 802
Cdd:cd05968 299 GLILGATMVLYDGAPDHPKADrLWRMVEDHEITHLGLSPTLIRALkprgdaPVNahDLSSLRVLGSTGEPWNPEpwnwLF 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 803 ERWGKTRR-FINAYGPTEttvnasmvdMGGGRAGLPVLRPAA---------NKQLYVLDDNLELLPFGVpGELHIGG--C 870
Cdd:cd05968 379 ETVGKGRNpIINYSGGTE---------ISGGILGNVLIKPIKpssfngpvpGMKADVLDESGKPARPEV-GELVLLApwP 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 871 GIARGY---HDRAALTAERFVPDpfatdgragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPA 947
Cdd:cd05968 449 GMTRGFwrdEDRYLETYWSRFDN----------VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPA 518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 796556827 948 IV-SATVAVRDDGRGGKrLAAYAV--PQIDQDAATRptpSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05968 519 VLeSAAIGVPHPVKGEA-IVCFVVlkPGVTPTEALA---EELMERVADELGKPLSPERILFVKDLPKTRNAKV 587
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
563-1017 |
5.78e-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: 119.14 E-value: 5.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSS 642
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 IdlpktanrlnLDEDFPDDesadnletvthssqLAYVIYTSGSTGKAKGVLVDHSGLI----------NLTRDKIRACdv 712
Cdd:cd05969 82 L----------YERTDPED--------------PTLLHYTSGTTGTPKGVLHVHDAMIfyyftgkyvlDLHPDDIYWC-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 713 TADDCVLQFFSFSFDAsiPELVMSLGAGARLLLLPR--YAtlpgaeladILRARHVTHLTMTPSALLSL------PVD-- 782
Cdd:cd05969 136 TADPGWVTGTVYGIWA--PWLNGVTNVVYEGRFDAEswYG---------IIERVKVTVWYTAPTAIRMLmkegdeLARky 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 783 DLLSLRTVLVGGEVPMPELIeRWGKTR---RFINAYGPTET----TVNASMVDMGGGRAGlpvlRPAANKQLYVLDDNLE 855
Cdd:cd05969 205 DLSSLRFIHSVGEPLNPEAI-RWGMEVfgvPIHDTWWQTETgsimIANYPCMPIKPGSMG----KPLPGVKAAVVDENGN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 856 LLPFGVPGELHI--GGCGIARGYHDRAALTAERFVpdpfatDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRI 933
Cdd:cd05969 280 ELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI------DG----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 934 EPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDaATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTM 1013
Cdd:cd05969 350 GPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE-PSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
....
gi 796556827 1014 NGKI 1017
Cdd:cd05969 429 SGKI 432
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
534-1017 |
2.02e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 118.91 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 534 FHELfEAHVARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRK-GVSAETVVAISLPRSFDMIVAWLAVWKAGGA 612
Cdd:PRK08314 13 FHNL-EVSARRYPDKTAIVF----YGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 613 YLPLDPEYPAERIGAMLSDAGARLVVSHSSIdLPKTA---NRLNLDE-------DFPDDESADNLE---TVTHSSQ---- 675
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSEL-APKVApavGNLRLRHvivaqysDYLPAEPEIAVPawlRAEPPLQalap 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 676 -------------------------LAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSF------ 724
Cdd:PRK08314 167 ggvvawkealaaglappphtagpddLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLfhvtgm 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 725 --SFDASI---PELVMslgagarlllLPRYatlpGAELADILRARH-VTHLTMTPSA---LLSLP-VD--DLLSLRtVLV 792
Cdd:PRK08314 247 vhSMNAPIyagATVVL----------MPRW----DREAAARLIERYrVTHWTNIPTMvvdFLASPgLAerDLSSLR-YIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 793 GGEVPMPE-----LIERWGktRRFINAYGPTETTVNASMVDMGGGR---AGLPVLRPAANkqlyVLD-DNLELLPFGVPG 863
Cdd:PRK08314 312 GGGAAMPEavaerLKELTG--LDYVEGYGLTETMAQTHSNPPDRPKlqcLGIPTFGVDAR----VIDpETLEELPPGEVG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 864 ELHIGGCGIARGYHDRAALTAERFVpdpfATDGRAgvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLL 943
Cdd:PRK08314 386 EIVVHGPQVFKGYWNRPEATAEAFI----EIDGKR--FFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLY 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 796556827 944 AHPAIVSATV-AVRDDGRgGKRLAAYAVPqiDQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK08314 460 KHPAIQEACViATPDPRR-GETVKAVVVL--RPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
541-1017 |
2.62e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 118.06 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEY 620
Cdd:PRK06145 11 HARRTPDRAALVY----RDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 621 PAERIGAMLSDAGARLVVSHSSIDLPKT--ANRLNLDEDFPDDES---ADNLET----VTHSSQLAYVIYTSGSTGKAKG 691
Cdd:PRK06145 87 AADEVAYILGDAGAKLLLVDEEFDAIVAleTPKIVIDAAAQADSRrlaQGGLEIppqaAVAPTDLVRLMYTSGTTDRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 692 VLVDHSGLINLTRDKIRACDVTADDCVlqffsfsfdasipeLVMSLGAGARLLLLPRYATL-------------PGAELA 758
Cdd:PRK06145 167 VMHSYGNLHWKSIDHVIALGLTASERL--------------LVVGPLYHVGAFDLPGIAVLwvggtlrihrefdPEAVLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 759 DILRARhVTHLTMTP---SALLSLPVD---DLLSLRTVLVGGEvPMPEL----IERWGKTRRFINAYGPTETTVNASMVD 828
Cdd:PRK06145 233 AIERHR-LTCAWMAPvmlSRVLTVPDRdrfDLDSLAWCIGGGE-KTPESrirdFTRVFTRARYIDAYGLTETCSGDTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 829 MGG-----GRAGlpvlRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlyR 903
Cdd:PRK06145 311 AGReiekiGSTG----RALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF----------R 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 904 TGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVpqidQDAATRPTP 983
Cdd:PRK06145 377 SGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV----LNPGATLTL 452
|
490 500 510
....*....|....*....|....*....|....
gi 796556827 984 SEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK06145 453 EALDRHCRQRLASFKVPRQLKVRDELPRNPSGKV 486
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
563-1017 |
7.10e-27 |
|
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: 115.14 E-value: 7.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLvvshss 642
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 idlpktanrlnldedfpddesadnletvthsSQLAYVIYTSGSTGKAKGVLV---DH-----SGLINLtrdkiracDVTA 714
Cdd:cd05912 77 -------------------------------DDIATIMYTSGTTGKPKGVQQtfgNHwwsaiGSALNL--------GLTE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 715 DD---CVLQFFSFSfDASIpeLVMSLGAGARLLLLPRYATlpgAELADILRARHVTHLTMTPSALLSLpVDDLL-----S 786
Cdd:cd05912 118 DDnwlCALPLFHIS-GLSI--LMRSVIYGMTVYLVDKFDA---EQVLHLINSGKVTIISVVPTMLQRL-LEILGegypnN 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 787 LRTVLVGGEVPMPELIERwGKTRRF--INAYGPTET-----TVNASMVDMGGGRAGlpvlRPAANKQLYVLDDNLEllPF 859
Cdd:cd05912 191 LRCILLGGGPAPKPLLEQ-CKEKGIpvYQSYGMTETcsqivTLSPEDALNKIGSAG----KPLFPVELKIEDDGQP--PY 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 860 GVpGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlyRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIE 939
Cdd:cd05912 264 EV-GEILLKGPNVTKGYLNRPDATEESFENGWF----------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 332
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 940 ARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAAtrptpsEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05912 333 EVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEE------ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKL 404
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
532-1017 |
1.69e-26 |
|
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: 115.30 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 532 QYFHELFEAHVARAPQAAALIMPQADADdiMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGG 611
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGLR--LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 612 AYLPLDPEYPAERIGAMLSDAGARLVVsHSSIDLPKTANRL-NLDEDFPDDESADNLETVTHSS---------QLAYVIY 681
Cdd:cd05923 79 VPALINPRLKAAELAELIERGEMTAAV-IAVDAQVMDAIFQsGVRVLALSDLVGLGEPESAGPLiedpprepeQPAFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 682 TSGSTGKAKGVLVDH-------------SGLinLTRDKIRACDVTADDCVLQFFSFsfdasipeLVMSLGAGARLLLlPR 748
Cdd:cd05923 158 TSGTTGLPKGAVIPQraaesrvlfmstqAGL--RHGRHNVVLGLMPLYHVIGFFAV--------LVAALALDGTYVV-VE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 749 YATlPGAELADILRARhVTHLTMTPSALLSLPV------DDLLSLRTVLVGGeVPMPE-LIERWG--KTRRFINAYGPTE 819
Cdd:cd05923 227 EFD-PADALKLIEQER-VTSLFATPTHLDALAAaaefagLKLSSLRHVTFAG-ATMPDaVLERVNqhLPGEKVNIYGTTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 820 TTVNASMVDMGGGRAglpvLRPAANKQLY---VLDDNLELLPFGVPGELHIGGCGIA--RGYHDRAALTAERFVpdpfat 894
Cdd:cd05923 304 AMNSLYMRDARTGTE----MRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 895 DGRagvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQid 974
Cdd:cd05923 374 DGW----YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPR-- 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 796556827 975 qdaATRPTPSEIRAW-LANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05923 448 ---EGTLSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKV 488
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
544-1115 |
3.77e-26 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 116.28 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 544 RAPQAAALIMPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAE 623
Cdd:PRK06060 13 QASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 624 RIGAMLSDAGARLVVSHSSI-DLPKTANRLNLDEDFPDDESAD--NLETVTHSSQlAYVIYTSGSTGKAKGVLVDHSGLI 700
Cdd:PRK06060 93 DHALAARNTEPALVVTSDALrDRFQPSRVAEAAELMSEAARVApgGYEPMGGDAL-AYATYTSGTTGPPKAAIHRHADPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 701 NLTRDKIR-ACDVTADDCVL----QFFSFSFDASI--PELVMSLGAGarllllpryATLP-GAELADILRARhvthltMT 772
Cdd:PRK06060 172 TFVDAMCRkALRLTPEDTGLcsarMYFAYGLGNSVwfPLATGGSAVI---------NSAPvTPEAAAILSAR------FG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 773 PSALLSLP-----------VDDLLSLRTVLVGGEVPMPELIERWgkTRRF-----INAYGPTE---TTVNASMVDMGGGR 833
Cdd:PRK06060 237 PSVLYGVPnffarvidscsPDSFRSLRCVVSAGEALELGLAERL--MEFFggipiLDGIGSTEvgqTFVSNRVDEWRLGT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 834 AGlPVLRPAankQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRaaltaerfvPDPFATDGraGVLyRTGDRAVLLAD 913
Cdd:PRK06060 315 LG-RVLPPY---EIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANE--GWL-DTRDRVCIDSD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 914 GRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQ----IDQDAAtrptpSEIRAW 989
Cdd:PRK06060 379 GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATsgatIDGSVM-----RDLHRG 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 990 LANRLPKFLVPDTFDWLEALPLTMNGKI--------DPLKLPAPRAETDPDGRAPeGEMEGRIAGAfghvlnidqvaatd 1061
Cdd:PRK06060 454 LLNRLSAFKVPHRFAVVDRLPRTPNGKLvrgalrkqSPTKPIWELSLTEPGSGVR-AQRDDLSASN-------------- 518
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1062 dFFTLGGHSLLAT---RFCAVAKDKFGLdigVIDLFNASTVEALAN---RLRTRDTGGSD 1115
Cdd:PRK06060 519 -MTIAGGNDGGATlreRLVALRQERQRL---VVDAVCAEAAKMLGEpdpWSVDQDLAFSE 574
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
529-1018 |
6.74e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 114.21 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 529 AGPQYFhELFEAHVARAPQAAALIMpqADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWK 608
Cdd:PRK05852 14 FGPRIA-DLVEVAATRLPEAPALVV--TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 609 AGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSS--------------IDLPKTANRLNLDEDFPDDESADNLETVTHSS 674
Cdd:PRK05852 91 ADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADgphdraepttrwwpLTVNVGGDSGPSGGTLSVHLDAATEPTPATST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 675 QL------AYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPR 748
Cdd:PRK05852 171 PEglrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 749 YATLPGAELADILRARHVTHLTMTPSA---LLSLPVDDLL-----SLRTVLVGGEVPMPELIErwGKTRRF----INAYG 816
Cdd:PRK05852 251 RGRFSAHTFWDDIKAVGATWYTAVPTIhqiLLERAATEPSgrkpaALRFIRSCSAPLTAETAQ--ALQTEFaapvVCAFG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 817 PTETTVNASMVDM-GGGRAGLPVLRP-----AANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFvpd 890
Cdd:PRK05852 329 MTEATHQVTTTQIeGIGQTENPVVSTglvgrSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF--- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 891 pfaTDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAV 970
Cdd:PRK05852 406 ---TDG----WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 796556827 971 PQidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:PRK05852 479 PR----ESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLD 522
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
542-1021 |
1.36e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 113.10 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 542 VARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYP 621
Cdd:PRK08316 21 ARRYPDKTALV----FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 622 AERIGAMLSDAGARLVVSHSSI--DLPKTANRLNLD--------------------EDFPDDESADNLETVTHSSQLAYV 679
Cdd:PRK08316 97 GEELAYILDHSGARAFLVDPALapTAEAALALLPVDtlilslvlggreapggwldfADWAEAGSVAEPDVELADDDLAQI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 680 IYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQ----FFSFSFDA-SIPELVMSlgagarllllpryAT--- 751
Cdd:PRK08316 177 LYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHalplYHCAQLDVfLGPYLYVG-------------ATnvi 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 752 LPGAELADILR--ARH-VTHLTMTPS---ALLSLPV---DDLLSLRTVLVGGEVpMP-----ELIERWGKTrRFINAYGP 817
Cdd:PRK08316 244 LDAPDPELILRtiEAErITSFFAPPTvwiSLLRHPDfdtRDLSSLRKGYYGASI-MPvevlkELRERLPGL-RFYNCYGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 818 TE-----TTVNASMVDMGGGRAGLPVLrpaaNKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFvpdpf 892
Cdd:PRK08316 322 TEiaplaTVLGPEEHLRRPGSAGRPVL----NVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF----- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 893 atdgrAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQ 972
Cdd:PRK08316 393 -----RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 796556827 973 IDQDAatrpTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIdpLK 1021
Cdd:PRK08316 468 AGATV----TEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI--LK 510
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
521-1022 |
1.69e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 113.90 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 521 FNSTAQEHAG-PQYFHELFEAHVARAPQAAALI-MPQADADD---IMTYGELNARANRLARLLRRKGVSAETVVAISLPR 595
Cdd:PRK07529 13 IEAVPLAARDlPASTYELLSRAAARHPDAPALSfLLDADPLDrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 596 SFDMIVAWLAVWKAGGAYlPLDPEYPAERIGAMLSDAGARLVVSHSS-------------------------IDLPK--- 647
Cdd:PRK07529 93 LPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwqkvaevlaalpelrtvveVDLARylp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 648 --------------TANRLNLDEDFpDDESADNLE--TVTHSSQLAYVIYTSGSTGKAKGVLVDHSG----------LIN 701
Cdd:PRK07529 172 gpkrlavplirrkaHARILDFDAEL-ARQPGDRLFsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevanawlgalLLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 702 LTRDKIRACDVTAddcvlqffsFSFDASIPELVMSLGagarllllpRYATL----------PG--AELADILRARHVTHL 769
Cdd:PRK07529 251 LGPGDTVFCGLPL---------FHVNALLVTGLAPLA---------RGAHVvlatpqgyrgPGviANFWKIVERYRINFL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 770 TMTP---SALLSLPVD--DLLSLRTVLVGGeVPMP-ELIERWGKTR--RFINAYGPTETTVNASMVDMGG----GRAGLP 837
Cdd:PRK07529 313 SGVPtvyAALLQVPVDghDISSLRYALCGA-APLPvEVFRRFEAATgvRIVEGYGLTEATCVSSVNPPDGerriGSVGLR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 838 VlrPAANKQLYVLDDN---LELLPFGVPGELHIGGCGIARGY----HDRAALTAERFVpdpfatdgragvlyRTGDRAVL 910
Cdd:PRK07529 392 L--PYQRVRVVILDDAgryLRDCAVDEVGVLCIAGPNVFSGYleaaHNKGLWLEDGWL--------------NTGDLGRI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 911 LADGRIHVSGRLDSQVkIR-GYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAvpQIDQDAATrpTPSEIRAW 989
Cdd:PRK07529 456 DADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYV--QLKPGASA--TEAELLAF 530
|
570 580 590
....*....|....*....|....*....|....
gi 796556827 990 LANRLP-KFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK07529 531 ARDHIAeRAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
523-1018 |
2.86e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 112.00 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 523 STAQEHAGPQYFHELFEAhVARAPQAAALIMPqadaDDIMTYGELNARANRLARLLRRKGVSAETVVAI-SLPRS---FD 598
Cdd:PRK06188 4 MADLLHSGATYGHLLVSA-LKRYPDRPALVLG----DTRLTYGQLADRISRYIQAFEALGLGTGDAVALlSLNRPevlMA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 599 MIVAWLAVWK-------------------AGGAYLPLDPEYPAERIGAMLSDA-GARLVVSHSsiDLPKTANRLNLDEDF 658
Cdd:PRK06188 79 IGAAQLAGLRrtalhplgslddhayvledAGISTLIVDPAPFVERALALLARVpSLKHVLTLG--PVPDGVDLLAAAAKF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 659 PDDEsadnLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDAS---IPELVm 735
Cdd:PRK06188 157 GPAP----LVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGaffLPTLL- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 736 slgagarllllpRYAT---LPGAELADILRA--RHVTHLTM-TPS---ALLSLPVD---DLLSLRTVLVGGEvPMP---- 799
Cdd:PRK06188 232 ------------RGGTvivLAKFDPAEVLRAieEQRITATFlVPTmiyALLDHPDLrtrDLSSLETVYYGAS-PMSpvrl 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 800 -ELIERWGKTrrFINAYGPTETTVNASMVDMGGGRAGLPVL-----RPAANKQLYVLDDNLELLPFGVPGELHIGGCGIA 873
Cdd:PRK06188 299 aEAIERFGPI--FAQYYGQTEAPMVITYLRKRDHDPDDPKRltscgRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 874 RGYHDRAALTAERFvpdpfatdgRAGVLyRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATV 953
Cdd:PRK06188 377 DGYWNRPEETAEAF---------RDGWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 796556827 954 AVRDDGRGGKRLAAYAVPQIDQDaatrPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:PRK06188 447 IGVPDEKWGEAVTAVVVLRPGAA----VDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPD 507
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
562-980 |
3.78e-25 |
|
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: 110.76 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVshs 641
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 sidlpktanrlnldedfpddesadnletVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQF 721
Cdd:cd05907 83 ----------------------------VEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 722 FSFsfdASIPELVMSLGAGARLLLLPRYATLPGAELADILRARhvthltmtPSALLSLP--------------------- 780
Cdd:cd05907 135 LPL---AHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVR--------PTVFLAVPrvwekvyaaikvkavpglkrk 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 781 VDDLL---SLRTVLVGGeVPMPELIERW----GKTrrFINAYGPTETTVNASMVDMGGGRAGLP--VLRPAankQLYVLD 851
Cdd:cd05907 204 LFDLAvggRLRFAASGG-APLPAELLHFfralGIP--VYEGYGLTETSAVVTLNPPGDNRIGTVgkPLPGV---EVRIAD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 852 DnlellpfgvpGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRL-DSQVKIRG 930
Cdd:cd05907 278 D----------GEILVRGPNVMLGYYKNPEATAEALDADGW---------LHTGDLGEIDEDGFLHITGRKkDLIITSGG 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 796556827 931 YRIEPGEIEARLLAHPAIvSATVAVrddGRGGKRLAAYAVPqiDQDAATR 980
Cdd:cd05907 339 KNISPEPIENALKASPLI-SQAVVI---GDGRPFLVALIVP--DPEALEA 382
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
557-1017 |
1.82e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 108.90 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 557 DADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARL 636
Cdd:PRK03640 23 FEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 637 V----------VSHSSI---DLPKTANR-LNLDEDFPDDESADnletvthssqlayVIYTSGSTGKAKGVLV---DH--- 696
Cdd:PRK03640 103 LitdddfeaklIPGISVkfaELMNGPKEeAEIQEEFDLDEVAT-------------IMYTSGTTGKPKGVIQtygNHwws 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 697 --SGLINLtrdkiracDVTADDC---VLQFFSFS--------------------FDAS-IPELVMSlgagarllllprya 750
Cdd:PRK03640 170 avGSALNL--------GLTEDDCwlaAVPIFHISglsilmrsviygmrvvlvekFDAEkINKLLQT-------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 751 tlpgaeladilraRHVTHLTMTPSALlslpvDDLL----------SLRTVLVGG-EVPMPELIErwGKTRRF--INAYGP 817
Cdd:PRK03640 228 -------------GGVTIISVVSTML-----QRLLerlgegtypsSFRCMLLGGgPAPKPLLEQ--CKEKGIpvYQSYGM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 818 TETtvnASMV------DMGG--GRAGLPvLRPAankQLYVLDDNLELLPFGVpGELHIGGCGIARGYHDRAALTAERFVp 889
Cdd:PRK03640 288 TET---ASQIvtlspeDALTklGSAGKP-LFPC---ELKIEKDGVVVPPFEE-GEIVVKGPNVTKGYLNREDATRETFQ- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 890 dpfatDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYA 969
Cdd:PRK03640 359 -----DG----WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 796556827 970 VpqidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK03640 430 V------KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKL 471
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
559-1017 |
2.46e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 108.54 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 559 DDIMTYGELNARANRLARLLRRKGV-------SAETVVAIslprsfdmiVAWLAvwkAGGAYLPLDPEY-PAERiGAMLS 630
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAERVAGARRvavlatpTLATVLAV---------VGALI---AGVPVVPVPPDSgVAER-RHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 631 DAGARLVVSHSSID---LPKTANRLNLDEDFPDDESADnletvthsSQLAYVIYTSGSTGKAKGVLvdhsglinLTRDKI 707
Cdd:PRK07787 90 DSGAQAWLGPAPDDpagLPHVPVRLHARSWHRYPEPDP--------DAPALIVYTSGTTGPPKGVV--------LSRRAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 708 RAC--------DVTADDCV---LQFF-----------SFSFDASIPELVMSLGAGARLLLLPRYATLPG--------AEL 757
Cdd:PRK07787 154 AADldalaeawQWTADDVLvhgLPLFhvhglvlgvlgPLRIGNRFVHTGRPTPEAYAQALSEGGTLYFGvptvwsriAAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 758 ADILRARHVTHLTMTPSALLSLPVDDLLSLRTvlvGGEVpmpelIERwgktrrfinaYGPTETTVNASMVDMGGGRAGLp 837
Cdd:PRK07787 234 PEAARALRGARLLVSGSAALPVPVFDRLAALT---GHRP-----VER----------YGMTETLITLSTRADGERRPGW- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 838 VLRPAANKQLYVLDDNLELLPFGVP--GELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGR 915
Cdd:PRK07787 295 VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW---------FRTGDVAVVDPDGM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 916 IHVSGRLDSQ-VKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqdaATRPTPSEIRAWLANRL 994
Cdd:PRK07787 366 HRIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVG------ADDVAADELIDFVAQQL 439
|
490 500
....*....|....*....|...
gi 796556827 995 PKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK07787 440 SVHKRPREVRFVDALPRNAMGKV 462
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
541-1017 |
2.52e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 109.01 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALIMPQADAddIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEY 620
Cdd:PRK13391 6 HAQTTPDKPAVIMASTGE--VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 621 PAERIGAMLSDAGAR-LVVSHSSID--------LPKTANRLNLDEDfPDDESADNLETVThSSQLAYVI----------Y 681
Cdd:PRK13391 84 TPAEAAYIVDDSGARaLITSAAKLDvarallkqCPGVRHRLVLDGD-GELEGFVGYAEAV-AGLPATPIadeslgtdmlY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 682 TSGSTGKAKGVLVDHSGL-----INLTRDKIRACDVTADDCVL----------QFFS---FSFDASIpeLVMSLGAgarl 743
Cdd:PRK13391 162 SSGTTGRPKGIKRPLPEQppdtpLPLTAFLQRLWGFRSDMVYLspaplyhsapQRAVmlvIRLGGTV--IVMEHFD---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 744 lllpryatlPGAELADILRARhVTHLTMTP---SALLSLPVD-----DLLSLRTVlVGGEVPMP-----ELIERWGKtrr 810
Cdd:PRK13391 236 ---------AEQYLALIEEYG-VTHTQLVPtmfSRMLKLPEEvrdkyDLSSLEVA-IHAAAPCPpqvkeQMIDWWGP--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 811 FINA-YGPTE----TTVNASMVDMGGGRAGLPVLrpaanKQLYVLDDNLELLPFGVPGELHIGGcGIARGYHDRAALTAE 885
Cdd:PRK13391 302 IIHEyYAATEglgfTACDSEEWLAHPGTVGRAMF-----GDLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 886 RFVPDP-FATDGRAGvlYRTGDRAVLLADGRIH--VSGrldsqvkirGYRIEPGEIEARLLAHPAIVSATV-AVRDDGRG 961
Cdd:PRK13391 376 ARHPDGtWSTVGDIG--YVDEDGYLYLTDRAAFmiISG---------GVNIYPQEAENLLITHPKVADAAVfGVPNEDLG 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 962 GkrlAAYAVPQ-IDQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK13391 445 E---EVKAVVQpVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
562-1022 |
3.72e-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: 107.56 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRKGVSAE-TVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAG-ARLVVS 639
Cdd:cd05958 11 WTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARiTVALCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 640 HSsidlpktanrlnldedfpddesadnletVTHSSQLAYVIYTSGSTGKAKGVLVDHsglinltRDKIRACD-------- 711
Cdd:cd05958 91 HA----------------------------LTASDDICILAFTSGTTGAPKATMHFH-------RDPLASADryavnvlr 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 712 VTADDCVLQ----FFSFSFDASI--PELVMSLGAGARLLLLPRYATLPGAELADILrarhVTHLTMTPSALLSLPVD--D 783
Cdd:cd05958 136 LREDDRFVGspplAFTFGLGGVLlfPFGVGASGVLLEEATPDLLLSAIARYKPTVL----FTAPTAYRAMLAHPDAAgpD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 784 LLSLRTVLVGGEVPMPELIERWGKTR--RFINAYGPTETT---VNASMVDMGGGRAGLPVlrpaANKQLYVLDDNLELLP 858
Cdd:cd05958 212 LSSLRKCVSAGEALPAALHRAWKEATgiPIIDGIGSTEMFhifISARPGDARPGATGKPV----PGYEAKVVDDEGNPVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 859 FGVPGELHIGGCGIARGYHDRAAltaerfvpdpfATDGRAGVLYrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEI 938
Cdd:cd05958 288 DGTIGRLAVRGPTGCRYLADKRQ-----------RTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 939 EARLLAHPAIVS-ATVAVRDDGRGGKrLAAYAVPQIDQDAATRPTpSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05958 356 EDVLLQHPAVAEcAVVGHPDESRGVV-VKAFVVLRPGVIPGPVLA-RELQDHAKAHIAPYKYPRAIEFVTELPRTATGKL 433
|
....*
gi 796556827 1018 DPLKL 1022
Cdd:cd05958 434 QRFAL 438
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
536-1017 |
1.04e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 107.78 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALIMPQADaddiMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:PRK05605 36 DLYDNAVARFGDRPALDFFGAT----TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLVVSHS-------------------SIDLPK-------TANRLNL--------------- 654
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIVWDkvaptverlrrttpletivSVNMIAampllqrLALRLPIpalrkaraaltgpap 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 655 ---------DEDFPDDESADNLETVTHSSqLAYVIYTSGSTGKAKGVLVDHSGLI-NLTRDKiracdvtaddcvlqffsf 724
Cdd:PRK05605 192 gtvpwetlvDAAIGGDGSDVSHPRPTPDD-VALILYTSGTTGKPKGAQLTHRNLFaNAAQGK------------------ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 725 sfdASIPELVMSLGAGarllllprYATLP-----------------GAELA-----------DILRARHVTHLTMTP--- 773
Cdd:PRK05605 253 ---AWVPGLGDGPERV--------LAALPmfhaygltlcltlavsiGGELVllpapdidlilDAMKKHPPTWLPGVPply 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 774 SALLSLPVDDLLSLRTV--LVGGEVPMP-ELIERWGKTR--RFINAYGPTETTVNASMVDMGGGR----AGLPVlrPAAN 844
Cdd:PRK05605 322 EKIAEAAEERGVDLSGVrnAFSGAMALPvSTVELWEKLTggLLVEGYGLTETSPIIVGNPMSDDRrpgyVGVPF--PDTE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 845 KQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDpfatdgragvLYRTGDRAVLLADGRIHVSGRLDS 924
Cdd:PRK05605 400 VRIVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG----------WFRTGDVVVMEEDGFIRIVDRIKE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 925 QVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPDTFD 1004
Cdd:PRK05605 470 LIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVL----EPGAALDPEGLRAYCREHLTRYKVPRRFY 545
|
570
....*....|...
gi 796556827 1005 WLEALPLTMNGKI 1017
Cdd:PRK05605 546 HVDELPRDQLGKV 558
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
542-1114 |
1.23e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 109.87 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 542 VARAPQAAALIMPQ-------ADADD---IMTYGELNARANRLARLLRRKGVSAETVVAIsLPRSFDMIVAWLAVWKAGG 611
Cdd:PRK05691 11 LVQALQRRAAQTPDrlalrflADDPGegvVLSYRDLDLRARTIAAALQARASFGDRAVLL-FPSGPDYVAAFFGCLYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 612 AYLPLDP-----EYPAERIGAMLSDAGARLVVSHSSIDLPKTANRLNLDEDFPDDESADNLETVTHSS---------QLA 677
Cdd:PRK05691 90 IAVPAYPpesarRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAwqepalqpdDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 678 YVIYTSGSTGKAKGVLVDHSGLINlTRDKIR---ACDVTADDCVLQFFSFSFD------------ASIPELVMSlgagar 742
Cdd:PRK05691 170 FLQYTSGSTALPKGVQVSHGNLVA-NEQLIRhgfGIDLNPDDVIVSWLPLYHDmgliggllqpifSGVPCVLMS------ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 743 llllpryatlPGAELADILR------------------ARHVTHLTMTPSALLSLpvdDLLSLRTVLVGGEVPMPELIER 804
Cdd:PRK05691 243 ----------PAYFLERPLRwleaiseyggtisggpdfAYRLCSERVSESALERL---DLSRWRVAYSGSEPIRQDSLER 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 805 WGK--------TRRFINAYGPTETTVNASmvdmGGGRA-GLPVLRP-----AANKQ--------------------LYVL 850
Cdd:PRK05691 310 FAEkfaacgfdPDSFFASYGLAEATLFVS----GGRRGqGIPALELdaealARNRAepgtgsvlmscgrsqpghavLIVD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 851 DDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVpdpfATDGRAGVlyRTGDRAvLLADGRIHVSGRLDSQVKIRG 930
Cdd:PRK05691 386 PQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFV----EHDGRTWL--RTGDLG-FLRDGELFVTGRLKDMLIVRG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 931 YRIEPGEIEARLLAHPAIVS----ATVAVRDDGRGGKRLAAyavpQIDQDAATRPTPSE----IRAWLANRLPKflVPDT 1002
Cdd:PRK05691 459 HNLYPQDIEKTVEREVEVVRkgrvAAFAVNHQGEEGIGIAA----EISRSVQKILPPQAliksIRQAVAEACQE--APSV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1003 FDWLE--ALPLTMNGKI--------------DPLKL-PAPRAETDPDGRAPEGEMEGRIAGAFGHVLNIDQVAATDDFFT 1065
Cdd:PRK05691 533 VLLLNpgALPKTSSGKLqrsacrlrladgslDSYALfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFL 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 796556827 1066 LGGHSLLATRFCAVAKDKFGLDIGVIDLFNASTVEALANRLRTRDTGGS 1114
Cdd:PRK05691 613 LGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGG 661
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
80-411 |
1.25e-23 |
|
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: 105.47 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQERLWLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRAR-IYSDKGVPKQTISAACDAPFSVV 158
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGfTWRDRAEPLQYVRDDLAPPWALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 159 EISPA-----AAAMEDVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGN 233
Cdd:cd19547 83 DWSGEdpdrrAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 234 aTPEAELPIQYGDFAAWQRERLATeiAGTLDAFWKQHLSqprqttQLVTDMARTAGHGHAGELHdfTIEKETADALRKIA 313
Cdd:cd19547 163 -EPQLSPCRPYRDYVRWIRARTAQ--SEESERFWREYLR------DLTPSPFSTAPADREGEFD--TVVHEFPEQLTRLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 314 A----AHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASR-PHIE-TEDLVGLFVNPLPVRSLVDPFGNFEKALRETHA 387
Cdd:cd19547 232 NeaarGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRpPELEgSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHR 311
|
330 340
....*....|....*....|....
gi 796556827 388 TLRQVISHQDMPFERIVDMVGVQR 411
Cdd:cd19547 312 DLATTAAHGHVPLAQIKSWASGER 335
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
546-997 |
2.05e-23 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 105.34 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERI 625
Cdd:PRK09029 17 PQAIALR----LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 626 GAMLSDAGARLVVSHSSIDLPKTANRLNLDEDFPDDESAdnletvTHSSQLAYVIYTSGSTGKAKGVLvdHSglinltrd 705
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVA------WQPQRLATMTLTSGSTGLPKAAV--HT-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 706 kIRACDVTADDcVLQFFSFSFDASipeLVMSlgagarllllpryatLP----------------GAELAdiLRARH---- 765
Cdd:PRK09029 157 -AQAHLASAEG-VLSLMPFTAQDS---WLLS---------------LPlfhvsgqgivwrwlyaGATLV--VRDKQpleq 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 766 ----VTHLTMTPSALLSLPVDDL--LSLRTVLVGGEVPMPELIERwgKTRRFINA---YGPTE--TTVNASMVDmggGRA 834
Cdd:PRK09029 215 alagCTHASLVPTQLWRLLDNRSepLSLKAVLLGGAAIPVELTEQ--AEQQGIRCwcgYGLTEmaSTVCAKRAD---GLA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 835 GlpVLRPAANKQLYVLDDnlellpfgvpgELHIGGCGIARGY-HDRA--ALTAErfvpdpfatDGragvLYRTGDRAVlL 911
Cdd:PRK09029 290 G--VGSPLPGREVKLVDG-----------EIWLRGASLALGYwRQGQlvPLVND---------EG----WFATRDRGE-W 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 912 ADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRlaAYAVPQIDQDAAtrptPSEIRAWLA 991
Cdd:PRK09029 343 QNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQR--PVAVVESDSEAA----VVNLAEWLQ 416
|
....*.
gi 796556827 992 NRLPKF 997
Cdd:PRK09029 417 DKLARF 422
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
529-1124 |
2.93e-23 |
|
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: 107.48 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 529 AGPQYFHELFEAHVARAPQAAALIMPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWK 608
Cdd:COG3319 1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 609 AGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSSIDLPKTANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGK 688
Cdd:COG3319 81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 689 AKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTH 768
Cdd:COG3319 161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 769 LTMTPSALLSLPVDDLLSLRTVLVGGEVPMPELI-------ERWGKTRRFINAYGPTETTVNASMVDMGGGRAGLPVLRP 841
Cdd:COG3319 241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALllllallLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 842 AANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRAGVLYRTGDRAVLLADGRIHVSGR 921
Cdd:COG3319 321 GPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 922 LDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAATRPtpseiRAWLANRLPKFLVPD 1001
Cdd:COG3319 401 LRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALL-----LLLLLLLLPPPLPPA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1002 TFDWLEALPLTMNGKIDPLKLPAPRAETDPDGRAPEGEMEGRIAGAFGHVLNIDQVAATDDFFTLGGHSLLATRFCAVAK 1081
Cdd:COG3319 476 LLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLL 555
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 796556827 1082 DKFGLDIGVIDLFNASTVEALANRLRTRDTGGSDDETLLLKRD 1124
Cdd:COG3319 556 ALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAG 598
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
523-993 |
2.98e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 106.34 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 523 STAQEHAGPQYFHELFEAHVARAPQAAALIMPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVA 602
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 603 WLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARL------------------------VVSHSSIDLPKTANRLNLDE-- 656
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVlfvedqeqldkllevrdelpslrhIVVLDPRGLRDDPRLLSLDEll 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 657 ----DFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVL------------- 719
Cdd:COG1022 162 algrEVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsflplahvfertv 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 QFFSFSFDASI-----------------PELVMSlgagarlllLPR-----YATL-------PGA---------ELADIL 761
Cdd:COG1022 242 SYYALAAGATVafaespdtlaedlrevkPTFMLA---------VPRvwekvYAGIqakaeeaGGLkrklfrwalAVGRRY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 762 RARHVTHLTMTPSALLSLPVDDLLSLRTV--LVGGEV--------PM-PELIerwgktrRFINA--------YGPTETTV 822
Cdd:COG1022 313 ARARLAGKSPSLLLRLKHALADKLVFSKLreALGGRLrfavsggaALgPELA-------RFFRAlgipvlegYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 823 NASMVDMGGGRAGlPVLRPAANKQLYVLDDnlellpfgvpGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlY 902
Cdd:COG1022 386 VITVNRPGDNRIG-TVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW---------L 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 903 RTGDRAVLLADGRIHVSGRLDSQVKIR-GYRIEPGEIEARLLAHPAIvsATVAVRDDGRggKRLAAYAVPqiDQDAatrp 981
Cdd:COG1022 446 HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLI--EQAVVVGDGR--PFLAALIVP--DFEA---- 515
|
570
....*....|..
gi 796556827 982 tpseIRAWLANR 993
Cdd:COG1022 516 ----LGEWAEEN 523
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
80-497 |
5.19e-23 |
|
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: 103.87 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 80 PLSFAQErlWLIDQIYPGsaLHHI--CIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSV 157
Cdd:cd19534 3 PLTPIQR--WFFEQNLAG--RHHFnqSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 158 VEISPAAAAMEDVIHAETS---RPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNA 234
Cdd:cd19534 79 EVVDLSSLAQAAAIEALAAeaqSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 235 TPeaeLPiQYGDFAAW--------QRERLATEIagtldAFWKQHLSQPRQTtqLVTDMARTagHGHAGELH-DFTIEkET 305
Cdd:cd19534 159 IP---LP-SKTSFQTWaellaeyaQSPALLEEL-----AYWRELPAADYWG--LPKDPEQT--YGDARTVSfTLDEE-ET 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 306 ADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVI-----GtpvasR-PHIETEDL---VGLFVNPLPVRSLVDPFG 376
Cdd:cd19534 225 EALLQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIfleghG-----ReEIDPGLDLsrtVGWFTSMYPVVLDLEASE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 377 NFEKALRETHATLRQvISHQDMPFE--RIVDMVGVQRDPDsHPLFQIKF----QLDAAPRERIRLPGLEMRRLARQDKVS 450
Cdd:cd19534 300 DLGDTLKRVKEQLRR-IPNKGIGYGilRYLTPEGTKRLAF-HPQPEISFnylgQFDQGERDDALFVSAVGGGGSDIGPDT 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 796556827 451 RLDLCLDLRETEAG--LSGTIEYKTALFRAETIGLFASHFQQLLKSIAA 497
Cdd:cd19534 378 PRFALLDINAVVEGgqLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
562-1025 |
6.09e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 104.78 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHS 641
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 siDL--------------------PKTANRLNLDE----------DFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKG 691
Cdd:PRK12406 92 --DLlhglasalpagvtvlsvptpPEIAAAYRISPalltppagaiDWEGWLAQQEPYDGPPVPQPQSMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 692 VlvdhsglinltrdkiracdvtaddcvlqffsfSFDASIPELVMSLGAGARLL-----------LLPRYATLPGA----- 755
Cdd:PRK12406 170 V--------------------------------RRAAPTPEQAAAAEQMRALIyglkpgirallTGPLYHSAPNAyglra 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 756 ----------------ELADILRARHVTHLTMTPSA---LLSLPVD-----DLLSLRTVlVGGEVPMP-----ELIERWG 806
Cdd:PRK12406 218 grlggvlvlqprfdpeELLQLIERHRITHMHMVPTMfirLLKLPEEvrakyDVSSLRHV-IHAAAPCPadvkrAMIEWWG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 807 KTrrFINAYGPTET-TVNASMVDMGGGRAGlPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIAR-GYHDRaalta 884
Cdd:PRK12406 297 PV--IYEYYGSTESgAVTFATSEDALSHPG-TVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNK----- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 885 erfvPDPFATDGRAGvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKR 964
Cdd:PRK12406 369 ----PEKRAEIDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 796556827 965 LAAYAVPQidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPAP 1025
Cdd:PRK12406 444 LMAVVEPQ----PGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
543-1017 |
4.56e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 102.04 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 543 ARAPQAAALIMpqadADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPA 622
Cdd:PRK07470 18 RRFPDRIALVW----GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 623 ERIGAMLSDAGARLVVSHSsiDLPK-----TANRLNLDEDFPDDES----------ADNL------ETVTHSSQLAYvIY 681
Cdd:PRK07470 94 DEVAYLAEASGARAMICHA--DFPEhaaavRAASPDLTHVVAIGGAragldyealvARHLgarvanAAVDHDDPCWF-FF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 682 TSGSTGKAKGVLVDHSGLINLTRDKIraCDV----TADDCVLQFFSFSFDASIPELVMSLgagarllllpRYAT--LPGA 755
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQMAFVITNHL--ADLmpgtTEQDASLVVAPLSHGAGIHQLCQVA----------RGAAtvLLPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 756 ELADI-----LRARH-VTHLTMTPSALLSL----PVD--DLLSLRTVLVGGeVPM-----PELIERWGKTrrFINAYGPT 818
Cdd:PRK07470 239 ERFDPaevwaLVERHrVTNLFTVPTILKMLvehpAVDryDHSSLRYVIYAG-APMyradqKRALAKLGKV--LVQYFGLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 819 ETTVNASMV--------DMGGGRAGlPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPD 890
Cdd:PRK07470 316 EVTGNITVLppalhdaeDGPDARIG-TCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 891 PFatdgragvlyRTGDRAVLLADGRIHVSGRlDSQVKIRG-YRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYA 969
Cdd:PRK07470 395 WF----------RTGDLGHLDARGFLYITGR-ASDMYISGgSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVC 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 796556827 970 VPQidqdAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK07470 464 VAR----DGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
537-1022 |
4.69e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 102.14 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 537 LFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL 616
Cdd:PRK06155 26 MLARQAERYPDRPLLV----FGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 617 DPEYPAERIGAMLSDAGARLVVSHSSIdLPKTANRLNLDEDFP-----DDESADNLETVTHSSQL--------------- 676
Cdd:PRK06155 102 NTALRGPQLEHILRNSGARLLVVEAAL-LAALEAADPGDLPLPavwllDAPASVSVPAGWSTAPLppldapapaaavqpg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 677 --AYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYAtlpG 754
Cdd:PRK06155 181 dtAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFS---A 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 755 AELADILRaRH---VTHL--TMTPsALLSLPV---DDLLSLRTVLVGGeVP---MPELIERWGKTrrFINAYGPTETtvN 823
Cdd:PRK06155 258 SGFWPAVR-RHgatVTYLlgAMVS-ILLSQPAresDRAHRVRVALGPG-VPaalHAAFRERFGVD--LLDGYGSTET--N 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 824 ASM-VDMGGGRAGLpVLRPAANKQLYVLDDNLELLPFGVPGEL---HIGGCGIARGYHDRAALTAERFvpdpfatdgrAG 899
Cdd:PRK06155 331 FVIaVTHGSQRPGS-MGRLAPGFEARVVDEHDQELPDGEPGELllrADEPFAFATGYFGMPEKTVEAW----------RN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 900 VLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATV-AVRDDgRGGKRLAAYAVPQidqdAA 978
Cdd:PRK06155 400 LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfPVPSE-LGEDEVMAAVVLR----DG 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 796556827 979 TRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK06155 475 TALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
563-1017 |
6.08e-22 |
|
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: 101.22 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVV---S 639
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFvdrE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 640 HSSIDLPKTAnrlnlDEDFPDDESADNLETVThssqlayVIYTSGSTGKAKGVLVDHsglinltrdkiRACDVTAddcvl 719
Cdd:cd12118 111 FEYEDLLAEG-----DPDFEWIPPADEWDPIA-------LNYTSGTTGRPKGVVYHH-----------RGAYLNA----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 qffsfsfdasipelvMSLGAGARLLLLPRYA-TLP---------------------------GAELADILRARHVTHLTM 771
Cdd:cd12118 163 ---------------LANILEWEMKQHPVYLwTLPmfhcngwcfpwtvaavggtnvclrkvdAKAIYDLIEKHKVTHFCG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 772 TP---SALLSLPVDDLLSL-RTV--LVGGEVPMPELIERwgKTR---RFINAYGPTET----TVNASMVDMGG------- 831
Cdd:cd12118 228 APtvlNMLANAPPSDARPLpHRVhvMTAGAPPPAAVLAK--MEElgfDVTHVYGLTETygpaTVCAWKPEWDElpteera 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 832 ---GRAGLPVLrpaANKQLYVLDDNLELlpfGVP------GELHIGGCGIARGYHDRAALTAERFvpdpfatdgRAGVlY 902
Cdd:cd12118 306 rlkARQGVRYV---GLEEVDVLDPETMK---PVPrdgktiGEIVFRGNIVMKGYLKNPEATAEAF---------RGGW-F 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 903 RTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAatrpT 982
Cdd:cd12118 370 HSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKV----T 445
|
490 500 510
....*....|....*....|....*....|....*
gi 796556827 983 PSEIRAWLANRLPKFLVPDTFDWLEaLPLTMNGKI 1017
Cdd:cd12118 446 EEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
107-384 |
9.57e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.50 E-value: 9.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 107 LEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVVEISPAAAAMEDVIHAETSRPFDLAAEPP 186
Cdd:PRK12316 3665 LKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPL 3744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 187 IRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNATPEAELPIQYGDFAAWQRERLATEIAGTLDAF 266
Cdd:PRK12316 3745 LRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAY 3824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 267 WKQHLsQPRQTTQLVTDMARTAGHGHAGELHDFTIEKETADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVIGTP 346
Cdd:PRK12316 3825 WQEQL-QGVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLE 3903
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 796556827 347 VASRPH----IETEDLVGLFVNPLPVR-SLVDPFGNFEKALRE 384
Cdd:PRK12316 3904 GHGREDlfadIDLSRTVGWFTSLFPVRlSPVEDLGASIKAIKE 3946
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
539-1017 |
1.12e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 100.70 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 539 EAHVARAPQAAALIMpqadADDIMTYGELNARANRLARLLR-RKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLD 617
Cdd:PRK06839 9 EKRAYLHPDRIAIIT----EEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 618 PEYPAERIGAMLSDAGARLVVSHS-------SIDLPKTANRLNLDEDFPDDESADNLETVTHSSQLAYVI-YTSGSTGKA 689
Cdd:PRK06839 85 IRLTENELIFQLKDSGTTVLFVEKtfqnmalSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASFIIcYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 690 KGVLVDHSGLINLTRDKIRACDVTADDC---VLQFFS------FSFdasiPELVMSLGAGARLLLLPRYA-TLPGAELAD 759
Cdd:PRK06839 165 KGAVLTQENMFWNALNNTFAIDLTMHDRsivLLPLFHiggiglFAF----PTLFAGGVIIVPRKFEPTKAlSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 760 ILRARHVTHLTMTPSALLSLPvdDLLSLRTVLVGGeVPMPELIERWGKTR--RFINAYGPTETTVNASMV--DMGGGRAG 835
Cdd:PRK06839 241 VVMGVPTIHQALINCSKFETT--NLQSVRWFYNGG-APCPEELMREFIDRgfLFGQGFGMTETSPTVFMLseEDARRKVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 836 lPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFvpdpfatdgRAGVLYrTGDRAVLLADGR 915
Cdd:PRK06839 318 -SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI---------QDGWLC-TGDLARVDEDGF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 916 IHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQidqdAATRPTPSEIRAWLANRLP 995
Cdd:PRK06839 387 VYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKK----SSSVLIEKDVIEHCRLFLA 462
|
490 500
....*....|....*....|..
gi 796556827 996 KFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK06839 463 KYKIPKEIVFLKELPKNATGKI 484
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
537-961 |
1.87e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 100.44 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 537 LFEaHVARAPQAAALImpQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL 616
Cdd:PLN02246 29 CFE-RLSEFSDRPCLI--DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 617 DPEYPAERIGAMLSDAGARLVVSHSS------------------IDLPkTANRLNLDEDFPDDESaDNLETVTHSSQLAY 678
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCyvdklkglaeddgvtvvtIDDP-PEGCLHFSELTQADEN-ELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 679 VIYTSGSTGKAKGVLVDHSGLI------------NLTrdkiracdVTADD---CVLQFFS-FSFD----------ASIpe 732
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHKGLVtsvaqqvdgenpNLY--------FHSDDvilCVLPMFHiYSLNsvllcglrvgAAI-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 733 LVMslgagarllllPRYATlpgAELADILRARHVTHLTMTPSALLSL---PV---DDLLSLRTVLVGGeVPMPELIERwG 806
Cdd:PLN02246 254 LIM-----------PKFEI---GALLELIQRHKVTIAPFVPPIVLAIaksPVvekYDLSSIRMVLSGA-APLGKELED-A 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 807 KTRRFINA-----YGPTETTVNASMVdMGGGRAGLPVlRPAA------NKQLYVLD-DNLELLPFGVPGELHIGGCGIAR 874
Cdd:PLN02246 318 FRAKLPNAvlgqgYGMTEAGPVLAMC-LAFAKEPFPV-KSGScgtvvrNAELKIVDpETGASLPRNQPGEICIRGPQIMK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 875 GYHDRAALTAerfvpdpfATDGRAGVLYrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIV-SATV 953
Cdd:PLN02246 396 GYLNDPEATA--------NTIDKDGWLH-TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIAdAAVV 466
|
....*...
gi 796556827 954 AVRDDGRG 961
Cdd:PLN02246 467 PMKDEVAG 474
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
535-1017 |
1.98e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 100.35 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 535 HELFEAHVA--RAPQAAaLIMPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGA 612
Cdd:PRK04319 46 YEAIDRHADggRKDKVA-LRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 613 YLPLDPEYPAERIGAMLSDAGARLVVSHSSIDLPKTANRL-------------NLDE---DFPD--DESADNLETV-THS 673
Cdd:PRK04319 125 VGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLpslkhvllvgedvEEGPgtlDFNAlmEQASDEFDIEwTDR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 674 SQLAYVIYTSGSTGKAKGVLVDHSGLI----------NLTRDKIRACdvTADdcvlqffsfsfdasipelvmslgagarl 743
Cdd:PRK04319 205 EDGAILHYTSGSTGKPKGVLHVHNAMLqhyqtgkyvlDLHEDDVYWC--TAD---------------------------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 744 lllPRYAT----------LPGAEL--------AD----ILRARHVTHLTMTPSA---LLSLPVD-----DLLSLRTVLVG 793
Cdd:PRK04319 255 ---PGWVTgtsygifapwLNGATNvidggrfsPErwyrILEDYKVTVWYTAPTAirmLMGAGDDlvkkyDLSSLRHILSV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 794 GEVPMPELIeRWGKT---RRFINAYGPTET----TVNASMVDMGGGRAGLPVlrP---AAnkqlyVLDDNLELLPFGVPG 863
Cdd:PRK04319 332 GEPLNPEVV-RWGMKvfgLPIHDNWWMTETggimIANYPAMDIKPGSMGKPL--PgieAA-----IVDDQGNELPPNRMG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 864 ELHI--GGCGIARGYHDRAALTAERFVPDpfatdgragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEAR 941
Cdd:PRK04319 404 NLAIkkGWPSMMRGIWNNPEKYESYFAGD----------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 942 LLAHPAIVSATVAVRDDGRGGKRLAAYavpqidqdAATRP--TPS-----EIRAWLANRLPKFLVPDTFDWLEALPLTMN 1014
Cdd:PRK04319 474 LMEHPAVAEAGVIGKPDPVRGEIIKAF--------VALRPgyEPSeelkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRS 545
|
...
gi 796556827 1015 GKI 1017
Cdd:PRK04319 546 GKI 548
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
1146-1401 |
2.67e-21 |
|
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187539 [Multi-domain] Cd Length: 318 Bit Score: 96.59 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPERkVTCLVR-GDDGMsrlrqafrqyDLPQsvltERVTIVTGELSKPGLgLAAAdydni 1224
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLAQGYR-VRALVRsGSDAV----------LLDG----LPVEVVEGDLTDAAS-LAAA----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1225 VRNADCIFHNGAEVHHLHRY-ERLRETNVLGIREILQlACAGEG-RHVHYISTLSALTPRRGSGGDprpvcELESVEGFV 1302
Cdd:cd05228 60 MKGCDRVFHLAAFTSLWAKDrKELYRTNVEGTRNVLD-AALEAGvRRVVHTSSIAALGGPPDGRID-----ETTPWNERP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1303 PPaGGYNRSKWVAEHLVNEAGRRGLPVTIYRPGAISGD-SVTGAFNGSDILC---RLVQAYLYTGTapegerllDMLPVD 1378
Cdd:cd05228 134 FP-NDYYRSKLLAELEVLEAAAEGLDVVIVNPSAVFGPgDEGPTSTGLDVLDylnGKLPAYPPGGT--------SFVDVR 204
|
250 260 270
....*....|....*....|....*....|....*
gi 796556827 1379 HVARAIV------------HLSGKPASAGQVFHLI 1401
Cdd:cd05228 205 DVAEGHIaamekgrrgeryILGGENLSFKQLFETL 239
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
536-1017 |
5.90e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 99.08 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALIMPQADADdiMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:PRK12583 22 DAFDATVARFPDREALVVRHQALR--YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLVV---------------------------SHSSIDLPKTANRLNLDEDFP--------- 659
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVIcadafktsdyhamlqellpglaegqpgALACERLPELRGVVSLAPAPPpgflawhel 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 660 ----DDESADNLETVTHSSQLAYVI---YTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADD--CVLQFFSFSFDASI 730
Cdd:PRK12583 180 qargETVSREALAERQASLDRDDPIniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDrlCVPVPLYHCFGMVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 731 PELV-MSLGAGARLlllPRYATLPGAELADILRARhVTHLTMTPSALLSlPVD-------DLLSLRTVLVGGEVPMPELI 802
Cdd:PRK12583 260 ANLGcMTVGACLVY---PNEAFDPLATLQAVEEER-CTALYGVPTMFIA-ELDhpqrgnfDLSSLRTGIMAGAPCPIEVM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 803 erwgktRRFIN---------AYGPTETtvnaSMVDMGGGRAG-LP-----VLRPAANKQLYVLDDNLELLPFGVPGELHI 867
Cdd:PRK12583 335 ------RRVMDemhmaevqiAYGMTET----SPVSLQTTAADdLErrvetVGRTQPHLEVKVVDPDGATVPRGEIGELCT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 868 GGCGIARGYHDRAALTAERFVPDpfatdgraGVLYrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPA 947
Cdd:PRK12583 405 RGYSVMKGYWNNPEATAESIDED--------GWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPA 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 948 IVSATVAVRDDGRGGKRLAAYAVPQIDQDAatrpTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK12583 476 VADVQVFGVPDEKYGEEIVAWVRLHPGHAA----SEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
537-1017 |
7.31e-21 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 98.02 E-value: 7.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 537 LFEAHVARAPQAAALIMpQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL 616
Cdd:PRK07514 5 LFDALRAAFADRDAPFI-ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 617 DPEYPAERIGAMLSDAGARLVVSHSSI--DLPKTANRLN------LDED----FPD--DESADNLETVTHSSQ-LAYVIY 681
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANfaWLSKIAAAAGaphvetLDADgtgsLLEaaAAAPDDFETVPRGADdLAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 682 TSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQffsfsfdasipelvmslgagarllllpryaTLPGAELADIL 761
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIH------------------------------ALPIFHTHGLF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 762 RARHVThlTMTPSALLSLP------VDDLLSLRTVLVGgeVP-------------------M--------PELIE----- 803
Cdd:PRK07514 214 VATNVA--LLAGASMIFLPkfdpdaVLALMPRATVMMG--VPtfytrllqeprltreaaahMrlfisgsaPLLAEthref 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 804 --RWGktRRFINAYGPTETTVNASMVDMGGGRAGlPVLRPAANKQLYVLD-DNLELLPFGVPGELHIGGCGIARGYHDRA 880
Cdd:PRK07514 290 qeRTG--HAILERYGMTETNMNTSNPYDGERRAG-TVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 881 ALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIV-SATVAV--RD 957
Cdd:PRK07514 367 EKTAEEFRADGF---------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVeSAVIGVphPD 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 796556827 958 DGRGGkrlAAYAVPQIDQDaatrPTPSEIRAWLANRLPKFLVPDTFDWLEALPL-TMnGKI 1017
Cdd:PRK07514 438 FGEGV---TAVVVPKPGAA----LDEAAILAALKGRLARFKQPKRVFFVDELPRnTM-GKV 490
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
541-1017 |
9.40e-21 |
|
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: 98.40 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALIMPQADADD--IMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAG-------G 611
Cdd:cd05966 62 HLKERGDKVAIIWEGDEPDQsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGavhsvvfA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 612 AYlplDPEYPAERIgamlSDAGARLVVSHS-------SIDLPKTAN----------------RLNLDEDFPD-------- 660
Cdd:cd05966 142 GF---SAESLADRI----NDAQCKLVITADggyrggkVIPLKEIVDealekcpsvekvlvvkRTGGEVPMTEgrdlwwhd 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 661 ---DESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSG-----------LINLTRDKIRACdvTAD----------- 715
Cdd:cd05966 215 lmaKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGyllyaattfkyVFDYHPDDIYWC--TADigwitghsyiv 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 716 --------DCVLqffsfsFDAsipelvmslgagarlllLPRYatlPGAE-LADILRARHVTHLTMTPSALLSL------P 780
Cdd:cd05966 293 ygplangaTTVM------FEG-----------------TPTY---PDPGrYWDIVEKHKVTIFYTAPTAIRALmkfgdeW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 781 VD--DLLSLR---TVlvgGEVPMPElIERW-----GKTR-RFINAYGPTET-----TVNASMVDMGGGRAGLPV--LRPA 842
Cdd:cd05966 347 VKkhDLSSLRvlgSV---GEPINPE-AWMWyyeviGKERcPIVDTWWQTETggimiTPLPGATPLKPGSATRPFfgIEPA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 843 ankqlyVLDDNLELLPFGVPGELHIGGC--GIARG-YHDRaaltaERFVPDPFATDgrAGVlYRTGDRAVLLADGRIHVS 919
Cdd:cd05966 423 ------ILDEEGNEVEGEVEGYLVIKRPwpGMARTiYGDH-----ERYEDTYFSKF--PGY-YFTGDGARRDEDGYYWIT 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 920 GRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQiDQDAATRPTPSEIRAWLANRLPKFLV 999
Cdd:cd05966 489 GRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLK-DGEEPSDELRKELRKHVRKEIGPIAT 567
|
570
....*....|....*...
gi 796556827 1000 PDTFDWLEALPLTMNGKI 1017
Cdd:cd05966 568 PDKIQFVPGLPKTRSGKI 585
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
563-1017 |
2.76e-20 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 96.59 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHS- 641
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDt 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 ------SIDLP-------KTANRLNLDE--DFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLInltrdk 706
Cdd:PLN02330 137 nygkvkGLGLPvivlgeeKIEGAVNWKEllEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLV------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 707 iracdvtADDCVlQFFSFSfdasiPELVMSLGAGARLLLLPRY-------ATLPGA---------ELADILRA---RHVT 767
Cdd:PLN02330 211 -------ANLCS-SLFSVG-----PEMIGQVVTLGLIPFFHIYgitgiccATLRNKgkvvvmsrfELRTFLNAlitQEVS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 768 HLTMTPSALLSLPVD------DL--LSLRTVLVGGEVPMPELIERWGKtrRFIN-----AYGPTE---TTVNASMVDMGG 831
Cdd:PLN02330 278 FAPIVPPIILNLVKNpiveefDLskLKLQAIMTAAAPLAPELLTAFEA--KFPGvqvqeAYGLTEhscITLTHGDPEKGH 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 832 G---RAGLPVLRPaaNKQLYVLD-DNLELLPFGVPGELHIGGCGIARGYHDRAALTAErfvpdpfaTDGRAGVLYrTGDR 907
Cdd:PLN02330 356 GiakKNSVGFILP--NLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDR--------TIDEDGWLH-TGDI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 908 AVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVpqIDQDAatRPTPSEIR 987
Cdd:PLN02330 425 GYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV--INPKA--KESEEDIL 500
|
490 500 510
....*....|....*....|....*....|
gi 796556827 988 AWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PLN02330 501 NFVAANVAHYKKVRVVQFVDSIPKSLSGKI 530
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
761-1022 |
3.32e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 94.08 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 761 LRARH-VTHLTMTP---SALLSLPVD-DLLSLRTVLVGGEvPMP-ELIERWGKTR--RFINAYGPTETTVNASMVDMGG- 831
Cdd:cd05944 92 LVERYrITSLSTVPtvyAALLQVPVNaDISSLRFAMSGAA-PLPvELRARFEDATglPVVEGYGLTEATCLVAVNPPDGp 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 832 ---GRAGLPVlrPAANKQLYVLD-DNLELLPFGVP--GELHIGGCGIARGY----HDRAALTAERFVpdpfatdgragvl 901
Cdd:cd05944 171 krpGSVGLRL--PYARVRIKVLDgVGRLLRDCAPDevGEICVAGPGVFGGYlyteGNKNAFVADGWL------------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 902 yRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAvpQIDQDAATrp 981
Cdd:cd05944 236 -NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYV--QLKPGAVV-- 310
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 796556827 982 TPSEIRAWLANRLP-KFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:cd05944 311 EEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
541-1017 |
7.24e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 95.23 E-value: 7.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARApqaaALIMPQADA----DDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL 616
Cdd:PRK07786 22 QLARH----ALMQPDAPAlrflGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 617 DPEYPAERIGAMLSDAGARLVVSHSSIDLPKTANR--------------------LNLDEDFPDDESADNLETVTHSSQl 676
Cdd:PRK07786 98 NFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRdivpllstvvvaggssddsvLGYEDLLAEAGPAHAPVDIPNDSP- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 677 AYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDV-TADD---CVLQFFSFsfdASIPELVMSLGAGARLLLLPRYATL 752
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINSDvgfVGVPLFHI---AGIGSMLPGLLLGAPTVIYPLGAFD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 753 PGaELADILRARHVTHLTMTPS---ALLSLPVDDL--LSLRtVLVGGEVPMPE-LIERWGKT---RRFINAYGPTETTVN 823
Cdd:PRK07786 254 PG-QLLDVLEAEKVTGIFLVPAqwqAVCAEQQARPrdLALR-VLSWGAAPASDtLLRQMAATfpeAQILAAFGQTEMSPV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 824 ASMVDMGGGRAGL-PVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFvpdpfatdgrAGVLY 902
Cdd:PRK07786 332 TCMLLGEDAIRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF----------AGGWF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 903 RTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAATRpt 982
Cdd:PRK07786 402 HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTL-- 479
|
490 500 510
....*....|....*....|....*....|....*
gi 796556827 983 pSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK07786 480 -EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
663-1018 |
1.02e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 92.83 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 663 SADNLetvthssqlaYVIYTSGSTGKAKGVLVDHS-------GLINLTR----DKIRACDVTADDCVLQFFSfsfdasIP 731
Cdd:cd05924 2 SADDL----------YILYTGGTTGMPKGVMWRQEdifrmlmGGADFGTgeftPSEDAHKAAAAAAGTVMFP------AP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 732 ELV--------MSLGAGARLLLLPRYATLPGAELADILRARhVTHLTMTPSALLSLPVD--------DLLSLRTVLVGGE 795
Cdd:cd05924 66 PLMhgtgswtaFGGLLGGQTVVLPDDRFDPEEVWRTIEKHK-VTSMTIVGDAMARPLIDalrdagpyDLSSLFAISSGGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 796 VPMPELIERW---GKTRRFINAYGPTETTVNASMVDMGGGRAGLPvlRPAANKQLYVLDDNLELLPFGVPGELHIGGCG- 871
Cdd:cd05924 145 LLSPEVKQGLlelVPNITLVDAFGSSETGFTGSGHSAGSGPETGP--FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGh 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 872 IARGYHDRAALTAERFVpdpfATDGRAGVLyrTGDRAVLLADGRIHVSGRlDSQ-VKIRGYRIEPGEIEARLLAHPAIVS 950
Cdd:cd05924 223 IPLGYYGDEAKTAETFP----EVDGVRYAV--PGDRATVEADGTVTLLGR-GSVcINTGGEKVFPEEVEEALKSHPAVYD 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 951 ATVAVRDDGRGGKRLAayAVPQIDQDAatRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd05924 296 VLVVGRPDERWGQEVV--AVVQLREGA--GVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
532-1042 |
1.16e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 94.71 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 532 QYFHELFEAHVARAPQAAALIMPQADaddiMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGG 611
Cdd:PRK06710 24 QPLHKYVEQMASRYPEKKALHFLGKD----ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 612 AYLPLDPEYPAERIGAMLSDAGARLVVSHSSIdLPKTAN-------------RL--------NLDEDFPDDESADNLETV 670
Cdd:PRK06710 100 IVVQTNPLYTERELEYQLHDSGAKVILCLDLV-FPRVTNvqsatkiehvivtRIadflpfpkNLLYPFVQKKQSNLVVKV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 671 THS------------------------SQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIR---ACdVTADDCVLQFFS 723
Cdd:PRK06710 179 SESetihlwnsvekevntgvevpcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwlyNC-KEGEEVVLGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 724 FsFDASIPELVMSLGAGARLlllpRYATLPGAELADILRARHVTHLTMTPSA------LLSLPV---DDLLSLRTVlVGG 794
Cdd:PRK06710 258 F-FHVYGMTAVMNLSIMQGY----KMVLIPKFDMKMVFEAIKKHKVTLFPGAptiyiaLLNSPLlkeYDISSIRAC-ISG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 795 EVPMP-ELIERWGKTR--RFINAYGPTE----TTVNASMVDMGGGRAGLPvlRPAANKQLYVLDDNlELLPFGVPGELHI 867
Cdd:PRK06710 332 SAPLPvEVQEKFETVTggKLVEGYGLTEsspvTHSNFLWEKRVPGSIGVP--WPDTEAMIMSLETG-EALPPGEIGEIVV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 868 GGCGIARGYHDRaaltaerfvPDPFATDGRAGVLYrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPA 947
Cdd:PRK06710 409 KGPQIMKGYWNK---------PEETAAVLQDGWLH-TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 948 IVSATVAVRDDGRGGKRLAAYAVPQIDQDAATRPTPSEIRAWLAnrlpKFLVPDTFDWLEALPLTMNGKIdplklpAPRA 1027
Cdd:PRK06710 479 VQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLA----AYKVPKVYEFRDELPKTTVGKI------LRRV 548
|
570
....*....|....*
gi 796556827 1028 ETDPDGRAPEGEMEG 1042
Cdd:PRK06710 549 LIEEEKRKNEDEQTG 563
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
679-1017 |
1.34e-19 |
|
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: 91.79 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 679 VIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADD---CVLQFF-SFSFDASI-----------PELVMSLGAGARL 743
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDrylIINPFFhTFGYKAGIvaclltgatvvPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 744 LLLPRYATLPGAeladilrarhvthltmtPSALLSL------PVDDLLSLRTVLVGGEVPMPELIERWGKTRRFIN---A 814
Cdd:cd17638 85 IERERITVLPGP-----------------PTLFQSLldhpgrKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETvltA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 815 YGPTEttvnASMVDMGggRAGLPVL-------RPAANKQLYVLDDnlellpfgvpGELHIGGCGIARGYHDRAALTAErf 887
Cdd:cd17638 148 YGLTE----AGVATMC--RPGDDAEtvattcgRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAE-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 888 vpdpfATDGRaGVLYrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAA 967
Cdd:cd17638 210 -----AIDAD-GWLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKA 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 796556827 968 YAVpqidqdaaTRP----TPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd17638 283 FVV--------ARPgvtlTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
562-1017 |
1.46e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 94.44 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRK-GVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSH 640
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 641 SSID------LPKTANR--------------------------------LNLDE--DFPDDESADNLETVT----HSSQL 676
Cdd:PRK05677 130 ANMAhlaekvLPKTGVKhvivtevadmlpplkrllinavvkhvkkmvpaYHLPQavKFNDALAKGAGQPVTeanpQADDV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 677 AYVIYTSGSTGKAKGVLVDHSGLI-NLTRDKIRACDVTADDC--------VLQFFSFSFDASIpelVMSLGAGARLLLLP 747
Cdd:PRK05677 210 AVLQYTGGTTGVAKGAMLTHRNLVaNMLQCRALMGSNLNEGCeiliaplpLYHIYAFTFHCMA---MMLIGNHNILISNP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 748 RyaTLPGaeLADILRARHVTHLTMTPSALLSLPVD------DLLSLRTVLVGGEVPMPELIERWGKTR--RFINAYGPTE 819
Cdd:PRK05677 287 R--DLPA--MVKELGKWKFSGFVGLNTLFVALCNNeafrklDFSALKLTLSGGMALQLATAERWKEVTgcAICEGYGMTE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 820 TTVNASMVDMGG---GRAGLPVlrpaANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdg 896
Cdd:PRK05677 363 TSPVVSVNPSQAiqvGTIGIPV----PSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW---- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 897 ragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVS-ATVAVRDDgRGGKRLAAYAVPQIDQ 975
Cdd:PRK05677 435 -----LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGVPDE-KSGEAIKVFVVVKPGE 508
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 796556827 976 DAatrpTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK05677 509 TL----TKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKI 546
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
78-411 |
2.47e-19 |
|
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: 91.98 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 78 CPPLsfaQERLWLIDQIYPGSALHHIciALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPK-QTISAacDAPFS 156
Cdd:cd19545 4 CTPL---QEGLMALTARQPGAYVGQR--VFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLlQVVVK--ESPIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 157 VVEISPAAAAMEDvihaETSRPFDLAaEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYsaevsgnATP 236
Cdd:cd19545 77 WTESTSLDEYLEE----DRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY-------QGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 237 EAELPIQYGDFAAWQRERLATEIAGtldaFWKQHLS--QPRQTTQLVtdmartagHGHAGELHDFTIEKETADALRkiaA 314
Cdd:cd19545 145 PVPQPPPFSRFVKYLRQLDDEAAAE----FWRSYLAglDPAVFPPLP--------SSRYQPRPDATLEHSISLPSS---A 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 315 AHGTTLFTALFTAFNLLIHRYTGQTDLVIGTPVASR----PHIetEDLVGLFVNPLPVRSLVDPFGNFEKALRETHATLR 390
Cdd:cd19545 210 SSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRnapvPGI--EQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLL 287
|
330 340
....*....|....*....|.
gi 796556827 391 QVISHQDMPFERIVDMVGVQR 411
Cdd:cd19545 288 DMIPFEHTGLQNIRRLGPDAR 308
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
563-1018 |
6.92e-19 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 92.05 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSS 642
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 IdLP-------KTANRLN----LDEDFPDDESADN------------LETVTHSSQ-LAYVIYTSGSTGKAKGVLVDHSG 698
Cdd:PRK08008 119 F-YPmyrqiqqEDATPLRhiclTRVALPADDGVSSftqlkaqqpatlCYAPPLSTDdTAEILFTSGTTSRPKGVVITHYN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 699 LINLTRDKIRACDVTADDCVLQFF-SFSFD----ASIPELVMSlgagarllllpryATLPGAE-------LADILRARH- 765
Cdd:PRK08008 198 LRFAGYYSAWQCALRDDDVYLTVMpAFHIDcqctAAMAAFSAG-------------ATFVLLEkysarafWGQVCKYRAt 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 766 VTH-LTMTPSALLSLPV---DDLLSLRTVLVGGEVPMPE---LIERWGKtrRFINAYGPTETTVNASMVDMGGGRAGLPV 838
Cdd:PRK08008 265 ITEcIPMMIRTLMVQPPsanDRQHCLREVMFYLNLSDQEkdaFEERFGV--RLLTSYGMTETIVGIIGDRPGDKRRWPSI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 839 LRPAANKQLYVLDDNLELLPFGVPGELHIGGC---GIARGYHDRAALTAERFVPDpfatdgraGVLYrTGDRAVLLADGR 915
Cdd:PRK08008 343 GRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEAD--------GWLH-TGDTGYVDEEGF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 916 IHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATV-AVRDDGRgGKRLAAYAVPqidqDAATRPTPSEIRAWLANRL 994
Cdd:PRK08008 414 FYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVvGIKDSIR-DEAIKAFVVL----NEGETLSEEEFFAFCEQNM 488
|
490 500
....*....|....*....|....
gi 796556827 995 PKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:PRK08008 489 AKFKVPSYLEIRKDLPRNCSGKII 512
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
673-1018 |
1.18e-18 |
|
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: 91.24 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 673 SSQLAYVIYTSGSTGKAKGVLVDHSGLINlTRDKIRAC-DVTADDCVLQ----FFSFSFDASI-------PELVMSlgag 740
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLA-NVEQITAIfDPNPEDVVFGalpfFHSFGLTGCLwlpllsgIKVVFH---- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 741 arllllprYATLPGAELADILRARHVTHLTMTPSALL----SLPVDDLLSLRTVLVGGEVPMPELIERWGKT--RRFINA 814
Cdd:cd05909 221 --------PNPLDYKKIPELIYDKKATILLGTPTFLRgyarAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 815 YGPTET----TVNASMVDMGGGRAGLPVlrPAANKQLyVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVpd 890
Cdd:cd05909 293 YGTTECspviSVNTPQSPNKEGTVGRPL--PGMEVKI-VSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFG-- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 891 pfatDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAI--VSATVAVrDDGRGGKRLAAY 968
Cdd:cd05909 368 ----DG----WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdnEVAVVSV-PDGRKGEKIVLL 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 796556827 969 AVPqidqdaaTRPTPSEIRAWLAN-RLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd05909 439 TTT-------TDTDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
537-1025 |
1.36e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 91.36 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 537 LFEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL 616
Cdd:PRK13382 48 GFAIAAQRCPDRPGLI----DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 617 DPEYPAERIGAMLSDAGARLV---------VSHSSIDLPKtANRLnldEDFPDDESADNLETV--THSSQLA-------- 677
Cdd:PRK13382 124 NTSFAGPALAEVVTREGVDTViydeefsatVDRALADCPQ-ATRI---VAWTDEDHDLTVEVLiaAHAGQRPeptgrkgr 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 678 YVIYTSGSTGKAKGVLVDHSGLIN-----LTRDKIRACDVTaddcVL---QFFSFSFDASIPELVMSLGAGARLLLLPRy 749
Cdd:PRK13382 200 VILLTSGTTGTPKGARRSGPGGIGtlkaiLDRTPWRAEEPT----VIvapMFHAWGFSQLVLAASLACTIVTRRRFDPE- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 750 ATLpgaELADILRArhvTHLTMTPSAL---LSLPVDDL-----LSLRTVLVGGEvPMP-----ELIERWGKTrrFINAYG 816
Cdd:PRK13382 275 ATL---DLIDRHRA---TGLAVVPVMFdriMDLPAEVRnrysgRSLRFAAASGS-RMRpdvviAFMDQFGDV--IYNNYN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 817 PTE----TTVNASMVDMGGGRAGlpvlRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAaltaerfvpdpf 892
Cdd:PRK13382 346 ATEagmiATATPADLRAAPDTAG----RPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGS------------ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 893 ATDGRAGVLyRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQ 972
Cdd:PRK13382 410 TKDFHDGFM-ASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 796556827 973 IDQDAATRPTPSEIRAWLANrlpkFLVPDTFDWLEALPLTMNGKIDPLKLPAP 1025
Cdd:PRK13382 489 PGASATPETLKQHVRDNLAN----YKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| UDP_G4E_4_SDR_e |
cd05232 |
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ... |
1146-1414 |
1.47e-18 |
|
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187543 [Multi-domain] Cd Length: 303 Bit Score: 88.18 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPErkvtcLVRgddGMSRLRQAFRQydlpqsvltervTIVTGELSKPglgLAAADYdniV 1225
Cdd:cd05232 2 VLVTGANGFIGRALVDKLLSRGE-----EVR---IAVRNAENAEP------------SVVLAELPDI---DSFTDL---F 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNADCIFHNGAEVHHLH-----RYERLRETNVLGIREILQLACAGEGRHVHYISTLSALtprrGSGGDPRPVCElESVEG 1300
Cdd:cd05232 56 LGVDAVVHLAARVHVMNdqgadPLSDYRKVNTELTRRLARAAARQGVKRFVFLSSVKVN----GEGTVGAPFDE-TDPPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1301 fvpPAGGYNRSKWVAEHLVNEAGRR-GLPVTIYRPGAISGDSVTGAFNGsdiLCRLVQAYLYTGTAPEGERlLDMLPVDH 1379
Cdd:cd05232 131 ---PQDAYGRSKLEAERALLELGASdGMEVVILRPPMVYGPGVRGNFAR---LMRLIDRGLPLPPGAVKNR-RSLVSLDN 203
|
250 260 270
....*....|....*....|....*....|....*
gi 796556827 1380 VARAIVHLSGKPASAGQVFHLIHSSPVSSARLFEA 1414
Cdd:cd05232 204 LVDAIYLCISLPKAANGTFLVSDGPPVSTAELVDE 238
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
783-1017 |
2.10e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 91.04 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 783 DLLSLRTVLVGGEVPMPELIERWGKTR--RFINAYGPTETTVNASMVDMGG----GRAGLPVlrpaANKQLYVLDDNLEL 856
Cdd:PRK12492 331 DFSALKLTNSGGTALVKATAERWEQLTgcTIVEGYGLTETSPVASTNPYGElarlGTVGIPV----PGTALKVIDDDGNE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 857 LPFGVPGELHIGGCGIARGYHDRAALTAErfvpdpfATDGRAgvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPG 936
Cdd:PRK12492 407 LPLGERGELCIKGPQVMKGYWQQPEATAE-------ALDAEG--WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPN 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 937 EIEARLLAHPAIVS-ATVAVRDDgRGGKRLAAYAVPQidqdaATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNG 1015
Cdd:PRK12492 478 EIEDVVMAHPKVANcAAIGVPDE-RSGEAVKLFVVAR-----DPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVG 551
|
..
gi 796556827 1016 KI 1017
Cdd:PRK12492 552 KI 553
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
674-1017 |
2.56e-18 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 88.09 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 674 SQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRA-CDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATL 752
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 753 pgAELADILRARHVTHLTMTPSAL--LSLPVDDLL----SLRTVLVGGEVPMPELIE--RWGKTRRFINAYGPTETTvNA 824
Cdd:cd17635 81 --KSLFKILTTNAVTTTCLVPTLLskLVSELKSANatvpSLRLIGYGGSRAIAADVRfiEATGLTNTAQVYGLSETG-TA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 825 SMVDMGGGRAGL-PVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVpdpfatdgraGVLYR 903
Cdd:cd17635 158 LCLPTDDDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI----------DGWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 904 TGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAV-PQIDQDAATRPT 982
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVaSAELDENAIRAL 307
|
330 340 350
....*....|....*....|....*....|....*
gi 796556827 983 PSEIRawlaNRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd17635 308 KHTIR----RELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
635-1022 |
4.20e-18 |
|
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: 89.83 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 635 RLVVSHSSIDlpktaNRLNLDEDFpdDESADNLETVTHSSQLAYVIY-TSGSTGKAKGVLVDHSGL-INLTRDKIRACDV 712
Cdd:cd05928 141 KLLVSEKSRD-----GWLNFKELL--NEASTEHHCVETGSQEPMAIYfTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 713 TADDCVLQFFSFSFDASIPELVMSLGAGAR---LLLLPRYATLpgaELADILRARHVTHLTMTPSALLSLPVDDLLS--- 786
Cdd:cd05928 214 TASDIMWNTSDTGWIKSAWSSLFEPWIQGAcvfVHHLPRFDPL---VILKTLSSYPITTFCGAPTVYRMLVQQDLSSykf 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 787 --LRTVLVGGEVPMPELIERW-GKTRRFI-NAYGPTETTV---NASMVDMGGGRAGLPVlrPAANKQlyVLDDNLELLPF 859
Cdd:cd05928 291 psLQHCVTGGEPLNPEVLEKWkAQTGLDIyEGYGQTETGLicaNFKGMKIKPGSMGKAS--PPYDVQ--IIDDNGNVLPP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 860 GVPGELHIggcgiaRGYHDRAALTAERFVPDPFATDG-RAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEI 938
Cdd:cd05928 367 GTEGDIGI------RVKPIRPFGLFSGYVDNPEKTAAtIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 939 EARLLAHPAIV-SATVAVRDDGRgGKRLAAYAV--PQI---DQDAATRptpsEIRAWLANRLPKFLVPDTFDWLEALPLT 1012
Cdd:cd05928 441 ESALIEHPAVVeSAVVSSPDPIR-GEVVKAFVVlaPQFlshDPEQLTK----ELQQHVKSVTAPYKYPRKVEFVQELPKT 515
|
410
....*....|
gi 796556827 1013 MNGKIDPLKL 1022
Cdd:cd05928 516 VTGKIQRNEL 525
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
491-1024 |
4.95e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 89.29 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 491 LLKSIAADPCLPVATLALLtQEEQRqricdfnstaqehaGPQYFHELFEAHVARAPQAAALImpqaDADDIMTYGELNAR 570
Cdd:PRK13383 9 LVRSGLLNPPSPRAVLRLL-REASR--------------GGTNPYTLLAVTAARWPGRTAII----DDDGALSYRELQRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 571 ANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSS-IDLPKTA 649
Cdd:PRK13383 70 TESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEfAERIAGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 650 NR--LNLDEDFPDDESADNLETVTHSSQLayVIYTSGSTGKAKGV-----LVDHSGL--INLTRDKIR-ACDVTADDCVL 719
Cdd:PRK13383 150 DDavAVIDPATAGAEESGGRPAVAAPGRI--VLLTSGTTGKPKGVprapqLRSAVGVwvTILDRTRLRtGSRISVAMPMF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 QFFSFSFdasipeLVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSALLSLP-----VDDLLSLRTVLVGG 794
Cdd:PRK13383 228 HGLGLGM------LMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPprvraRNPLPQLRVVMSSG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 795 EVPMPELIERWGKTRRFI--NAYGPTETTVNASMVDMGGGRAGLPVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGI 872
Cdd:PRK13383 302 DRLDPTLGQRFMDTYGDIlyNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 873 ARGYHDRAALTAerfvpdpfaTDGRAGvlyrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSAT 952
Cdd:PRK13383 382 GTRYTDGGGKAV---------VDGMTS----TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNA 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 796556827 953 VAVRDDGRGGKRLAAYAV--PQIDQDAAtrptpsEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKLPA 1024
Cdd:PRK13383 449 VIGVPDERFGHRLAAFVVlhPGSGVDAA------QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
531-1017 |
1.20e-17 |
|
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: 88.32 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 531 PQYF---HELFEAHVARAPQAAALI-MPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAV 606
Cdd:cd05970 13 PENFnfaYDVVDAMAKEYPDKLALVwCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 607 WKAGGAYLPL-------DPEYPAER--IGAMLSDAGARL--VVSHSSIDLPKTANRLNLDEDFPD-----DESADNL--- 667
Cdd:cd05970 93 HKLGAIAIPAthqltakDIVYRIESadIKMIVAIAEDNIpeEIEKAAPECPSKPKLVWVGDPVPEgwidfRKLIKNAspd 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 668 ------ETVTHSSQLAYVIYTSGSTGKAKGVLVDHS---GLI-------NLTRDKIRAcdVTADD--------------- 716
Cdd:cd05970 173 ferptaNSYPCGEDILLVYFSSGTTGMPKMVEHDFTyplGHIvtakywqNVREGGLHL--TVADTgwgkavwgkiygqwi 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 717 CVLQFFSFSFDASIPElvmslgagarllllpryatlpgaELADILRARHVTHLTMTPSALLSLPVDDLL-----SLRTVL 791
Cdd:cd05970 251 AGAAVFVYDYDKFDPK-----------------------ALLEKLSKYGVTTFCAPPTIYRFLIREDLSrydlsSLRYCT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 792 VGGEVPMPELIERWGKTR--RFINAYGPTETTVN-ASMVDMGG--GRAGlpvlRPAANKQLYVLDDNLELLPFGVPGELH 866
Cdd:cd05970 308 TAGEALNPEVFNTFKEKTgiKLMEGFGQTETTLTiATFPWMEPkpGSMG----KPAPGYEIDLIDREGRSCEAGEEGEIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 867 IG-----GCGIARGYHDRAALTAERFvpdpfaTDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEAR 941
Cdd:cd05970 384 IRtskgkPVGLFGGYYKDAEKTAEVW------HDG----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 796556827 942 LLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAATRPTpSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05970 454 LIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELK-KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
565-1018 |
1.30e-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: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 565 GELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPaERIGAMLSDAGAR-LVVShssi 643
Cdd:cd05929 21 DVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP-RAEACAIIEIKAAaLVCG---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 644 dLPKTANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTrDKIRACDV----TADDCVL 719
Cdd:cd05929 96 -LFTGGGALDGLEDYEAAEGGSPETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDN-DTLMAAALgfgpGADSVYL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 Q----FFSFSFDASIPELVMSLGAGARllllPRYAtlPGAELADILRARhVTHLTMTP---SALLSLPVD-----DLLSL 787
Cdd:cd05929 174 SpaplYHAAPFRWSMTALFMGGTLVLM----EKFD--PEEFLRLIERYR-VTFAQFVPtmfVRLLKLPEAvrnayDLSSL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 788 RTVLVGGeVPMP-----ELIERWGKtrRFINAYGPTE----TTVNASMVDMGGGRAGLPVLrpaanKQLYVLDDNLELLP 858
Cdd:cd05929 247 KRVIHAA-APCPpwvkeQWIDWGGP--IIWEYYGGTEgqglTIINGEEWLTHPGSVGRAVL-----GKVHILDEDGNEVP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 859 FGVPGELHIGGcGIARGYHDRAALTAERFVPDPFATdgragvlyrTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEI 938
Cdd:cd05929 319 PGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST---------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 939 EARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAATRPTpSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd05929 389 ENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALA-EELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLY 467
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
94-395 |
3.22e-17 |
|
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: 85.95 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 94 IYPGSAL------HH----------ICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDkGVP-------KQtisaa 150
Cdd:cd19544 1 IYPLAPLqegilfHHllaeegdpylLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWE-GLSepvqvvwRQ----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 151 cdAPFSVVEIS-----PAAAAMEDVIHAETSRpFDLAAEPPIRLLVAKCDD-GHHVLVFTLHHICADGWSTEILLKDLGA 224
Cdd:cd19544 75 --AELPVEELTldpgdDALAQLRARFDPRRYR-LDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 225 FYSAEvsgnatpEAEL--PIQYGDFAAWQRERLATEIAgtlDAFWKQHLSQPRQTTqLVTDMARTAGHGHAGELHDFTIE 302
Cdd:cd19544 152 ILAGR-------AAALppPVPYRNFVAQARLGASQAEH---EAFFREMLGDVDEPT-APFGLLDVQGDGSDITEARLALD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 303 KETADALRKIAAAHGTTLfTALF-TAFNLLIHRYTGQTDLVIGTPVASRPH--IETEDLVGLFVNPLPVR-SLVDpfGNF 378
Cdd:cd19544 221 AELAQRLRAQARRLGVSP-ASLFhLAWALVLARCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLRvRLGG--RSV 297
|
330
....*....|....*..
gi 796556827 379 EKALRETHATLRQVISH 395
Cdd:cd19544 298 REAVRQTHARLAELLRH 314
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
679-1018 |
3.68e-17 |
|
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: 84.63 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 679 VIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDC---VLQFF-------SFS-FDASIPELVMSlgagarllllp 747
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVylnMLPLFhiaglnlALAtFHAGGANVVME----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 748 RYATlpgAELADILRARHVTHLTMTPSALLSL-------PVDdLLSLRTVLvggEVPMPELIERWGKT--RRFINAYGPT 818
Cdd:cd17637 74 KFDP---AEALELIEEEKVTLMGSFPPILSNLldaaeksGVD-LSSLRHVL---GLDAPETIQRFEETtgATFWSLYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 819 ETTVNASM--VDMGGGRAGlpvlRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFvpdpfatdg 896
Cdd:cd17637 147 ETSGLVTLspYRERPGSAG----RPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF--------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 897 RAGvLYRTGDRAVLLADGRIHVSGRLDSQ--VKIRGYRIEPGEIEARLLAHPAIVSATV-AVRDD--GRGGKrlaayAVP 971
Cdd:cd17637 214 RNG-WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCViGVPDPkwGEGIK-----AVC 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 796556827 972 QIdqDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd17637 288 VL--KPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSID 332
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
536-1022 |
3.90e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.79 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALIMPqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:PRK08315 20 QLLDRTAARYPDREALVYR--DQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLVVSHSS--------------------------------------IDLPKTANRLNLDE- 656
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlyelapelatcepgqlqsarlpelrrvifLGDEKHPGMLNFDEl 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 657 -DFPDDESADNLETVTHSSQLAYVI---YTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADD-------------CVL 719
Cdd:PRK08315 178 lALGRAVDDAELAARQATLDPDDPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcipvplyhcfgMVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 Q------------FFSFSFDasiPELVMSLGAGArllllpRYATLPG------AELADILRARHvthltmtpsallslpv 781
Cdd:PRK08315 258 GnlacvthgatmvYPGEGFD---PLATLAAVEEE------RCTALYGvptmfiAELDHPDFARF---------------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 782 dDLLSLRTVLVGG-----EVpMPELIERWGKTRRFInAYGPTET------------------TVnasmvdmggGRAgLPV 838
Cdd:PRK08315 313 -DLSSLRTGIMAGspcpiEV-MKRVIDKMHMSEVTI-AYGMTETspvstqtrtddplekrvtTV---------GRA-LPH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 839 LrpaankQLYVLD-DNLELLPFGVPGELHIGGCGIARGYHDRAALTAErfvpdpfATDgRAGVLyRTGDRAVLLADGRIH 917
Cdd:PRK08315 380 L------EVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE-------AID-ADGWM-HTGDLAVMDEEGYVN 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 918 VSGRLDSQVkIR-GYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAatrpTPSEIRAWLANRLPK 996
Cdd:PRK08315 445 IVGRIKDMI-IRgGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATL----TEEDVRDFCRGKIAH 519
|
570 580
....*....|....*....|....*.
gi 796556827 997 FLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK08315 520 YKIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
671-1018 |
4.01e-17 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 87.67 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 671 THSSQLAYVIYTSGSTGKAKGVLVDH----------SGLINLTRDkiracDVTADdcVLQFF-SFSFDASIpELVMSLGA 739
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMLSHhnilsnieqiSDVFNLRND-----DVILS--SLPFFhSFGLTVTL-WLPLLEGI 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 740 GARLLLLPryatLPGAELADILRARHVTHLTMTPSALLS------LPVDDLLSLRTVLVGGEVPMPEL----IERWGKtr 809
Cdd:PRK08633 851 KVVYHPDP----TDALGIAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAEKLKPEVadafEEKFGI-- 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 810 RFINAYGPTETT----VNASMVDMGG---------GRAGLPVLRPAANkqlyVLD-DNLELLPFGVPGELHIGGCGIARG 875
Cdd:PRK08633 925 RILEGYGATETSpvasVNLPDVLAADfkrqtgskeGSVGMPLPGVAVR----IVDpETFEELPPGEDGLILIGGPQVMKG 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 876 YHDRAALTAErfvpdpFATDGRAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIE---ARLLAHPAIVSAT 952
Cdd:PRK08633 1001 YLGDPEKTAE------VIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeelAKALGGEEVVFAV 1074
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 953 VAVRDDGRGGKRLAAYAVPQIDqdaatrptPSEIRAWLAN-RLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:PRK08633 1075 TAVPDEKKGEKLVVLHTCGAED--------VEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
563-948 |
5.74e-17 |
|
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: 85.98 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSS 642
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 IDLPKTAN---------RLNLDEDFPDDESADNL---------ETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTR 704
Cdd:cd05932 88 DDWKAMAPgvpeglisiSLPPPSAANCQYQWDDLiaqhppleeRPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 705 DKIRACDVTADDCVLQFFSFsfdASIPELVMSLGAGARLLLLPRYATLPGAELADILRAR---------------HVTHL 769
Cdd:cd05932 168 AGIEHIGTEENDRMLSYLPL---AHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQRARptlffsvprlwtkfqQGVQD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 770 TMTPSA---LLSLPVDDLLSLRTVLVG-----------GEVPMPELIERWgkTRRF----INAYGPTETTVNASMVDMGG 831
Cdd:cd05932 245 KIPQQKlnlLLKIPVVNSLVKRKVLKGlgldqcrlagcGSAPVPPALLEW--YRSLglniLEAYGMTENFAYSHLNYPGR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 832 GRAGLpVLRPAANKQLYVLDDnlellpfgvpGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLL 911
Cdd:cd05932 323 DKIGT-VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF---------LRTGDKGELD 382
|
410 420 430
....*....|....*....|....*....|....*...
gi 796556827 912 ADGRIHVSGRLDSQVKI-RGYRIEPGEIEARLLAHPAI 948
Cdd:cd05932 383 ADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV 420
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
546-1017 |
9.76e-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: 85.83 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 546 PQAAALIM--PQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAE 623
Cdd:cd05967 65 GDQIALIYdsPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 624 RIGAMLSDAGARLVVS-----------------HSSIDLPKTANRLNLDEDFPD--DESADNLETVTHSSQLA------- 677
Cdd:cd05967 145 ELASRIDDAKPKLIVTascgiepgkvvpykpllDKALELSGHKPHHVLVLNRPQvpADLTKPGRDLDWSELLAkaepvdc 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 678 ---------YVIYTSGSTGKAKGVLVDHSGLINLTRDKIRAC-DVTADDCvlqFFSFSfdaSIPELV----------MSL 737
Cdd:cd05967 225 vpvaatdplYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIyGIKPGDV---WWAAS---DVGWVVghsyivygplLHG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 738 GAGARLLLLPRYATLPGAELADIlrARH-VTHLTMTPSALLSLPVDD----------LLSLRTVLVGGE---VPMPELIE 803
Cdd:cd05967 299 ATTVLYEGKPVGTPDPGAFWRVI--EKYqVNALFTAPTAIRAIRKEDpdgkyikkydLSSLRTLFLAGErldPPTLEWAE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 804 RwgKTRR-FINAYGPTET----TVNASMVDMGGGRAGLPVlRPAANKQLYVLDDNLELLPFGVPGELHIG-----GCgIA 873
Cdd:cd05967 377 N--TLGVpVIDHWWQTETgwpiTANPVGLEPLPIKAGSPG-KPVPGYQVQVLDEDGEPVGPNELGNIVIKlplppGC-LL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 874 RGYHDRaaltaERFVPDPFATDgrAGVlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVS-AT 952
Cdd:cd05967 453 TLWKND-----ERFKKLYLSKF--PGY-YDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEcAV 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 796556827 953 VAVRDDGRGGKRLaAYAVP----QIDQDAATRptpsEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05967 525 VGVRDELKGQVPL-GLVVLkegvKITAEELEK----ELVALVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
562-970 |
1.12e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 85.28 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRK-GVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSH 640
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 641 -------SSIDLPKTANRLNLDEDFPDDESADNLETVTHSSQ-----------LAYVIYTSGSTGKAKGVLVDHSGLINL 702
Cdd:PLN02574 147 penveklSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDfvpkpvikqddVAAIMYSSGTTGASKGVVLTHRNLIAM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 703 TRDKIR--ACDVTADDC------VLQFFS-----------FSFDASIpeLVMSLgagarllllpryatLPGAELADILRA 763
Cdd:PLN02574 227 VELFVRfeASQYEYPGSdnvylaALPMFHiyglslfvvglLSLGSTI--VVMRR--------------FDASDMVKVIDR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 764 RHVTHLTMTPSALLSL-----PV--DDLLSLRTVLVGGEVPMPELIERWGKTR---RFINAYGPTETT-VNASMVDMGGG 832
Cdd:PLN02574 291 FKVTHFPVVPPILMALtkkakGVcgEVLKSLKQVSCGAAPLSGKFIQDFVQTLphvDFIQGYGMTESTaVGTRGFNTEKL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 833 RAGLPVLRPAANKQLYVLD-DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLL 911
Cdd:PLN02574 371 SKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW---------LRTGDIAYFD 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 796556827 912 ADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAV 970
Cdd:PLN02574 442 EDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV 500
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
677-1022 |
1.19e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 83.56 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 677 AYVIYTSGSTGKAKGVLVDHSGLIN-----------------------------LTRDKIRACDVTADDcvlqfFSFSFD 727
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTAsadathdrlggpgqwllalpahhiaglqvLVRSVIAGSEPVELD-----VSAGFD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 728 asIPELVMSLGAGARLLllpRYATLPGAELADILRarhvthltmTPSAllslpVDDLLSLRTVLVGGeVPMPELIERWGK 807
Cdd:PRK07824 113 --PTALPRAVAELGGGR---RYTSLVPMQLAKALD---------DPAA-----TAALAELDAVLVGG-GPAPAPVLDAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 808 TR--RFINAYGPTETtvnasmvdmgggrAGLPVL--RPAANKQLYVLDdnlellpfgvpGELHIGGCGIARGYhdRAALT 883
Cdd:PRK07824 173 AAgiNVVRTYGMSET-------------SGGCVYdgVPLDGVRVRVED-----------GRIALGGPTLAKGY--RNPVD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 884 aerfvPDPFATDGragvLYRTGDRAVLlADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGK 963
Cdd:PRK07824 227 -----PDPFAEPG----WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQ 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 796556827 964 RLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK07824 297 RVVAAVVG----DGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
563-976 |
1.92e-16 |
|
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: 84.03 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVshss 642
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 idlpktanrlnldedfpddesadnletVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFF 722
Cdd:cd05914 85 ---------------------------VSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSIL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 723 SFSfdaSIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSAL----------------------LSLP 780
Cdd:cd05914 138 PLH---HIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfkLAKK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 781 VDDLLSLRTV--------------LVGGEVPMPELIERWGKTRRF--INAYGPTETtvnASMVDMGG------GRAGLPV 838
Cdd:cd05914 215 INNRKIRKLAfkkvheafggnikeFVIGGAKINPDVEEFLRTIGFpyTIGYGMTET---APIISYSPpnrirlGSAGKVI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 839 lrpaankqlyvldDNLEL-----LPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLAD 913
Cdd:cd05914 292 -------------DGVEVridspDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW---------FHTGDLGKIDAE 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 796556827 914 GRIHVSGRLDSQ-VKIRGYRIEPGEIEARLLAHPAIVSATVAVRDdgrggKRLAAYAVPQIDQD 976
Cdd:cd05914 350 GYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQE-----KKLVALAYIDPDFL 408
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
107-397 |
2.09e-16 |
|
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: 83.69 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 107 LEVRGA-LDLDALKVALAGVMSRHTVLRARIYSD------KGVPKQTIsAACDapFSVVEISPAAAAMEDVIHAETSRPF 179
Cdd:cd19535 30 LEFDGEdLDPDRLERAWNKLIARHPMLRAVFLDDgtqqilPEVPWYGI-TVHD--LRGLSEEEAEAALEELRERLSHRVL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 180 DLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYsaevsgnATPEAELP---IQYGDFAAWQRERLA 256
Cdd:cd19535 107 DVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALY-------EDPGEPLPpleLSFRDYLLAEQALRE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 257 TEIAGTLdAFWKQHLS------------QPRQTTQlvTDMARtaghghagelHDFTIEKETADALRKIAAAHGTTLFTAL 324
Cdd:cd19535 180 TAYERAR-AYWQERLPtlppapqlplakDPEEIKE--PRFTR----------REHRLSAEQWQRLKERARQHGVTPSMVL 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 325 FTAFNLLIHRYTGQTDLVIGTPVASRP--HIETEDLVGLFVNPLPVRslVDPFG--NFEKALRETHATLRQVISHQD 397
Cdd:cd19535 247 LTAYAEVLARWSGQPRFLLNLTLFNRLplHPDVNDVVGDFTSLLLLE--VDGSEgqSFLERARRLQQQLWEDLDHSS 321
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
538-1018 |
2.77e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 83.68 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 538 FEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVvAISLPRSFDMIVAWLAVWKAGGAYLPLD 617
Cdd:PRK07638 7 YKKHASLQPNKIAIK----ENDRVLTYKDWFESVCKVANWLNEKESKNKTI-AILLENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 618 PEYPAERIGAMLSDAGARLVVS--HSSIDLPKTANR-LNLDEDFPDDESADNLETVTHSSQLA--YVIYTSGSTGKAKGV 692
Cdd:PRK07638 82 IKWKQDELKERLAISNADMIVTerYKLNDLPDEEGRvIEIDEWKRMIEKYLPTYAPIENVQNApfYMGFTSGSTGKPKAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 693 LVDHSGLINLTRDKIRACDVTADDCVL----QFFSFSFDASIPELVMSLGAGARLLLLPryatlpgAELADILRARHVTH 768
Cdd:PRK07638 162 LRAQQSWLHSFDCNVHDFHMKREDSVLiagtLVHSLFLYGAISTLYVGQTVHLMRKFIP-------NQVLDKLETENISV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 769 LTMTPSALLSLPVDDLL---SLRTVLVGGEVPMP---ELIERWGKTRRFiNAYGPTETTVNASMVDMGGGRAGLPVLRPA 842
Cdd:PRK07638 235 MYTVPTMLESLYKENRVienKMKIISSGAKWEAEakeKIKNIFPYAKLY-EFYGASELSFVTALVDEESERRPNSVGRPF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 843 ANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAErfvPDPfatDGRAGVlyrtGDRAVLLADGRIHVSGRL 922
Cdd:PRK07638 314 HNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE---LNA---DGWMTV----RDVGYEDEEGFIYIVGRE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 923 DSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYavpqIDQDAATRptpsEIRAWLANRLPKFLVPDT 1002
Cdd:PRK07638 384 KNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAI----IKGSATKQ----QLKSFCLQRLSSFKIPKE 455
|
490
....*....|....*.
gi 796556827 1003 FDWLEALPLTMNGKID 1018
Cdd:PRK07638 456 WHFVDEIPYTNSGKIA 471
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
562-1022 |
4.06e-16 |
|
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: 82.62 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP----LDPEYPAERIgamlsDAGARLV 637
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRV-----DRGGAVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 638 VShssidlpktanrlnldedfpddesadnLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSG-----LINLTRDKIRACDV 712
Cdd:cd05974 76 AA---------------------------VDENTHADDPMLLYFTSGTTSKPKLVEHTHRSypvghLSTMYWIGLKPGDV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 713 ---------------------TADDCVLQFFSFSFDASipelvmslgagarllllpryatlpgAELADILRARhVTHLTM 771
Cdd:cd05974 129 hwnisspgwakhawscffapwNAGATVFLFNYARFDAK-------------------------RVLAALVRYG-VTTLCA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 772 TPSALLSLPVDDLLS----LRTVLVGGEVPMPELIER----WGKTRRfiNAYGPTETTVNAsmvdmgGGRAGLPVL---- 839
Cdd:cd05974 183 PPTVWRMLIQQDLASfdvkLREVVGAGEPLNPEVIEQvrraWGLTIR--DGYGQTETTALV------GNSPGQPVKagsm 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 840 -RPAANKQLYVLDdnlellPFGVP---GE--LHIGGC---GIARGYHDRAALTAErfvpdpfatdGRAGVLYRTGDRAVL 910
Cdd:cd05974 255 gRPLPGYRVALLD------PDGAPateGEvaLDLGDTrpvGLMKGYAGDPDKTAH----------AMRGGYYRTGDIAMR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 911 LADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDgrgGKRLaayAVPQ--IDQDAATRPTPS---E 985
Cdd:cd05974 319 DEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPD---PVRL---SVPKafIVLRAGYEPSPEtalE 392
|
490 500 510
....*....|....*....|....*....|....*..
gi 796556827 986 IRAWLANRLPKFLVPDTFDWLEaLPLTMNGKIDPLKL 1022
Cdd:cd05974 393 IFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVEL 428
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
776-1018 |
3.84e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 80.04 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 776 LLSLPVDDLLSLRTVLVGGEVPMPELIErwgKTRRF-IN---AYGPTETtvnASMV------DMGGGRAGLPVLRPAANK 845
Cdd:PRK07445 221 LLQLRPQWLAQFRTILLGGAPAWPSLLE---QARQLqLRlapTYGMTET---ASQIatlkpdDFLAGNNSSGQVLPHAQI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 846 QLYVLDDnlellpfgvpGELHIGGCGIARGYhdraaltaerfVPDPFATDGragvLYRTGDRAVLLADGRIHVSGRLDSQ 925
Cdd:PRK07445 295 TIPANQT----------GNITIQAQSLALGY-----------YPQILDSQG----IFETDDLGYLDAQGYLHILGRNSQK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 926 VKIRGYRIEPGEIEARLLahpaivsATVAVRD-------DGRGGKRLAAYAVPQidqdaATRPTPSEIRAWLANRLPKFL 998
Cdd:PRK07445 350 IITGGENVYPAEVEAAIL-------ATGLVQDvcvlglpDPHWGEVVTAIYVPK-----DPSISLEELKTAIKDQLSPFK 417
|
250 260
....*....|....*....|
gi 796556827 999 VPDTFDWLEALPLTMNGKID 1018
Cdd:PRK07445 418 QPKHWIPVPQLPRNPQGKIN 437
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
563-1022 |
4.59e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 80.18 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSS 642
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 I--DLPKTANRLNLDEDFPDDESADNLETVTHSSQLAY-----------------------VIYTSGSTGKAKGVLVDHS 697
Cdd:PRK06018 121 FvpILEKIADKLPSVERYVVLTDAAHMPQTTLKNAVAYeewiaeadgdfawktfdentaagMCYTSGTTGDPKGVLYSHR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 698 G-----LINLTRDkirACDVTADDCVLQF----------FSFSFDASIPELVMSLgagarllllpryATLPGAELADILR 762
Cdd:PRK06018 201 SnvlhaLMANNGD---ALGTSAADTMLPVvplfhanswgIAFSAPSMGTKLVMPG------------AKLDGASVYELLD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 763 ARHVTHLTMTPSALLSL------PVDDLLSLRTVLVGGEVpMPELIerwgkTRRF-------INAYGPTETTVNASMVDM 829
Cdd:PRK06018 266 TEKVTFTAGVPTVWLMLlqymekEGLKLPHLKMVVCGGSA-MPRSM-----IKAFedmgvevRHAWGMTEMSPLGTLAAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 830 GGGRAGLPVL----------RPAANKQLYVLDDNLELLPFG--VPGELHIGGCGIARGYH--DRAALTAERFvpdpfatd 895
Cdd:PRK06018 340 KPPFSKLPGDarldvlqkqgYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYrvDGEILDDDGF-------- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 896 gragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQ 975
Cdd:PRK06018 412 ------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGE 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 796556827 976 DaatrPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK06018 486 T----ATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
837-1110 |
6.49e-15 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 77.10 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 837 PVLRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDGRAGVLYRTGDRAVLLADGRI 916
Cdd:COG3433 17 PPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 917 HVSGRLDSQVKIRGYR-IEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAATRptpseirAWLANRLP 995
Cdd:COG3433 97 GGLERLVQQVVIRAERgEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAA-------LAALDKVP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 996 KFLVPDTFDWLEALPLTMNGKIDPLKLPAPRAETDPDGRAPEG----------EMEGRIAGAFGhvLNIDQVAATDDFFT 1065
Cdd:COG3433 170 PDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPApaletalteeELRADVAELLG--VDPEEIDPDDNLFD 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 796556827 1066 LGGHSLLATRFCAVAKdKFGLDIGVIDLFNASTVEALANRLRTRD 1110
Cdd:COG3433 248 LGLDSIRLMQLVERWR-KAGLDVSFADLAEHPTLAAWWALLAAAQ 291
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
563-972 |
7.70e-15 |
|
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: 79.49 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVShSS 642
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC-SK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 IDLPKTAN------------RLNLDEDFPDDESADNL----------------ETVTHSSQLAYVIYTSGSTGKAKGVLV 694
Cdd:cd17642 125 KGLQKVLNvqkklkiiktiiILDSKEDYKGYQCLYTFitqnlppgfneydfkpPSFDRDEQVALIMNSSGSTGLPKGVQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 695 DHSGLI---NLTRDKIRACDVTADDCVLQ----FFSFSFDASIPELVMSLgagarllllpRYATLPGAELADILRARH-- 765
Cdd:cd17642 205 THKNIVarfSHARDPIFGNQIIPDTAILTvipfHHGFGMFTTLGYLICGF----------RVVLMYKFEEELFLRSLQdy 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 766 -VTHLTMTPSALLSLP----VD--DLLSLRTVLVGGeVPMPELIERWGKTRRFIN----AYGPTETTVNASMVDMGGGRA 834
Cdd:cd17642 275 kVQSALLVPTLFAFFAkstlVDkyDLSNLHEIASGG-APLSKEVGEAVAKRFKLPgirqGYGLTETTSAILITPEGDDKP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 835 G-LPVLRPAANKQlyVLD-DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDpfatdgraGVLyRTGDRAVLLA 912
Cdd:cd17642 354 GaVGKVVPFFYAK--VVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKD--------GWL-HSGDIAYYDE 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 913 DGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQ 972
Cdd:cd17642 423 DGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE 482
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
544-1022 |
8.17e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 79.26 E-value: 8.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 544 RAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAylPLDPEY--- 620
Cdd:PRK10946 35 AASDAIAVI----CGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFshq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 621 ------------PAERIG----AMLSDAG--ARLVVSHSSIDLPKTANRlNLDEDFPD---DESADNLETVTHSSQLAYV 679
Cdd:PRK10946 109 rselnayasqiePALLIAdrqhALFSDDDflNTLVAEHSSLRVVLLLND-DGEHSLDDainHPAEDFTATPSPADEVAFF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 680 IYTSGSTGKAKgvlvdhsgLINLTRD----KIRA----CDVTADD---CVLQFfSFSFDASIP----------ELVMslg 738
Cdd:PRK10946 188 QLSGGSTGTPK--------LIPRTHNdyyySVRRsveiCGFTPQTrylCALPA-AHNYPMSSPgalgvflaggTVVL--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 739 agarllllpryATLPGAELADILRARH-VTHLTMTPSAL--------LSLPVDDLLSLRTVLVGGeVPMPElierwgKTR 809
Cdd:PRK10946 256 -----------APDPSATLCFPLIEKHqVNVTALVPPAVslwlqaiaEGGSRAQLASLKLLQVGG-ARLSE------TLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 810 RFINA---------YGPTETTVNASMVDMGGGR----AGLPVlrpAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGY 876
Cdd:PRK10946 318 RRIPAelgcqlqqvFGMAEGLVNYTRLDDSDERifttQGRPM---SPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 877 HDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVR 956
Cdd:PRK10946 395 YKSPQHNASAFDANGF---------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSM 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 957 DDGRGGKRLAAYAVpqidqdaATRP-TPSEIRAWLANR-LPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK10946 466 EDELMGEKSCAFLV-------VKEPlKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
549-1017 |
1.84e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 78.07 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 549 AALIMPQADA----DDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAER 624
Cdd:PRK08162 27 AAEVYPDRPAvihgDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAAS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 625 IGAMLSDAGARLV--------VSHSSIDLPKTANRLNLDEDFPDDESADNLETVTHSSQLAY------------------ 678
Cdd:PRK08162 107 IAFMLRHGEAKVLivdtefaeVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAFLASgdpdfawtlpadewdaia 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 679 VIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVL----QF------FSFSFDASI----------PELVMslg 738
Cdd:PRK08162 187 LNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLwtlpMFhcngwcFPWTVAARAgtnvclrkvdPKLIF--- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 739 agarllllpryatlpgaelaDILRARHVTHLTMTP---SALLSLPVDDLLSLR---TVLVGGEVPMPELIErwGKTRRFI 812
Cdd:PRK08162 264 --------------------DLIREHGVTHYCGAPivlSALINAPAEWRAGIDhpvHAMVAGAAPPAAVIA--KMEEIGF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 813 N---AYGPTETTVNASMVDMGGGRAGLPVLRPAANK-----------QLYVLD-DNLELlpfgVP------GELHIGGCG 871
Cdd:PRK08162 322 DlthVYGLTETYGPATVCAWQPEWDALPLDERAQLKarqgvryplqeGVTVLDpDTMQP----VPadgetiGEIMFRGNI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 872 IARGYHDRAALTAERFvpdpfatdgrAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSA 951
Cdd:PRK08162 398 VMKGYLKNPKATEEAF----------AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVA 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 796556827 952 TVAVRDDGRGGKRLAAYavpqIDQDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEaLPLTMNGKI 1017
Cdd:PRK08162 468 AVVAKPDPKWGEVPCAF----VELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKI 528
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
541-1017 |
2.26e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALIMpqADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEY 620
Cdd:PRK13390 6 HAQIAPDRPAVIV--AETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 621 PAERIGAMLSDAGARLVVSHSSID--LPKTANRLNLD-------EDFPDDES--ADNLETVTHSSQLAYVIYTSGSTGKA 689
Cdd:PRK13390 84 TAPEADYIVGDSGARVLVASAALDglAAKVGADLPLRlsfggeiDGFGSFEAalAGAGPRLTEQPCGAVMLYSSGTTGFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 690 KGVLVDHSGL-INLTRDKIRAC-----DVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATlpGAELADILRA 763
Cdd:PRK13390 164 KGIQPDLPGRdVDAPGDPIVAIarafyDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDA--QATLGHVERY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 764 RhVTHLTMTPSA---LLSLPVD-----DLLSLRTVlVGGEVPMPELIErwgktRRFINAYGP------TETTVNA-SMVD 828
Cdd:PRK13390 242 R-ITVTQMVPTMfvrLLKLDADvrtryDVSSLRAV-IHAAAPCPVDVK-----HAMIDWLGPivyeyySSTEAHGmTFID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 829 MGG-----GRAGLPVLrpaanKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVP-DPFATDgragvly 902
Cdd:PRK13390 315 SPDwlahpGSVGRSVL-----GDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPaHPFWTT------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 903 rTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYavpqIDQDAATRPT 982
Cdd:PRK13390 383 -VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAV----IQLVEGIRGS 457
|
490 500 510
....*....|....*....|....*....|....*...
gi 796556827 983 PS---EIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK13390 458 DElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
563-1012 |
2.55e-14 |
|
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: 77.40 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVshss 642
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 idlpktanrlnldedfpddesADNletvtHSSQLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVL--- 719
Cdd:cd17640 83 ---------------------VEN-----DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLsil 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 ----------QFFSFSFDASIpelvmslgagarllllpRYATLPgAELADILRARhvthltmtPSALLSLP--------- 780
Cdd:cd17640 137 piwhsyersaEYFIFACGCSQ-----------------AYTSIR-TLKDDLKRVK--------PHYIVSVPrlweslysg 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 781 VDDLLS---------LRTVLVGGEV--------PMPELIERWGKTR--RFINAYGPTETTVNASMvdmggGRAGLPVL-- 839
Cdd:cd17640 191 IQKQVSksspikqflFLFFLSGGIFkfgisgggALPPHVDTFFEAIgiEVLNGYGLTETSPVVSA-----RRLKCNVRgs 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 840 --RPAANKQLYVLD-DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRI 916
Cdd:cd17640 266 vgRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW---------FNTGDLGWLTCGGEL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 917 HVSGRL-DSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDgrggKRLAAYAVPQIDqdaatrptpsEIRAWLANRLP 995
Cdd:cd17640 337 VLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ----KRLGALIVPNFE----------ELEKWAKESGV 402
|
490
....*....|....*..
gi 796556827 996 KFLvPDTFDWLEALPLT 1012
Cdd:cd17640 403 KLA-NDRSQLLASKKVL 418
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
538-705 |
3.50e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 77.61 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 538 FEAHVARAPQAAALImpqaDADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGA----- 612
Cdd:PRK08279 43 FEEAAARHPDRPALL----FEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVvalln 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 613 ------------------YLPLDPEYpAERIGAMLSD-AGARLVVSHSSIDLPKTANRLNLD---EDFPDDESADNlETV 670
Cdd:PRK08279 119 tqqrgavlahslnlvdakHLIVGEEL-VEAFEEARADlARPPRLWVAGGDTLDDPEGYEDLAaaaAGAPTTNPASR-SGV 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 796556827 671 ThSSQLAYVIYTSGSTGKAKGVLVDH----------SGLINLTRD 705
Cdd:PRK08279 197 T-AKDTAFYIYTSGTTGLPKAAVMSHmrwlkamggfGGLLRLTPD 240
|
|
| SDR_e |
cd08946 |
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ... |
1146-1400 |
5.33e-14 |
|
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 212494 [Multi-domain] Cd Length: 200 Bit Score: 72.33 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPERkvtclVRGDDgmsrlrqafrqydlpqsvltervtivtgelskpglglaaadydniv 1225
Cdd:cd08946 1 ILVTGGAGFIGSHLVRRLLERGHE-----VVVID---------------------------------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 rNADCIFHNGAEVHHLHRY---ERLRETNVLGIREILQLACAGEGRHVHYISTlSALTPrrgsGGDPRPVCELESVEGFV 1302
Cdd:cd08946 30 -RLDVVVHLAALVGVPASWdnpDEDFETNVVGTLNLLEAARKAGVKRFVYASS-ASVYG----SPEGLPEEEETPPRPLS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1303 PpaggYNRSKWVAEHLVNEAGRR-GLPVTIYRPGAISGDSVTGAFNG--SDILCRLVQA---YLYTGtapeGERLLDMLP 1376
Cdd:cd08946 104 P----YGVSKLAAEHLLRSYGESyGLPVVILRLANVYGPGQRPRLDGvvNDFIRRALEGkplTVFGG----GNQTRDFIH 175
|
250 260
....*....|....*....|....
gi 796556827 1377 VDHVARAIVHLSGKPASAGQVFHL 1400
Cdd:cd08946 176 VDDVVRAILHALENPLEGGGVYNI 199
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
107-392 |
6.52e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.69 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 107 LEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFSVVEISPAAAAMEDVIHaETSRPFDLAAEPP 186
Cdd:PRK12316 1127 LQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCE-EAQRSLDLEQGPL 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 187 IRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYsaevsgnATPEAELPIQYGDFAAWQR--ERLATEIAGTLD 264
Cdd:PRK12316 1206 LRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAY-------ADLDADLPARTSSYQAWARrlHEHAGARAEELD 1278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 265 aFWKQHLSQPRQTtqLVTDMARTAGHGHAGELHDFTIEKE-TADALRKIAAAHGTTLFTALFTAFNLLIHRYTGQTDLVI 343
Cdd:PRK12316 1279 -YWQAQLEDAPHE--LPCENPDGALENRHERKLELRLDAErTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLV 1355
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 796556827 344 GTPVASRPHI-ETEDL---VGLFVNPLPVRslVDPFGNFEKALRETHATLRQV 392
Cdd:PRK12316 1356 QLEGHGREDLfEDIDLsrtVGWFTSLFPVR--LTPAADLGESIKAIKEQLRAV 1406
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
536-1017 |
8.68e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.07 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALimpqADADDIMTYGELNARANRLAR-LLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYL 614
Cdd:PRK08751 29 EVFATSVAKFADRPAY----HSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 615 PLDPEYPAERIGAMLSDAGARLVVSHSS-------------------------IDLPKTA---------------NRLNL 654
Cdd:PRK08751 105 NVNPLYTPRELKHQLIDSGASVLVVIDNfgttvqqviadtpvkqvittglgdmLGFPKAAlvnfvvkyvkklvpeYRING 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 655 DEDFPDDESADNLETVT----HSSQLAYVIYTSGSTGKAKGVLVDHSGLI-NL--------TRDKIRACDVTADDCVLQF 721
Cdd:PRK08751 185 AIRFREALALGRKHSMPtlqiEPDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMqqahqwlaGTGKLEEGCEVVITALPLY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 722 FSFSFDASipELV-MSLGAGARLLLLPRyaTLPG--AELADIlRARHVTHLTMTPSALLSLPVDDLL---SLRTVLVGGE 795
Cdd:PRK08751 265 HIFALTAN--GLVfMKIGGCNHLISNPR--DMPGfvKELKKT-RFTAFTGVNTLFNGLLNTPGFDQIdfsSLKMTLGGGM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 796 VPMPELIERWGKTR--RFINAYGPTETTVNASMVDMG----GGRAGLPVlrPAANkqLYVLDDNLELLPFGVPGELHIGG 869
Cdd:PRK08751 340 AVQRSVAERWKQVTglTLVEAYGLTETSPAACINPLTlkeyNGSIGLPI--PSTD--ACIKDDAGTVLAIGEIGELCIKG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 870 CGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIV 949
Cdd:PRK08751 416 PQVMKGYWKRPEETAKVMDADGW---------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 796556827 950 S-ATVAVRDDGRGgkrlAAYAVPQIDQDAATrpTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK08751 487 EvAAVGVPDEKSG----EIVKVVIVKKDPAL--TAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKI 549
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
559-1000 |
1.92e-13 |
|
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: 74.31 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 559 DDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVV 638
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 639 shssIDlpktanrlnldedfpddesadnletvthssqLAYVIYTSGSTGKAKGVLVDHSGLINLTRdkiracdvtaddcv 718
Cdd:cd05940 81 ----VD-------------------------------AALYIYTSGTTGLPKAAIISHRRAWRGGA-------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 719 lqFFSFSFDAsIPELVMslgagarllllprYATLP-----------------GAELA-----------DILRARHVT--- 767
Cdd:cd05940 112 --FFAGSGGA-LPSDVL-------------YTCLPlyhstalivgwsaclasGATLVirkkfsasnfwDDIRKYQATifq 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 768 -------HLTMTPSAllslPVDDLLSLRTVLVGGEVPmpeliERWGK-TRRF-----INAYGPTETT---VNASMVDMGG 831
Cdd:cd05940 176 yigelcrYLLNQPPK----PTERKHKVRMIFGNGLRP-----DIWEEfKERFgvpriAEFYAATEGNsgfINFFGKPGAI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 832 GRAGlPVLRPAANKQLYVLD-DNLELL----------PFGVPGEL--HIGGCGIARGYHDRAAlTAERFVPDPFAtDGRA 898
Cdd:cd05940 247 GRNP-SLLRKVAPLALVKYDlESGEPIrdaegrcikvPRGEPGLLisRINPLEPFDGYTDPAA-TEKKILRDVFK-KGDA 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 899 gvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATV-AV---RDDGRGGkrLAAYAVPqid 974
Cdd:cd05940 324 --WFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVyGVqvpGTDGRAG--MAAIVLQ--- 396
|
490 500
....*....|....*....|....*.
gi 796556827 975 qdAATRPTPSEIRAWLANRLPKFLVP 1000
Cdd:cd05940 397 --PNEEFDLSALAAHLEKNLPGYARP 420
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
536-1017 |
2.38e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 74.67 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 536 ELFEAHVARAPQAAALI-MPQAdaddiMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYL 614
Cdd:PRK07059 27 DLLEESFRQYADRPAFIcMGKA-----ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 615 PLDPEYPAERIGAMLSDAGARLVV------SHSSIDLPKTANR-----------------LNL----------------D 655
Cdd:PRK07059 102 NVNPLYTPRELEHQLKDSGAEAIVvlenfaTTVQQVLAKTAVKhvvvasmgdllgfkghiVNFvvrrvkkmvpawslpgH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 656 EDFPDDESAD---NLETVTHS-SQLAYVIYTSGSTGKAKGVLVDHSGLI----------NLTRDKIRACDVTADDCVL-- 719
Cdd:PRK07059 182 VRFNDALAEGarqTFKPVKLGpDDVAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawlQPAFEKKPRPDQLNFVCALpl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 -QFFSFSFDASipeLVMSLGAGARLLLLPRyaTLPG--AELAdilraRHVTHltMTPS------ALLSLPvD----DLLS 786
Cdd:PRK07059 262 yHIFALTVCGL---LGMRTGGRNILIPNPR--DIPGfiKELK-----KYQVH--IFPAvntlynALLNNP-DfdklDFSK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 787 LRTVLVGGEVPMPELIERWGKTRR--FINAYGPTET----TVNASMVDMGGGRAGLPVlrPAAnkQLYVLDDNLELLPFG 860
Cdd:PRK07059 329 LIVANGGGMAVQRPVAERWLEMTGcpITEGYGLSETspvaTCNPVDATEFSGTIGLPL--PST--EVSIRDDDGNDLPLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 861 VPGELHIGGCGIARGYHDRAALTAERFVPDPFatdgragvlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEA 940
Cdd:PRK07059 405 EPGEICIRGPQVMAGYWNRPDETAKVMTADGF---------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 941 RLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQiDQDAatrpTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK07059 476 VVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK-DPAL----TEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKI 547
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
937-1016 |
1.12e-12 |
|
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: 64.49 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 937 EIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPqidqDAATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGK 1016
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVL----KPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
574-1017 |
1.36e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.14 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 574 LARLLRRKGVSAETVVAISLPRSfDMIVAW-LAVWKAGGAYLPLDPEYPAERIG-AMLSDAGARLVVS---------HSS 642
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNS-DLYLEWlLAVACAGGIVAPLNYRWSFEEAKsAMLLVRPVMLVTDetcsswyeeLQN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 IDLPKTANRLNLDED----FPDDESADNLETVTH----SSQLAY---------VIYTSGSTGKAKGVLVDHSGLINLTRD 705
Cdd:PLN02860 124 DRLPSLMWQVFLESPsssvFIFLNSFLTTEMLKQralgTTELDYawapddavlICFTSGTTGRPKGVTISHSALIVQSLA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 706 KIRACDVTADDCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYAtlpgAELA-DILRARHVTHLTMTPSALLslpvdDL 784
Cdd:PLN02860 204 KIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFD----AKAAlQAIKQHNVTSMITVPAMMA-----DL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 785 LSL-------------RTVLVGGEVPMPELIERWGKT---RRFINAYGPTETTvnASMVDMGggragLPVLRPAANKQLY 848
Cdd:PLN02860 275 ISLtrksmtwkvfpsvRKILNGGGSLSSRLLPDAKKLfpnAKLFSAYGMTEAC--SSLTFMT-----LHDPTLESPKQTL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 849 VLDDNLELLPFGVPG-----------ELHIG-------GCGIARGYHdraalTAERFVPDPFATdgrAGVLYR-----TG 905
Cdd:PLN02860 348 QTVNQTKSSSVHQPQgvcvgkpaphvELKIGldessrvGRILTRGPH-----VMLGYWGQNSET---ASVLSNdgwldTG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 906 DRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYA----------VPQIDQ 975
Cdd:PLN02860 420 DIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwsdNEKENA 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 796556827 976 DAATRPTPSEIRAWLANR-LPKFLVPDTF-DWLEALPLTMNGKI 1017
Cdd:PLN02860 500 KKNLTLSSETLRHHCREKnLSRFKIPKLFvQWRKPFPLTTTGKI 543
|
|
| SDR_e_a |
cd05226 |
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ... |
1146-1340 |
1.36e-12 |
|
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187537 [Multi-domain] Cd Length: 176 Bit Score: 67.43 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDpERKVTCLVRGDDGMSRLRQafrqydlpqsvltERVTIVTGELSKPglglaaADYDNIV 1225
Cdd:cd05226 1 ILILGATGFIGRALARELLEQ-GHEVTLLVRNTKRLSKEDQ-------------EPVAVVEGDLRDL------DSLSDAV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNADCIFHNGAEVHHLHRYerlRETNVLGIREILQLACAGEGRHVHYISTLSALtprrgsgGDPRPvcelesvEGFVPPA 1305
Cdd:cd05226 61 QGVDVVIHLAGAPRDTRDF---CEVDVEGTRNVLEAAKEAGVKHFIFISSLGAY-------GDLHE-------ETEPSPS 123
|
170 180 190
....*....|....*....|....*....|....*
gi 796556827 1306 GGYNRSKWVAEHLVNEAgrrGLPVTIYRPGAISGD 1340
Cdd:cd05226 124 SPYLAVKAKTEAVLREA---SLPYTIVRPGVIYGD 155
|
|
| 3b-HSD-like_SDR_e |
cd05241 |
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ... |
1146-1412 |
8.51e-12 |
|
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187552 [Multi-domain] Cd Length: 331 Bit Score: 68.23 E-value: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPERKVTCLVRGDdgmsrLRQAFRQYDLPQsvlterVTIVTGELSkpglglaaaDYDNIV 1225
Cdd:cd05241 2 VLVTGGSGFFGERLVKQLLERGGTYVRSFDIAP-----PGEALSAWQHPN------IEFLKGDIT---------DRNDVE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RN---ADCIFHNGAEVHHLHRYERLRETNVLGIREILQlACAGEG-RHVHYISTLSAltprRGSGGDPRPVCELESVEGF 1301
Cdd:cd05241 62 QAlsgADCVFHTAAIVPLAGPRDLYWEVNVGGTQNVLD-ACQRCGvQKFVYTSSSSV----IFGGQNIHNGDETLPYPPL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1302 vpPAGGYNRSKWVAEHLVNEA-GRRGLPVTIYRPGAISGDSVTGAFNGSDILCRLVQAYLYTGtapEGERLLDMLPVDHV 1380
Cdd:cd05241 137 --DSDMYAETKAIAEIIVLEAnGRDDLLTCALRPAGIFGPGDQGLVPILFEWAEKGLVKFVFG---RGNNLVDFTYVHNL 211
|
250 260 270
....*....|....*....|....*....|....*..
gi 796556827 1381 ARAIV----HL-SGKPASaGQVFHLIHSSPVSSARLF 1412
Cdd:cd05241 212 AHAHIlaaaALvKGKTIS-GQTYFITDAEPHNMFELL 247
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
563-1017 |
8.94e-12 |
|
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: 69.38 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLR-RKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAylpldpeyPAeRIGAMLSDA--------- 632
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PA-FINYNLSGDplihclkls 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 633 GARLVVShssidlpktanrlnlDEDFPddesadnletvthssqlAYVIYTSGSTGKAKGVLVDhsglinlTRDKIRACDV 712
Cdd:cd05937 78 GSRFVIV---------------DPDDP-----------------AILIYTSGTTGLPKAAAIS-------WRRTLVTSNL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 713 TADDCVLQF----FS----FSFDASIPELVMSLGAGARLLLLPRYATLPGAELADILRARHVTHLTMTPSALLSLPV--- 781
Cdd:cd05937 119 LSHDLNLKNgdrtYTcmplYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPspy 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 782 DDLLSLRTVLVGGEVPmpeliERWGKTRRFINA------YGPTE---TTVNASMVDMGGGRAGL--PVLRPAANKQLYV- 849
Cdd:cd05937 199 DRDHKVRVAWGNGLRP-----DIWERFRERFNVpeigefYAATEgvfALTNHNVGDFGAGAIGHhgLIRRWKFENQVVLv 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 850 -LDDN------------LELLPFGVPGE----LHIGGCGIARGYHDRAALTAERFVPDPFatdgRAGVLY-RTGDRAVLL 911
Cdd:cd05937 274 kMDPEtddpirdpktgfCVRAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVF----RKGDIYfRTGDLLRQD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 912 ADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATV-AVR---DDGRGGkrlaaYAVPQIdQDAATRPTP---S 984
Cdd:cd05937 350 ADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVyGVKvpgHDGRAG-----CAAITL-EESSAVPTEftkS 423
|
490 500 510
....*....|....*....|....*....|...
gi 796556827 985 EIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05937 424 LLASLARKNLPSYAVPLFLRLTEEVATTDNHKQ 456
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
89-392 |
9.20e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.58 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 89 WLIDQIYPGSALHHICIALEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGVPKQTISAACDAPFsVVEISPAAAAME 168
Cdd:PRK05691 2800 WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQEL-LWQVTVADFAEC 2878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 169 DVIHAETSRPFDLAAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNATPEAELPIQYGDFA 248
Cdd:PRK05691 2879 AALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWA 2958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 249 AWQRERLATEIAGTLDAFWKQHLSQPRqtTQLVTDMARTAGHGHAGELHDFTIEKE-TADALRKIAAAHGTTLFTALFTA 327
Cdd:PRK05691 2959 ARLQAYAGSESLREELGWWQAQLGGPR--AELPCDRPQGGNLNRHAQTVSVRLDAErTRQLLQQAPAAYRTQVNDLLLTA 3036
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 796556827 328 FNLLIHRYTGQTDLVIGTPVASRPHIETE-DL---VGLFVNPLPVRSLVDPFGNFE-----KALREthaTLRQV 392
Cdd:PRK05691 3037 LARVLCRWSGQPSVLVQLEGHGREALFDDiDLtrsVGWFTSAYPLRLTPAPGDDAArgesiKAIKE---QLRAV 3107
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
559-1017 |
1.23e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 69.54 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 559 DDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVV 638
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 639 SHSSIdlpKTANRLNLDEDFPD---DESADNLETV----THSSQLA---------------------------------- 677
Cdd:PLN02654 198 TCNAV---KRGPKTINLKDIVDaalDESAKNGVSVgiclTYENQLAmkredtkwqegrdvwwqdvvpnyptkcevewvda 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 678 ----YVIYTSGSTGKAKGVLVDHSGLINLTRDKIR-ACDVTADD---CVLQ---FFSFSFDASIPelVMSLGAGARLLLL 746
Cdd:PLN02654 275 edplFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKyAFDYKPTDvywCTADcgwITGHSYVTYGP--MLNGATVLVFEGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 747 PRYATlPGaELADILRARHVTHLTMTPSALLSLPVDDL-----LSLRTVLVGGEVPMPELIERWgktRRFINAYGPTETT 821
Cdd:PLN02654 353 PNYPD-SG-RCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyvtrHSRKSLRVLGSVGEPINPSAW---RWFFNVVGDSRCP 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 822 VNAS--MVDMGG--------------GRAGLPVLrpaaNKQLYVLDDNLELLPFGVPGELHIGGC--GIAR---GYHDRA 880
Cdd:PLN02654 428 ISDTwwQTETGGfmitplpgawpqkpGSATFPFF----GVQPVIVDEKGKEIEGECSGYLCVKKSwpGAFRtlyGDHERY 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 881 ALTAERfvpdPFATdgragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGR 960
Cdd:PLN02654 504 ETTYFK----PFAG------YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEV 573
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 796556827 961 GGKRLAAYaVPQIDqdaaTRPTPSEIRAWLA----NRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PLN02654 574 KGQGIYAF-VTLVE----GVPYSEELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKI 629
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
563-1033 |
2.07e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 68.66 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRK-GVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPL-----------------------DP 618
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLnkqlmndqivhiinhaedevivaDP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 619 EYpAERIGAMLSD---AGARLVVSHSSIDLPKTANRLNLD----EDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKG 691
Cdd:PRK05620 120 RL-AEQLGEILKEcpcVRAVVFIGPSDADSAAAHMPEGIKvysyEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 692 VLVDHSGLInLTRDKIRACD---VTADD----CVLQFFSFS-------FDASIPeLVMSLgagarllllpryATLPGAEL 757
Cdd:PRK05620 199 VVYSHRSLY-LQSLSLRTTDslaVTHGEsflcCVPIYHVLSwgvplaaFMSGTP-LVFPG------------PDLSAPTL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 758 ADILRARHVTHLTMTPSALLSLPVDDL------LSLRTVLVGGEVPMPELIERWgkTRRF----INAYGPTETTVNASMV 827
Cdd:PRK05620 265 AKIIATAMPRVAHGVPTLWIQLMVHYLknpperMSLQEIYVGGSAVPPILIKAW--EERYgvdvVHVWGMTETSPVGTVA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 828 DMGGGRAGLPVLR--------PAANKQLYVLDDNLELLPFGVPGELHIGGCGI-ARGYHD---RAALTAERF-------V 888
Cdd:PRK05620 343 RPPSGVSGEARWAyrvsqgrfPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVtASYYHSpteEGGGAASTFrgedvedA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 889 PDPFATDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAY 968
Cdd:PRK05620 423 NDRFTADG----WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 969 AV--PQIDQdaaTRPTPSEIRAWLANRLPKFLVP--------------DTFDWLEALPLTMNGKIDPLKLPAPRAETDPD 1032
Cdd:PRK05620 499 TVlaPGIEP---TRETAERLRDQLRDRLPNWMLPeywtfvdeidktsvGKFDKKDLRQHLADGDFEIIKLKGPGESGESD 575
|
.
gi 796556827 1033 G 1033
Cdd:PRK05620 576 S 576
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
550-979 |
3.85e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 67.71 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 550 ALIMPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYP-------A 622
Cdd:PRK07768 18 GMVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPrtdlavwA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 623 ERIGAMLSDAGARLVVSHSSID-----LPKTANRLNLDEDFPDDESADNLETvtHSSQLAYVIYTSGSTGKAKGVLVDHS 697
Cdd:PRK07768 98 EDTLRVIGMIGAKAVVVGEPFLaaapvLEEKGIRVLTVADLLAADPIDPVET--GEDDLALMQLTSGSTGSPKAVQITHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 698 GLINLTRDKIRACDVTAD-DCVLQFFSFSFDasipelvMSLGAgarllllprYATLP---GAEL-----ADILR-----A 763
Cdd:PRK07768 176 NLYANAEAMFVAAEFDVEtDVMVSWLPLFHD-------MGMVG---------FLTVPmyfGAELvkvtpMDFLRdpllwA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 764 RHVTHL--TMTPS-----ALL-----SLPVD---DLLSLRTVLVGGEVPMPELIE-------RWG-KTRRFINAYGPTET 820
Cdd:PRK07768 240 ELISKYrgTMTAApnfayALLarrlrRQAKPgafDLSSLRFALNGAEPIDPADVEdlldagaRFGlRPEAILPAYGMAEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 821 TVNASMVDMGGG--------------RAGLPVLRPAANK-----------QLYVLDDNLELLPFGVPGELHIGGCGIARG 875
Cdd:PRK07768 320 TLAVSFSPCGAGlvvdevdadllaalRRAVPATKGNTRRlatlgpplpglEVRVVDEDGQVLPPRGVGVIELRGESVTPG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 876 YhdraaLTAERFVPdpfATDgrAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEaRLLAHPAIVSA--TV 953
Cdd:PRK07768 400 Y-----LTMDGFIP---AQD--ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE-RAAARVEGVRPgnAV 468
|
490 500
....*....|....*....|....*..
gi 796556827 954 AVR-DDGRGGKRLAAYAVPQIDQDAAT 979
Cdd:PRK07768 469 AVRlDAGHSREGFAVAVESNAFEDPAE 495
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
902-1018 |
5.38e-11 |
|
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: 65.89 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 902 YRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGkrlaAYAVPQIDQDAATRP 981
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFG----EIAVALYSGDKLTYK 285
|
90 100 110
....*....|....*....|....*....|....*..
gi 796556827 982 TpseIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd17633 286 Q---LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
755-1018 |
6.03e-11 |
|
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: 65.79 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 755 AELADILRARHVTHLTMTP---SALLSLPVD---DLLSLRTV--LVGGEVPMPELIERWGktrRFINAYGPTETTVNASM 826
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPptiDQIVELNADglyDLSSLRSSpaAPEWNDMATVDTSPWG---RKPGGYGQTEVMGLATF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 827 VDMGG---GRAGlpvlRPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFvpdpfatdgRAGvLYR 903
Cdd:cd17636 155 AALGGgaiGGAG----RPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT---------RGG-WHH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 904 TGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAatrpTP 983
Cdd:cd17636 221 TNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASV----TE 296
|
250 260 270
....*....|....*....|....*....|....*
gi 796556827 984 SEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:cd17636 297 AELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
541-960 |
8.67e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 66.46 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARA-PQAAALIMPQA-DAD-----DIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAY 613
Cdd:PRK09274 14 RAAQErPDQLAVAVPGGrGADgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 614 LPLDP-------------EYPAERIGAMLSDAGARL------------VVSHSSIDLPKTANRLNLDEDFPDDESADnle 668
Cdd:PRK09274 94 VLVDPgmgiknlkqclaeAQPDAFIGIPKAHLARRLfgwgkpsvrrlvTVGGRLLWGGTTLATLLRDGAAAPFPMAD--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 669 tvTHSSQLAYVIYTSGSTGKAKGVLVDHSGL---INLTRD--KIRACDVtaDDCVLQFFSFsFDAS------IPELVMSl 737
Cdd:PRK09274 171 --LAPDDMAAILFTSGSTGTPKGVVYTHGMFeaqIEALREdyGIEPGEI--DLPTFPLFAL-FGPAlgmtsvIPDMDPT- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 738 gagarllllpRYATLPGAELADILRARHVTHLTMTPsALL------------SLPvddllSLRTVLVGGE-VPmPELIER 804
Cdd:PRK09274 245 ----------RPATVDPAKLFAAIERYGVTNLFGSP-ALLerlgrygeangiKLP-----SLRRVISAGApVP-IAVIER 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 805 WGK----TRRFINAYGPTE--------------TTVNASmvDMGGGRAglpVLRPAANKQLYVL----------DDNLEL 856
Cdd:PRK09274 308 FRAmlppDAEILTPYGATEalpissiesreilfATRAAT--DNGAGIC---VGRPVDGVEVRIIaisdapipewDDALRL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 857 LPfGVPGELHIGGCGIARGYHDRAALTAERFVPDPfatdgRAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPG 936
Cdd:PRK09274 383 AT-GEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG-----QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTI 456
|
490 500
....*....|....*....|....*
gi 796556827 937 EIEARLLAHPAIV-SATVAVRDDGR 960
Cdd:PRK09274 457 PCERIFNTHPGVKrSALVGVGVPGA 481
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
562-955 |
8.88e-11 |
|
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: 65.94 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVvshs 641
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAF---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 sIDLPKTanrlnlDEDfpddesadnletvthssqlAYVIYTSGSTGKAKGVLVDHS---GLINLTRDK--IRACDVTADd 716
Cdd:cd05910 79 -IGIPKA------DEP-------------------AAILFTSGSTGTPKGVVYRHGtfaAQIDALRQLygIRPGEVDLA- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 717 CVLQFFSFSfdasiPELVMSLGAGARLLLLPryATLPGAELADILRARHVTHLTMTPSAL-----------LSLPvddll 785
Cdd:cd05910 132 TFPLFALFG-----PALGLTSVIPDMDPTRP--ARADPQKLVGAIRQYGVSIVFGSPALLervarycaqhgITLP----- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 786 SLRTVLVGGEVPMPELIERWGK----TRRFINAYGPTET---------TVNASMVDMGGGRAGLPVLRPAANKQLYVLD- 851
Cdd:cd05910 200 SLRRVLSAGAPVPIALAARLRKmlsdEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTCVGRPIPGVRVRIIEi 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 852 --------DNLELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPfatdgRAGVLYRTGDRAVLLADGRIHVSGRLD 923
Cdd:cd05910 280 ddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN-----SEGFWHRMGDLGYLDDEGRLWFCGRKA 354
|
410 420 430
....*....|....*....|....*....|...
gi 796556827 924 SQVKIRGYRIEPGEIEARLLAHPAIV-SATVAV 955
Cdd:cd05910 355 HRVITTGGTLYTEPVERVFNTHPGVRrSALVGV 387
|
|
| YbjT |
COG0702 |
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
1146-1400 |
9.74e-11 |
|
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];
Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 63.33 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPERkVTCLVRGDDGMSRLRQAfrqydlpqsvlteRVTIVTGELSKPGlGLAAAdydniV 1225
Cdd:COG0702 2 ILVTGATGFIGRRVVRALLARGHP-VRALVRDPEKAAALAAA-------------GVEVVQGDLDDPE-SLAAA-----L 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNADCIFHngaeVHHLHRYERLrETNVLGIREILQLAC-AGEGRHVHyistLSALTPRRGSGgdprpvcelesvegfvpp 1304
Cdd:COG0702 62 AGVDAVFL----LVPSGPGGDF-AVDVEGARNLADAAKaAGVKRIVY----LSALGADRDSP------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1305 aGGYNRSKWVAEHLVNEAgrrGLPVTIYRPGAISGdsvtgafNGSDILCRLVQAYLYtgTAPEGERLLDMLPVDHVARAI 1384
Cdd:COG0702 115 -SPYLRAKAAVEEALRAS---GLPYTILRPGWFMG-------NLLGFFERLRERGVL--PLPAGDGRVQPIAVRDVAEAA 181
|
250
....*....|....*.
gi 796556827 1385 VHLSGKPASAGQVFHL 1400
Cdd:COG0702 182 AAALTDPGHAGRTYEL 197
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
783-1017 |
1.20e-10 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 65.85 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 783 DLLSLRTVlVGGEVPMPELI-ERWGKT--RRFINAYGPTETT--VNASMVDMGG--GRAGLPVlrpaANKQLYVLDDNLE 855
Cdd:PRK08974 323 DFSSLKLS-VGGGMAVQQAVaERWVKLtgQYLLEGYGLTECSplVSVNPYDLDYysGSIGLPV----PSTEIKLVDDDGN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 856 LLPFGVPGELHIGGCGIARGYHDRAALTAErfvpdpFATDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEP 935
Cdd:PRK08974 398 EVPPGEPGELWVKGPQVMLGYWQRPEATDE------VIKDG----WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYP 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 936 GEIEARLLAHPAIV-SATVAVRDDGrGGKRLAAYAVPqidQDAATrpTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMN 1014
Cdd:PRK08974 468 NEIEDVVMLHPKVLeVAAVGVPSEV-SGEAVKIFVVK---KDPSL--TEEELITHCRRHLTGYKVPKLVEFRDELPKSNV 541
|
...
gi 796556827 1015 GKI 1017
Cdd:PRK08974 542 GKI 544
|
|
| NDUFA9_like_SDR_a |
cd05271 |
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ... |
1146-1400 |
1.95e-10 |
|
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187579 [Multi-domain] Cd Length: 273 Bit Score: 63.42 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRdPERKVTCLVRGDDGMSRLRQafrQYDLPQsvlterVTIVTGELSKPGLGLAAADYDNIV 1225
Cdd:cd05271 3 VTVFGATGFIGRYVVNRLAK-RGSQVIVPYRCEAYARRLLV---MGDLGQ------VLFVEFDLRDDESIRKALEGSDVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNadCIfhnGAEvhhlhrYER----LRETNVLGIREILQLAC-AGEGRHVHyistLSALtprrgsGGDPRPVCElesveg 1300
Cdd:cd05271 73 IN--LV---GRL------YETknfsFEDVHVEGPERLAKAAKeAGVERLIH----ISAL------GADANSPSK------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1301 fvppaggYNRSKWVAEHLVNEAGRrglPVTIYRPGAISGDsvtgafnGSDILCRLVQAYLYT---GTAPEGERLLDMLPV 1377
Cdd:cd05271 126 -------YLRSKAEGEEAVREAFP---EATIVRPSVVFGR-------EDRFLNRFAKLLAFLpfpPLIGGGQTKFQPVYV 188
|
250 260
....*....|....*....|...
gi 796556827 1378 DHVARAIVHLSGKPASAGQVFHL 1400
Cdd:cd05271 189 GDVAEAIARALKDPETEGKTYEL 211
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
541-1017 |
1.98e-10 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 65.36 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALIM--PQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAvwkaggaylpldp 618
Cdd:PRK10524 62 HLAKRPEQLALIAvsTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLA------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 619 eypAERIGAMLS--------------------------DAGAR-------------------------LVVSHSSIDLPK 647
Cdd:PRK10524 129 ---CARIGAIHSvvfggfashslaariddakpvlivsaDAGSRggkvvpykplldeaialaqhkprhvLLVDRGLAPMAR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 648 TANRlnlDEDFPD--DESADNLETVT--HSSQLAYVIYTSGSTGKAKGVLVDHSGL---INLTRDKI---RACDVtaddc 717
Cdd:PRK10524 206 VAGR---DVDYATlrAQHLGARVPVEwlESNEPSYILYTSGTTGKPKGVQRDTGGYavaLATSMDTIfggKAGET----- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 718 vlqFFS---------FSFDASIPEL-----VMslgagarllllprYATLP----GAELADILRARHVTHLTMTPSALLSL 779
Cdd:PRK10524 278 ---FFCasdigwvvgHSYIVYAPLLagmatIM-------------YEGLPtrpdAGIWWRIVEKYKVNRMFSAPTAIRVL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 780 ---PVD-----DLLSLRTVLVGGEvPMPELIERW---GKTRRFINAYGPTET----TVNASMVDMGGGRAGLPVlRPAAN 844
Cdd:PRK10524 342 kkqDPAllrkhDLSSLRALFLAGE-PLDEPTASWiseALGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPG-VPMYG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 845 KQLYVLDDNL-ELLPFGVPGELHIG-----GCgIARGYHDRaaltaERFVPDPFATDGRagVLYRTGDRAVLLADGRIHV 918
Cdd:PRK10524 420 YNVKLLNEVTgEPCGPNEKGVLVIEgplppGC-MQTVWGDD-----DRFVKTYWSLFGR--QVYSTFDWGIRDADGYYFI 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 919 SGRLDSQVKIRGYRIEPGEIEARLLAHPAIVS-ATVAVRDDGRGgkRLA-AYAVPQ----IDQDAATRPTPSEIRAWLAN 992
Cdd:PRK10524 492 LGRTDDVINVAGHRLGTREIEESISSHPAVAEvAVVGVKDALKG--QVAvAFVVPKdsdsLADREARLALEKEIMALVDS 569
|
570 580
....*....|....*....|....*
gi 796556827 993 RLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK10524 570 QLGAVARPARVWFVSALPKTRSGKL 594
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
541-1017 |
2.31e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 65.16 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 541 HVARAPQAAALIM---PQADADDImTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAG------- 610
Cdd:PRK00174 76 HLKTRGDKVAIIWegdDPGDSRKI-TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvf 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 611 GAYlplDPEYPAERI---GAML---SDAGAR------------------------LVVSHSSIDLPKTANRlnlD---ED 657
Cdd:PRK00174 155 GGF---SAEALADRIidaGAKLvitADEGVRggkpiplkanvdealancpsvekvIVVRRTGGDVDWVEGR---DlwwHE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 658 FPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLvdHS------GLINLTR---DkIRACDV---TAD---------- 715
Cdd:PRK00174 229 LVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVL--HTtggylvYAAMTMKyvfD-YKDGDVywcTADvgwvtghsyi 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 716 --------DCVLQFfsfsfdasipELVmslgagarllllPRYATlPGaELADILrARH-VTHLTMTPSALLSL------P 780
Cdd:PRK00174 306 vygplangATTLMF----------EGV------------PNYPD-PG-RFWEVI-DKHkVTIFYTAPTAIRALmkegdeH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 781 VD--DLLSLRtvLVG--GEVPMPELIErW-----GKTR-RFINAYGPTETtvNASM-------VDMGGGRAGLPV--LRP 841
Cdd:PRK00174 361 PKkyDLSSLR--LLGsvGEPINPEAWE-WyykvvGGERcPIVDTWWQTET--GGIMitplpgaTPLKPGSATRPLpgIQP 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 842 AankqlyVLDDNLELLPFGVPGELHIGGC--GIARG-YHDRaaltaERFVPDPFATDgrAGVlYRTGDRAVLLADGRIHV 918
Cdd:PRK00174 436 A------VVDEEGNPLEGGEGGNLVIKDPwpGMMRTiYGDH-----ERFVKTYFSTF--KGM-YFTGDGARRDEDGYYWI 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 919 SGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQidqdAATRPTP---SEIRAWLANRLP 995
Cdd:PRK00174 502 TGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLK----GGEEPSDelrKELRNWVRKEIG 577
|
570 580
....*....|....*....|..
gi 796556827 996 KFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK00174 578 PIAKPDVIQFAPGLPKTRSGKI 599
|
|
| UDP_G4E_3_SDR_e |
cd05240 |
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ... |
1146-1347 |
4.31e-10 |
|
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187551 [Multi-domain] Cd Length: 306 Bit Score: 62.77 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPErkvtclVRGDDGMSRlrqafRQYDLPQsvltERVTIVTGELSKPglglaAADYDNIV 1225
Cdd:cd05240 1 ILVTGAAGGLGRLLARRLAASPR------VIGVDGLDR-----RRPPGSP----PKVEYVRLDIRDP-----AAADVFRE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNADCIFHNGAEVHHLHRYERLRETNVLGIREILqLACAGEG-RHVHYISTLSALtprrGSGGDpRPVCELESVEGFVPP 1304
Cdd:cd05240 61 READAVVHLAFILDPPRDGAERHRINVDGTQNVL-DACAAAGvPRVVVTSSVAVY----GAHPD-NPAPLTEDAPLRGSP 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 796556827 1305 AGGYNRSKWVAEHLVNEAGRR--GLPVTIYRPGAISGDSVTGAFN 1347
Cdd:cd05240 135 EFAYSRDKAEVEQLLAEFRRRhpELNVTVLRPATILGPGTRNTTR 179
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
107-369 |
5.37e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.80 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 107 LEVRGALDLDALKVALAGVMSRHTVLRARIYSDKGvpkqTISAACDAPFSVVE-----ISPAAAAMEDVIHAETSRPFDL 181
Cdd:PRK12467 2207 LEPREALDAELLEAALQALLVHHDALRLGFVQEDG----GWSAMHRAPEQERRpllwqVVVADKEELEALCEQAQRSLDL 2282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 182 AAEPPIRLLVAKCDDGHHVLVFTLHHICADGWSTEILLKDLGAFYSAEVSGNATpeaELPIQYGDFAAWQrERLAT---- 257
Cdd:PRK12467 2283 EEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPV---KLPAKTSAFKAWA-ERLQTyaas 2358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 258 -EIAGTLDaFWKQHLSQprQTTQLVTDMaRTAGHGHAGELHDFT-IEKE-TADALRKIAAAHGTTLFTALFTAFNLLIHR 334
Cdd:PRK12467 2359 aALADELG-YWQAQLQG--ASTELPCDH-PQGGLQRRHAASVTThLDSEwTRRLLQEAPAAYRTQVNDLLLTALARVIAR 2434
|
250 260 270
....*....|....*....|....*....|....*....
gi 796556827 335 YTGQTDLVIGTPVASRPHI-ETEDL---VGLFVNPLPVR 369
Cdd:PRK12467 2435 WTGQASTLIQLEGHGREDLfDEIDLtrtVGWFTSLYPVK 2473
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
903-1017 |
5.39e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.52 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 903 RTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVpqidqdAATRPT 982
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI------SHEEID 367
|
90 100 110
....*....|....*....|....*....|....*
gi 796556827 983 PSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK08308 368 PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| TubC_N |
pfam18563 |
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ... |
7-56 |
6.03e-10 |
|
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins from the tubulysin polyketide synthase and nonribosomal polypeptide synthetase (PKS-NRPS) system, which binds to C-terminal docking domain of TubB.
Pssm-ID: 436580 [Multi-domain] Cd Length: 52 Bit Score: 55.99 E-value: 6.03e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 796556827 7 VETLITRLHQNNIRVWIDAGSLKCSDPDGHLNDAVMSEIRTRKTDILAFL 56
Cdd:pfam18563 1 IVELLAELYALGIKLWLEGGRLRFRAPKGVLTPELREKLKERKAEIIAFL 50
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
556-700 |
1.13e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 63.04 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 556 ADADDIMTYGELNARANRLARLLRRKGVSAETVVaISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPA---ERIGAMLSDA 632
Cdd:PRK05850 30 AGVAETLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGahdERVSAVLRDT 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 633 GARLVVSHSSI--DLPKTANRLNLDE-------DFPDDESADNLETVTHS-SQLAYVIYTSGSTGKAKGVLVDHSGLI 700
Cdd:PRK05850 109 SPSVVLTTSAVvdDVTEYVAPQPGQSappvievDLLDLDSPRGSDARPRDlPSTAYLQYTSGSTRTPAGVMVSHRNVI 186
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
1146-1398 |
1.54e-09 |
|
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 60.00 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPERKVtclvrgddGMSRLRQAFRqydlpqSVLTERVTIVTGELSkpglglaaaDYDNIV 1225
Cdd:pfam01370 1 ILVTGATGFIGSHLVRRLLEKGYEVI--------GLDRLTSASN------TARLADLRFVEGDLT---------DRDALE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 R-----NADCIFHNGAEVHHLHRYERLRET---NVLGIREILQLACAGEGRHVHYISTlSALTPRrgsgGDPRPVcELES 1297
Cdd:pfam01370 58 KlladvRPDAVIHLAAVGGVGASIEDPEDFieaNVLGTLNLLEAARKAGVKRFLFASS-SEVYGD----GAEIPQ-EETT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1298 VEGFVPPAGGYNRSKWVAEHLVNEAGRR-GLPVTIYRPGaisgdSVTGAFNGSDILCRLVQAYLYTGTAPEGERLL---- 1372
Cdd:pfam01370 132 LTGPLAPNSPYAAAKLAGEWLVLAYAAAyGLRAVILRLF-----NVYGPGDNEGFVSRVIPALIRRILEGKPILLWgdgt 206
|
250 260
....*....|....*....|....*....
gi 796556827 1373 ---DMLPVDHVARAIVHLSGKPASAGQVF 1398
Cdd:pfam01370 207 qrrDFLYVDDVARAILLALEHGAVKGEIY 235
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1035-1109 |
2.14e-09 |
|
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: 55.63 E-value: 2.14e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 1035 APEGEMEGRIAGAFGHVLNID--QVAATDDFFT-LGGHSLLATRFCAVAKDKFGLDIGVIDLFNASTVEALANRLRTR 1109
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| CDP_TE_SDR_e |
cd05258 |
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ... |
1146-1430 |
2.41e-09 |
|
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187568 [Multi-domain] Cd Length: 337 Bit Score: 60.77 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPERkvtclVRGDDGMSRlRQAFRQ-YDLPQSVLTERVTIVTGELSKPglglaaADYDNI 1224
Cdd:cd05258 3 VLITGGAGFIGSNLARFFLKQGWE-----VIGFDNLMR-RGSFGNlAWLKANREDGGVRFVHGDIRNR------NDLEDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1225 VRNADCIFHNGAEVHHLHRYERLR---ETNVLGIREILQLA---CAG--------------EGRHVHYISTLSALTPRRG 1284
Cdd:cd05258 71 FEDIDLIIHTAAQPSVTTSASSPRldfETNALGTLNVLEAArqhAPNapfiftstnkvygdLPNYLPLEELETRYELAPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1285 sGGDPRPVCELESVEGFVPPaggYNRSKWVAEHLVNEAGRR-GLPVTIYRPGAISGDSvtgAFNGSD--ILCRLVQA--- 1358
Cdd:cd05258 151 -GWSPAGISESFPLDFSHSL---YGASKGAADQYVQEYGRIfGLKTVVFRCGCLTGPR---QFGTEDqgWVAYFLKCavt 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1359 ---YLYTGTApeGERLLDMLPVDHVARAIVHLSGKPAS-AGQVFHL---IHSSpVSSARLFEACE-LEGIELkRVSQREW 1430
Cdd:cd05258 224 gkpLTIFGYG--GKQVRDVLHSADLVNLYLRQFQNPDRrKGEVFNIgggRENS-VSLLELIALCEeITGRKM-ESYKDEN 299
|
|
| SDR_a1 |
cd05265 |
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ... |
1150-1425 |
5.11e-09 |
|
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187575 [Multi-domain] Cd Length: 250 Bit Score: 58.84 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1150 GATGFLGTYLLHELL-RDPErkVTCLVRGDdgmsrlrqafRQYDLPqsvltERVTIVTGELSKP-GL--GLAAADYDNIV 1225
Cdd:cd05265 7 GGTRFIGKALVEELLaAGHD--VTVFNRGR----------TKPDLP-----EGVEHIVGDRNDRdALeeLLGGEDFDVVV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 rnaDCIFHNGAEVhhlhryERLREtnvlgireilqlACAGEGRHVHYISTLSALTPRRGSGGDPRPVCELESVEGFVPpa 1305
Cdd:cd05265 70 ---DTIAYTPRQV------ERALD------------AFKGRVKQYIFISSASVYLKPGRVITESTPLREPDAVGLSDP-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1306 GGYNRSKWVAEHLVNEAGrrGLPVTIYRPGAISG-DSVTGAF--------NGSDILcrlvqaylytgtAP-EGERLLDML 1375
Cdd:cd05265 127 WDYGRGKRAAEDVLIEAA--AFPYTIVRPPYIYGpGDYTGRLayffdrlaRGRPIL------------VPgDGHSLVQFI 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 796556827 1376 PVDHVARAIVHLSGKPASAGQVFHLIHSSPVSSARLFEAC-ELEGIELKRV 1425
Cdd:cd05265 193 HVKDLARALLGAAGNPKAIGGIFNITGDEAVTWDELLEACaKALGKEAEIV 243
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
675-939 |
5.21e-09 |
|
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: 60.58 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 675 QLAYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFSFDASIPELVMSlgagarllllPRYAT--- 751
Cdd:cd05908 107 ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLA----------PLIAGmnq 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 752 --LPGAELadILR--------ARHVTHLTMTPSALLSLPVD----------DLLSLRTVLVGGEVPMPELIE-------R 804
Cdd:cd05908 177 ylMPTRLF--IRRpilwlkkaSEHKATIVSSPNFGYKYFLKtlkpekandwDLSSIRMILNGAEPIDYELCHefldhmsK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 805 WGKTRRFI-NAYGPTETTVNASMVDMGG-------GRAG--------------------LPVLRPAANKQLYVLDDNLEL 856
Cdd:cd05908 255 YGLKRNAIlPVYGLAEASVGASLPKAQSpfktitlGRRHvthgepepevdkkdsecltfVEVGKPIDETDIRICDEDNKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 857 LPFGVPGELHIGGCGIARGYHDRAALTAERFVPDpfatdgraGVLyRTGDRAvLLADGRIHVSGRLDSQVKIRGYRIEPG 936
Cdd:cd05908 335 LPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDD--------GWL-KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPH 404
|
...
gi 796556827 937 EIE 939
Cdd:cd05908 405 DIE 407
|
|
| AR_like_SDR_e |
cd05193 |
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ... |
1146-1352 |
6.19e-09 |
|
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187536 [Multi-domain] Cd Length: 295 Bit Score: 59.17 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLrdpER--KVTCLVRgdDGmSRLRQAFRQYDLPQsvLTERVTIVTGELSKPGlglaaaDYDN 1223
Cdd:cd05193 1 VLVTGASGFVASHVVEQLL---ERgyKVRATVR--DP-SKVKKVNHLLDLDA--KPGRLELAVADLTDEQ------SFDE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1224 IVRNADCIFHNGAEVHHLHRY-ERLRETNVLGIREILQlACAGEG---RHVHYISTLSALTP---RRGSGGDPRPVCELE 1296
Cdd:cd05193 67 VIKGCAGVFHVATPVSFSSKDpNEVIKPAIGGTLNALK-AAAAAKsvkRFVLTSSAGSVLIPkpnVEGIVLDEKSWNLEE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 796556827 1297 SVEGFVPPAGGYNRSKWVAEHLVNE-AGRRGLPVTIYRPGAISGDSVTGAFNGSDIL 1352
Cdd:cd05193 146 FDSDPKKSAWVYAASKTLAEKAAWKfADENNIDLITVIPTLTIGTIFDSETPSSSGW 202
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
563-1022 |
7.92e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 60.03 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIGAMLSDAGARLVVSHSS 642
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 643 ID---------LPKTANRLNL------DEDFPDDESADNL---------ETVTHSSQLAYVI----------YTSGSTGK 688
Cdd:PLN03102 121 FEplarevlhlLSSEDSNLNLpvifihEIDFPKRPSSEELdyecliqrgEPTPSLVARMFRIqdehdpislnYTSGTTAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 689 AKGVLVDHSGLINLTRDKIRACDVTAddCVLQFFSFS-FDASIPELVMSLGAGARLLLLPRYATLPgaELADILRARHVT 767
Cdd:PLN03102 201 PKGVVISHRGAYLSTLSAIIGWEMGT--CPVYLWTLPmFHCNGWTFTWGTAARGGTSVCMRHVTAP--EIYKNIEMHNVT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 768 HLTMTPSALLSLPVDDLLSLR------TVLVGGEVPMPELI---ERWGktRRFINAYGPTETTVNASMVDMGGGRAGLP- 837
Cdd:PLN03102 277 HMCCVPTVFNILLKGNSLDLSprsgpvHVLTGGSPPPAALVkkvQRLG--FQVMHAYGLTEATGPVLFCEWQDEWNRLPe 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 838 ----VLRPAANKQLYVLDD----NLELLPfGVP------GELHIGGCGIARGYHDRAALTAERFvpdpfatdgRAGVLyR 903
Cdd:PLN03102 355 nqqmELKARQGVSILGLADvdvkNKETQE-SVPrdgktmGEIVIKGSSIMKGYLKNPKATSEAF---------KHGWL-N 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 904 TGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQ------IDQDA 977
Cdd:PLN03102 424 TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEkgettkEDRVD 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 796556827 978 ATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PLN03102 504 KLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
863-1031 |
8.29e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 60.24 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 863 GELHIGGCGIARGYHDRAALTAERFvpdpfatdgrAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARL 942
Cdd:PLN02479 403 GEIVMRGNMVMKGYLKNPKANEEAF----------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 943 LAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAATRP-TPSEIRAWLANRLPKFLVPDTFDWlEALPLTMNGKIDPLK 1021
Cdd:PLN02479 473 YTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAaLAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHV 551
|
170
....*....|
gi 796556827 1022 LPAPRAETDP 1031
Cdd:PLN02479 552 LRAKAKEMGP 561
|
|
| Arna_like_SDR_e |
cd05257 |
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ... |
1145-1334 |
1.94e-08 |
|
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187567 [Multi-domain] Cd Length: 316 Bit Score: 57.69 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1145 HVFLTGATGFLGTYLLHELLRDperkvTCLVRGDDGMSRlrqaFRQYDLPQSVLTERVTIVTGELSKPGLGlaaadyDNI 1224
Cdd:cd05257 1 NVLVTGADGFIGSHLTERLLRE-----GHEVRALDIYNS----FNSWGLLDNAVHDRFHFISGDVRDASEV------EYL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1225 VRNADCIFHNGAEV---HHLHRYERLRETNVLGIREILQLACAGEGRHVHYISTlsaltprrgS----GGDPRPVCELES 1297
Cdd:cd05257 66 VKKCDVVFHLAALIaipYSYTAPLSYVETNVFGTLNVLEAACVLYRKRVVHTST---------SevygTAQDVPIDEDHP 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 796556827 1298 VEGFVPPAGGYNRSKWVAEHLVNEAGRR-GLPVTIYRP 1334
Cdd:cd05257 137 LLYINKPRSPYSASKQGADRLAYSYGRSfGLPVTIIRP 174
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
548-725 |
8.73e-08 |
|
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: 56.97 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 548 AAALIMPQADADDIMTYGELNARANRLARLLR-RKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEYPAERIG 626
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 627 AMLSDAGARLVVShSSIDLpkTANRLNLDEDFPDDESADN------LETVTHSSQ------------------LAYVIYT 682
Cdd:cd05905 81 FLLGTCKVRVALT-VEACL--KGLPKKLLKSKTAAEIAKKkgwpkiLDFVKIPKSkrsklkkwgphpptrdgdTAYIEYS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 796556827 683 SGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQFFSFS 725
Cdd:cd05905 158 FSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFK 200
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1043-1101 |
9.74e-08 |
|
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: 50.25 E-value: 9.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 796556827 1043 RIAGAFGHVLNID--QVAATDDFFTLGGHSLLATRFCAVAKDKFGLDIGVIDLFNASTVEA 1101
Cdd:pfam00550 2 RLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
562-948 |
2.31e-07 |
|
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: 55.30 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGgayLPLDPEYpaerigAMLSDAGarlvVSHS 641
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVY------ATLGEDA----LIHS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 642 sidlpktanrlnLDEdfpddESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGLIN--LTRDKIRACDVTADDCVL 719
Cdd:cd17639 73 ------------LNE-----TECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAgiAGLGDRVPELLGPDDRYL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 720 QF------FSFSFdasipELVMSLGAGARLLLLPRyaTL----------------------------------------P 753
Cdd:cd17639 136 AYlplahiFELAA-----ENVCLYRGGTIGYGSPR--TLtdkskrgckgdltefkptlmvgvpaiwdtirkgvlaklnpM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 754 GA------ELADILRARHVTHLTMTP--SALLSLPVDDLLS--LRTVLVGGEvPMPElierwgKTRRFIN--------AY 815
Cdd:cd17639 209 GGlkrtlfWTAYQSKLKALKEGPGTPllDELVFKKVRAALGgrLRYMLSGGA-PLSA------DTQEFLNivlcpviqGY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 816 GPTETTVNASMV---DMGGGRAGLPVlrPAANKQLyvLD-DNLELLPFGVP--GELHIGGCGIARGYHDRAALTAERFVP 889
Cdd:cd17639 282 GLTETCAGGTVQdpgDLETGRVGPPL--PCCEIKL--VDwEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDG 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 890 DPFatdgragvlYRTGDRAVLLADGRIHVSGRLDSQVKIR-GYRIEPGEIEARLLAHPAI 948
Cdd:cd17639 358 DGW---------FHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV 408
|
|
| Gne_like_SDR_e |
cd05238 |
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ... |
1144-1336 |
2.39e-07 |
|
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187549 [Multi-domain] Cd Length: 305 Bit Score: 54.31 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1144 DHVFLTGATGFLGTYLLHELLRDPERkvtclvrgddgmSRLRQAFRQYDLPQSVLTeRVTIVTGELSKPGLGLAAAD-YD 1222
Cdd:cd05238 1 MKVLITGASGFVGQRLAERLLSDVPN------------ERLILIDVVSPKAPSGAP-RVTQIAGDLAVPALIEALANgRP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1223 NIVRNADCIFHNGAEVHhlhrYERLRETNVLGIREILQlACAGEGRHVHYISTLS----ALTPRRGSGGDPRPVcelesv 1298
Cdd:cd05238 68 DVVFHLAAIVSGGAEAD----FDLGYRVNVDGTRNLLE-ALRKNGPKPRFVFTSSlavyGLPLPNPVTDHTALD------ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 796556827 1299 egfvpPAGGYNRSKWVAEHLVNEAGRRG--------LPVTIYRPGA 1336
Cdd:cd05238 137 -----PASSYGAQKAMCELLLNDYSRRGfvdgrtlrLPTVCVRPGR 177
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
525-1017 |
2.44e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.40 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 525 AQEHAGPQYFHELFE-AHvaRAPQAAALimPQADADDIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAW 603
Cdd:PRK05857 8 AMPQLPSTVLDRVFEqAR--QQPEAIAL--RRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 604 LAVWKAGGAYLPLDPEYPAERIG--AMLSDAGARLVVSHSSID---LPK---TANRLNLDEDFPDDESADNLETVTHSSQ 675
Cdd:PRK05857 84 LACAKLGAIAVMADGNLPIAAIErfCQITDPAAALVAPGSKMAssaVPEalhSIPVIAVDIAAVTRESEHSLDAASLAGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 676 LAY-------VIYTSGSTGKAKGVLVDHSGLINLTrDKIRACDVTADDCVLQFFSFSfdaSIPELVMSLGAGARLLLLPR 748
Cdd:PRK05857 164 ADQgsedplaMIFTSGTTGEPKAVLLANRTFFAVP-DILQKEGLNWVTWVVGETTYS---PLPATHIGGLWWILTCLMHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 749 YATLPGAE----LADILRARHVTHLTMTPSaLLSLPVDDLLSLRTVlvggeVPMPELIErWGKTR------RFINA---- 814
Cdd:PRK05857 240 GLCVTGGEnttsLLEILTTNAVATTCLVPT-LLSKLVSELKSANAT-----VPSLRLVG-YGGSRaiaadvRFIEAtgvr 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 815 ----YGPTET--------TVNASMVDMGGGRAGlpvlRPAANKQLYVLDDN--LELLPFGVP----GELHIGGCGIARGY 876
Cdd:PRK05857 313 taqvYGLSETgctalclpTDDGSIVKIEAGAVG----RPYPGVDVYLAATDgiGPTAPGAGPsasfGTLWIKSPANMLGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 877 HDRAALTAERFVpdpfatDGragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVR 956
Cdd:PRK05857 389 WNNPERTAEVLI------DG----WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEI 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 796556827 957 DDGRGGKRLAAYAVPQIDQD-AATRPTPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKI 1017
Cdd:PRK05857 459 PDEEFGALVGLAVVASAELDeSAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKV 520
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
680-1032 |
3.26e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 55.03 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 680 IYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADD-CVLQFFSFSFDASIPELVMSLGAGARLLLLPRYAtlPGAELA 758
Cdd:PRK13388 156 IFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDvCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFS--ASGFLD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 759 DIlRARHVTHLTMTPSAL---LSLP--VDDLLSLRTVLVGGEVPmPELIERWGktRRF----INAYGPTETTVNASMVD- 828
Cdd:PRK13388 234 DV-RRYGATYFNYVGKPLayiLATPerPDDADNPLRVAFGNEAS-PRDIAEFS--RRFgcqvEDGYGSSEGAVIVVREPg 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 829 -----MGGGRAGLPVLRPAANKQLYV--LDDNLELL-PFGVPGEL-HIGGCGIARGYHDRAALTAERFvpdpfatdgRAG 899
Cdd:PRK13388 310 tppgsIGRGAPGVAIYNPETLTECAVarFDAHGALLnADEAIGELvNTAGAGFFEGYYNNPEATAERM---------RHG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 900 vLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQIDQDAat 979
Cdd:PRK13388 381 -MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATF-- 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 796556827 980 rpTPSEIRAWLANR-------LPKFLvpdtfdWL-EALPLTMNGKIDPLKLPAPRAETDPD 1032
Cdd:PRK13388 458 --DPDAFAAFLAAQpdlgtkaWPRYV------RIaADLPSTATNKVLKRELIAQGWATGDP 510
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
562-993 |
1.08e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 53.21 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 562 MTYGELNAR----ANRLARLLRRKgvsaeTVVAISLPRSFDMIVAWLAVWKAGGAYLPL-DPEYP--AERIGAMLSDAGA 634
Cdd:PRK12476 69 LTWTQLGVRlravGARLQQVAGPG-----DRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 635 RLVVSHSSI---------DLPK-TANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDHSGL----- 699
Cdd:PRK12476 144 TVVLTTTAAaeavegflrNLPRlRRPRVIAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVgtnlv 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 700 -----INLTRDKIRACDVTA--DDCVLQFFSFSFDASIPELVMSLGAgarllllprYATLPG---AELADilRARHVTHL 769
Cdd:PRK12476 224 qmilsIDLLDRNTHGVSWLPlyHDMGLSMIGFPAVYGGHSTLMSPTA---------FVRRPQrwiKALSE--GSRTGRVV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 770 TMTP------SALLSLPVD-DLLSLRTV--LVGGEVPMPELIERWGKT--------RRFINAYGPTETTVNASMVD---- 828
Cdd:PRK12476 293 TAAPnfayewAAQRGLPAEgDDIDLSNVvlIIGSEPVSIDAVTTFNKAfapyglprTAFKPSYGIAEATLFVATIApdae 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 829 ----------MGGGRAgLPVL-------------RPAANKQLYVLDDNLEL-LPFGVPGELHIGGCGIARGYHDRAALTA 884
Cdd:PRK12476 373 psvvyldreqLGAGRA-VRVAadapnavahvscgQVARSQWAVIVDPDTGAeLPDGEVGEIWLHGDNIGRGYWGRPEETE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 885 ERF-------VPDPFATDGRA--GVLYRTGDRAVLLaDGRIHVSGRLDSQVKIRGYRIEPGEIEArllahpAIVSATVAV 955
Cdd:PRK12476 452 RTFgaklqsrLAEGSHADGAAddGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEA------TVAEASPMV 524
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 796556827 956 RddgRGgkRLAAYAVPQIDQD----------AATRPTPSE----IRAWLANR 993
Cdd:PRK12476 525 R---RG--YVTAFTVPAEDNErlvivaeraaGTSRADPAPaidaIRAAVSRR 571
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
545-972 |
1.10e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 53.15 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 545 APQAAALIMPQADADD--------IMTYGELNARANRLARLLR-RKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLP 615
Cdd:PRK07867 4 APTVAELLLPLAEDDDrglyfedsFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 LDPEYPAERIGAMLSDAGARLVVSHSSI-----DLPKTANRLNLDEDFPDDESADNLET-----VTHSSQLAYVIYTSGS 685
Cdd:PRK07867 84 LNPTRRGAALARDIAHADCQLVLTESAHaelldGLDPGVRVINVDSPAWADELAAHRDAeppfrVADPDDLFMLIFTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 686 TGKAKGVLVDH-----SGLINLTRDKIRACDVtaddCVLQFFSFSFDASIPELVMSLGAGARLLLLPRYATlpGAELADI 760
Cdd:PRK07867 164 SGDPKAVRCTHrkvasAGVMLAQRFGLGPDDV----CYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSA--SGFLPDV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 761 lRARHVTHLTMTPSAL---LS---LPVDDLLSLRtVLVGGEVPMPElIERWGktRRF----INAYGPTETTVNASMVD-- 828
Cdd:PRK07867 238 -RRYGATYANYVGKPLsyvLAtpeRPDDADNPLR-IVYGNEGAPGD-IARFA--RRFgcvvVDGFGSTEGGVAITRTPdt 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 829 ----MGGGRAGLPVLRPAANKQL--YVLDDNLELLPFGVPGEL-HIGGCGIARGYHDRAALTAERFvpdpfatdgRAGVl 901
Cdd:PRK07867 313 ppgaLGPLPPGVAIVDPDTGTECppAEDADGRLLNADEAIGELvNTAGPGGFEGYYNDPEADAERM---------RGGV- 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 796556827 902 YRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAVRDDGRGGKRLAAYAVPQ 972
Cdd:PRK07867 383 YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
563-1022 |
1.33e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 52.79 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSA---------------ETVVAIS---------LPRSFDMIVAWLaVWKAGGAYLPLD- 617
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPgdrvgtlawngyrhlEAYYGVSgsgavchtiNPRLFPEQIAYI-VNHAEDRYVLFDl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 618 ----------PEYPAERIGAMLSDAgarlvvSHssidLPKTANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTG 687
Cdd:PRK07008 120 tflplvdalaPQCPNVKGWVAMTDA------AH----LPAGSTPLLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 688 KAKGVLVDH---------SGLINltrdkirACDVTADDCVLQFFS-FSFDA-SIPelvMSLGAGARLLLLPRYAtLPGAE 756
Cdd:PRK07008 190 NPKGALYSHrstvlhaygAALPD-------AMGLSARDAVLPVVPmFHVNAwGLP---YSAPLTGAKLVLPGPD-LDGKS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 757 LADILRARHVTHLTMTPSALLSLPVD------DLLSLRTVLVGGEVPMPELIERWGKTR--RFINAYGPTETTVNASMVD 828
Cdd:PRK07008 259 LYELIEAERVTFSAGVPTVWLGLLNHmreaglRFSTLRRTVIGGSACPPAMIRTFEDEYgvEVIHAWGMTEMSPLGTLCK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 829 MGGGRAGLP--VLRPAANKQ--------LYVLDDNLELLPF-GVP-GELHIGGCGIARGYHDRAAltaerfvpDPFaTDG 896
Cdd:PRK07008 339 LKWKHSQLPldEQRKLLEKQgrviygvdMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRGDA--------SPL-VDG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 897 ragvLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSAtvavrddgrggkrlAAYAVPQIDQD 976
Cdd:PRK07008 410 ----WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEA--------------ACIACAHPKWD 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 796556827 977 ------AATRP----TPSEIRAWLANRLPKFLVPDTFDWLEALPLTMNGKIDPLKL 1022
Cdd:PRK07008 472 erpllvVVKRPgaevTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
759-948 |
2.55e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 51.69 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 759 DILRARHVTHLTMTPSALLSL----------PVDdlLSLRTVLVGGEvPMPE-----LIERWGktRRFINAYGPTETTVN 823
Cdd:COG1541 169 RLMQDFGPTVLVGTPSYLLYLaevaeeegidPRD--LSLKKGIFGGE-PWSEemrkeIEERWG--IKAYDIYGLTEVGPG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 824 ASMvdMGGGRAGLpVLRPAankQLYV--LD-DNLELLPFGVPGELhiggcgiargyhdraaltaerfVpdpFATDGRAGV 900
Cdd:COG1541 244 VAY--ECEAQDGL-HIWED---HFLVeiIDpETGEPVPEGEEGEL----------------------V---VTTLTKEAM 292
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 901 L---YRTGDRAVLLAD----GRIH-----VSGRLDSQVKIRGYRIEPGEIEARLLAHPAI 948
Cdd:COG1541 293 PlirYRTGDLTRLLPEpcpcGRTHprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
559-718 |
2.59e-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: 51.91 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 559 DDIMTYGELNARANRLAR-LLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAG--GAYLP-------------------- 615
Cdd:cd05938 3 GETYTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakvl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 616 -LDPEYPA--ERIGAMLSDAGARL-VVSHSSIDlPKTANRLNLDEDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKG 691
Cdd:cd05938 83 vVAPELQEavEEVLPALRADGVSVwYLSHTSNT-EGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKA 161
|
170 180
....*....|....*....|....*..
gi 796556827 692 VLVDHSGLINLTrDKIRACDVTADDCV 718
Cdd:cd05938 162 ARISHLRVLQCS-GFLSLCGVTADDVI 187
|
|
| 3b-HSD-NSDHL-like_SDR_e |
cd09813 |
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ... |
1146-1406 |
5.53e-06 |
|
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187673 [Multi-domain] Cd Length: 335 Bit Score: 50.43 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPErkvtCLVRGDDgmsrLRQAFrqYDLPQSVltERVTIVTGELSKPGlglaaaDYDNIV 1225
Cdd:cd09813 2 CLVVGGSGFLGRHLVEQLLRRGN----PTVHVFD----IRPTF--ELDPSSS--GRVQFHTGDLTDPQ------DLEKAF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 R--NADCIFHNGAEVHHLHR--YERLretNVLGIREILQlACAGEG-RHVHYISTLSALtprrgSGGdpRPVCEL-ESVE 1299
Cdd:cd09813 64 NekGPNVVFHTASPDHGSNDdlYYKV---NVQGTRNVIE-ACRKCGvKKLVYTSSASVV-----FNG--QDIINGdESLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1300 GFVPPAGGYNRSKWVAEHLVNEAGRR--GLPVTIYRPGAISGDSVTGAFNGSDILCRLVQAYLYTGtapEGERLLDMLPV 1377
Cdd:cd09813 133 YPDKHQDAYNETKALAEKLVLKANDPesGLLTCALRPAGIFGPGDRQLVPGLLKAAKNGKTKFQIG---DGNNLFDFTYV 209
|
250 260 270
....*....|....*....|....*....|....*...
gi 796556827 1378 DHVARAivHL---------SGKPASAGQVFHLIHSSPV 1406
Cdd:cd09813 210 ENVAHA--HIlaadallssSHAETVAGEAFFITNDEPI 245
|
|
| 3Beta_HSD |
pfam01073 |
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ... |
1149-1408 |
7.36e-06 |
|
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.
Pssm-ID: 366449 [Multi-domain] Cd Length: 279 Bit Score: 49.67 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1149 TGATGFLGTYLLHELLRDPERKVtclVRGDDgmsrlrQAFRQYDLPQSVLTERVTIVTGELSKPglglaaADYDNIVRNA 1228
Cdd:pfam01073 3 TGGGGFLGRHIIKLLVREGELKE---VRVFD------LRESPELLEDFSKSNVIKYIQGDVTDK------DDLDNALEGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1229 DCIFHNGA--EVHHLHRYERLRETNVLGIREILQlACAGEG-RHVHYISTLSALTP-------RRGSGGDPRPVCelesv 1298
Cdd:pfam01073 68 DVVIHTASavDVFGKYTFDEIMKVNVKGTQNVLE-ACVKAGvRVLVYTSSAEVVGPnsygqpiLNGDEETPYEST----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1299 egfvpPAGGYNRSKWVAEHLVNEAGRRGL--PVTIY----RPGAISGDsvtgafnGSDILCRLVQAYLYTGTA----PEG 1368
Cdd:pfam01073 142 -----HQDAYPRSKAIAEKLVLKANGRPLknGGRLYtcalRPAGIYGE-------GDRLLVPFIVNLAKLGLAkfktGDD 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 796556827 1369 ERLLDMLPVDHVARAIVhLSGK--------PASAGQVFHLIHSSPVSS 1408
Cdd:pfam01073 210 NNLSDRVYVGNVAWAHI-LAARalqdpkkmSSIAGNAYFIYDDTPVQS 256
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
563-997 |
1.26e-05 |
|
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: 49.74 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 563 TYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLDPEY---------------------- 620
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslmsqdlaklkhlfellkpglv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 621 ------PAERIGAMLSDAGARLVVSHSSIDLPKTANRLNLDEdFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLV 694
Cdd:cd05921 107 faqdaaPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAA-TPPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVIN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 695 DHsGLINLTRDKIRACDVTADDCVLQF-----FSFSFDASI--------------------PELVMSLGAGARLLLLPRY 749
Cdd:cd05921 186 TQ-RMLCANQAMLEQTYPFFGEEPPVLvdwlpWNHTFGGNHnfnlvlynggtlyiddgkpmPGGFEETLRNLREISPTVY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 750 ATLPG--AELA------DILRARHVTHLTMTPSALLSLPVD-----DLLSLRTVlvggevpmpelierwGKTRRFINAYG 816
Cdd:cd05921 265 FNVPAgwEMLVaalekdEALRRRFFKRLKLMFYAGAGLSQDvwdrlQALAVATV---------------GERIPMMAGLG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 817 PTETTVNASMVDMGGGRAGLPVLrPAANKQLyvlddnlELLPFGVPGELHIGGCGIARGYHDRAALTAERFVPDPFATDG 896
Cdd:cd05921 330 ATETAPTATFTHWPTERSGLIGL-PAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 897 RAGVLYRTGD-RAVLLADGRIHVSGRLDSqvkirGYRIEPGEIEARLLAH--PAIVSATVAvrddGRGGKRLAAYAVPQI 973
Cdd:cd05921 402 DAAKLADPDDpAKGLVFDGRVAEDFKLAS-----GTWVSVGPLRARAVAAcaPLVHDAVVA----GEDRAEVGALVFPDL 472
|
490 500 510
....*....|....*....|....*....|....*..
gi 796556827 974 -------------DQDAATRPtpsEIRAWLANRLPKF 997
Cdd:cd05921 473 lacrrlvglqeasDAEVLRHA---KVRAAFRDRLAAL 506
|
|
| SDR_a7 |
cd05262 |
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ... |
1145-1414 |
1.40e-05 |
|
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187572 [Multi-domain] Cd Length: 291 Bit Score: 48.88 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1145 HVFLTGATGFLGTYLLHELLRDPERkVTCLVRGDDGMSRLRQAfrqydlpqsvlteRVTIVTGELSKPGLGLAAAdydni 1224
Cdd:cd05262 2 KVFVTGATGFIGSAVVRELVAAGHE-VVGLARSDAGAAKLEAA-------------GAQVHRGDLEDLDILRKAA----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1225 vRNADCIFHNGAeVHHLHRYERLRETNVLGIREILQlACAGEGRHVHYISTLSALTPRRGSGGDPRPVcelesvegFVPP 1304
Cdd:cd05262 63 -AEADAVIHLAF-THDFDNFAQACEVDRRAIEALGE-ALRGTGKPLIYTSGIWLLGPTGGQEEDEEAP--------DDPP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1305 AGGYNRskwVAEHLVNEAGRRGLPVTIYR-PGAISGDSVTGAFNGSDILCRLVQAYLYTGtapEGERLLDMLPVDHVARA 1383
Cdd:cd05262 132 TPAARA---VSEAAALELAERGVRASVVRlPPVVHGRGDHGFVPMLIAIAREKGVSAYVG---DGKNRWPAVHRDDAARL 205
|
250 260 270
....*....|....*....|....*....|.
gi 796556827 1384 IVHLSGKPaSAGQVFHLIHSSPVSSARLFEA 1414
Cdd:cd05262 206 YRLALEKG-KAGSVYHAVAEEGIPVKDIAEA 235
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
677-1018 |
8.46e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 47.27 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 677 AYVIYTSGSTGKAKGVLVDHSGLINLTRDKIRACDVTADDCVLQ----FFSFSFDA----------------------SI 730
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNalpvFHSFGLTGglvlpllsgvkvflypsplhyrII 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 731 PELVmslgagarllllprYATlpgaeLADILRArhvTHLTMTPSALLSLPVdDLLSLRTVLVGGEvPMPE-----LIERW 805
Cdd:PRK06814 876 PELI--------------YDT-----NATILFG---TDTFLNGYARYAHPY-DFRSLRYVFAGAE-KVKEetrqtWMEKF 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 806 GKtrRFINAYGPTETT----VNASMVDMGG--GRAgLPvlrpaankqlyVLDDNLELLPfGVP--GELHIGGCGIARGYh 877
Cdd:PRK06814 932 GI--RILEGYGVTETApviaLNTPMHNKAGtvGRL-LP-----------GIEYRLEPVP-GIDegGRLFVRGPNVMLGY- 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 878 draaLTAERfvpdPFATDGRAGVLYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEArlLAH---PAIVSATVA 954
Cdd:PRK06814 996 ----LRAEN----PGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE--LAAelwPDALHAAVS 1065
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 796556827 955 VrDDGRGGKRLAAYAvpqiDQDAATRptpSEIRAWL-ANRLPKFLVPDTFDWLEALPLTMNGKID 1018
Cdd:PRK06814 1066 I-PDARKGERIILLT----TASDATR---AAFLAHAkAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
543-1017 |
1.15e-04 |
|
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: 46.88 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 543 ARAPQAAALIMPQADADDIMTYGELNARANRLARLLRRKGV-SAETVVAIsLPRSFDMIVAWLAVWKAGGAYLPLDPEYP 621
Cdd:cd05943 80 ADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVkPGDRVAGY-LPNIPEAVVAMLATASIGAIWSSCSPDFG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 622 A----ERIG------------------------------AMLSDAGARLVVSHSS----IDLPKTANRLNLdEDFPDDES 663
Cdd:cd05943 159 VpgvlDRFGqiepkvlfavdaytyngkrhdvrekvaelvKGLPSLLAVVVVPYTVaagqPDLSKIAKALTL-EDFLATGA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 664 ADNLE-TVTHSSQLAYVIYTSGSTGKAKGVLVDHSG-LINLTRDKIRACDVTADDcVLQFFS----------FSFDASIP 731
Cdd:cd05943 238 AGELEfEPLPFDHPLYILYSSGTTGLPKCIVHGAGGtLLQHLKEHILHCDLRPGD-RLFYYTtcgwmmwnwlVSGLAVGA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 732 ELVMslgagarLLLLPRYATLpgAELADILRARHVTHLTMTPSALLSL------PVD--DLLSLRTVLVGGEvPMP---- 799
Cdd:cd05943 317 TIVL-------YDGSPFYPDT--NALWDLADEEGITVFGTSAKYLDALekaglkPAEthDLSSLRTILSTGS-PLKpesf 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 800 ELIERWGKTRRFINAY-GPTettvnasmvDMGGGRAG----LPVLR-----PAANKQLYVLDDNLELLPfGVPGELHIgg 869
Cdd:cd05943 387 DYVYDHIKPDVLLASIsGGT---------DIISCFVGgnplLPVYRgeiqcRGLGMAVEAFDEEGKPVW-GEKGELVC-- 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 870 cgiargyhdRAALTAE--RFVPDPFATDGRA-------GVlYRTGDRAVLLADGRIHVSGRLDSQVKIRGYRIEPGEIEA 940
Cdd:cd05943 455 ---------TKPFPSMpvGFWNDPDGSRYRAayfakypGV-WAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYR 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 941 RLLAHPAIVSATVAVRDDGRGGKRLAAYaVPQIDQDAATRPTPSEIRAWLANRL-PKFlVPDTFDWLEALPLTMNGKI 1017
Cdd:cd05943 525 VVEKIPEVEDSLVVGQEWKDGDERVILF-VKLREGVELDDELRKRIRSTIRSALsPRH-VPAKIIAVPDIPRTLSGKK 600
|
|
| SDR_a2 |
cd05245 |
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ... |
1146-1415 |
1.64e-04 |
|
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187556 [Multi-domain] Cd Length: 293 Bit Score: 45.41 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPERkVTCLVRGDDGMSRLRQAfrqydlpqsvltERVTIVTGELSKPGlGLAAAdydniV 1225
Cdd:cd05245 1 VLVTGATGYVGGRLVPRLLQEGHQ-VRALVRSPEKLADRPWS------------ERVTVVRGDLEDPE-SLRAA-----L 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNADCIFHngaEVHHLHRYERLRETNVLGIREILQLACAGEGRHVHYistLSALTPRrgsGGDPRPvcelesvegfvppa 1305
Cdd:cd05245 62 EGIDTAYY---LVHSMGSGGDFEEADRRAARNFARAARAAGVKRIIY---LGGLIPK---GEELSP-------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1306 ggYNRSKWVAEHLVNEAgrrGLPVTIYRPGAISGdSVTGAFngsDILCRLVQ--------AYLYTGTAPegerlldmLPV 1377
Cdd:cd05245 119 --HLRSRAEVGEILRAG---GVPVTELRAAVIIG-SGSASF---EMVRYLVErlpvmitpRWVNTPCQP--------IAI 181
|
250 260 270
....*....|....*....|....*....|....*....
gi 796556827 1378 DHVARAIVHLSGKPASAGQVFHlIHSSPVSSAR-LFEAC 1415
Cdd:cd05245 182 RDVLEYLVAALDRPATAGETFE-IGGPDVLSYKdMMERF 219
|
|
| 3b-HSD_HSDB1_like_SDR_e |
cd09811 |
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ... |
1148-1327 |
3.74e-04 |
|
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187671 [Multi-domain] Cd Length: 354 Bit Score: 44.42 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1148 LTGATGFLGTYLLHELL-RDPERKVTCLVrgDDGMSR-LRQAFRQYDLPQsvlteRVTIVTGELskpglgLAAADYDNIV 1225
Cdd:cd09811 4 VTGGGGFLGQHIIRLLLeRKEELKEIRVL--DKAFGPeLIEHFEKSQGKT-----YVTDIEGDI------KDLSFLFRAC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNADCIFHNGAEVHHLHR--YERLRETNVLGIREILQlACAGEG-RHVHYISTLS-ALTPRRG----SGGDPRPvceLES 1297
Cdd:cd09811 71 QGVSVVIHTAAIVDVFGPpnYEELEEVNVNGTQAVLE-ACVQNNvKRLVYTSSIEvAGPNFKGrpifNGVEDTP---YED 146
|
170 180 190
....*....|....*....|....*....|
gi 796556827 1298 VEGFvppagGYNRSKWVAEHLVNEAGRRGL 1327
Cdd:cd09811 147 TSTP-----PYASSKLLAENIVLNANGAPL 171
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1055-1109 |
7.36e-04 |
|
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: 7.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 796556827 1055 DQVAATDDFFTLGGHSLLATRFCAVAKDKFGLDIGVIDLFNASTVEALANRLRTR 1109
Cdd:smart00823 31 EAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
|
|
| AR_SDR_e |
cd05227 |
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ... |
1146-1413 |
8.54e-04 |
|
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187538 [Multi-domain] Cd Length: 301 Bit Score: 43.03 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLRDPErKVTCLVRGDDGMSRLRQAFRQYDLPQSVLTERVTIVTgelskpglglAAADYDNIV 1225
Cdd:cd05227 2 VLVTGATGFIASHIVEQLLKAGY-KVRGTVRSLSKSAKLKALLKAAGYNDRLEFVIVDDLT----------APNAWDEAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1226 RNADCIFHNGAEVHH--LHRYERLRETNVLGIREILQlACAGEG--RHVHYISTLSALTPrrGSGGDPRPVCELES---- 1297
Cdd:cd05227 71 KGVDYVIHVASPFPFtgPDAEDDVIDPAVEGTLNVLE-AAKAAGsvKRVVLTSSVAAVGD--PTAEDPGKVFTEEDwndl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1298 VEGFVPPAGGYNRSKWVAEhlvNEA------GRRGLPVTIYRPGAISGDSVTGA-FNGS-DILCRLVQAYLYTGTAPEGE 1369
Cdd:cd05227 148 TISKSNGLDAYIASKTLAE---KAAwefvkeNKPKFELITINPGYVLGPSLLADeLNSSnELINKLLDGKLPAIPPNLPF 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 796556827 1370 RLLDmlpVDHVARAIVHLSGKPASAGQVFhLIHSSPVSSARLFE 1413
Cdd:cd05227 225 GYVD---VRDVADAHVRALESPEAAGQRF-IVSAGPFSFQEIAD 264
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
786-946 |
8.62e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 43.95 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 786 SLRTVLVGGeVPMPelierwGKTRRFIN---------AYGPTETTVNASMV---DMGGGRAGLPVlrPAANKQL------ 847
Cdd:PLN02387 421 RIRFMLSGG-APLS------GDTQRFINiclgapigqGYGLTETCAGATFSewdDTSVGRVGPPL--PCCYVKLvsweeg 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 848 -YVLDDNlellPfgVP-GELHIGGCGIARGYHDRAALTAErfvpdPFATDGRAGVLYRTGDRAVLLADGRIHVSGRLDSQ 925
Cdd:PLN02387 492 gYLISDK----P--MPrGEIVIGGPSVTLGYFKNQEKTDE-----VYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDI 560
|
170 180
....*....|....*....|..
gi 796556827 926 VKIR-GYRIEPGEIEARLLAHP 946
Cdd:PLN02387 561 VKLQhGEYVSLGKVEAALSVSP 582
|
|
| PLN02996 |
PLN02996 |
fatty acyl-CoA reductase |
1146-1275 |
1.14e-03 |
|
fatty acyl-CoA reductase
Pssm-ID: 215538 [Multi-domain] Cd Length: 491 Bit Score: 43.16 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1146 VFLTGATGFLGTYLLHELLR-DPE-RKVTCLVRGDDG---MSRLRQAFRQYDL-----------PQSVLTERVTIVTGEL 1209
Cdd:PLN02996 14 ILVTGATGFLAKIFVEKILRvQPNvKKLYLLLRASDAksaTQRLHDEVIGKDLfkvlreklgenLNSLISEKVTPVPGDI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 796556827 1210 SKPGLGLAAADY-DNIVRNADCIFHNGAEVHHLHRYERLRETNVLGIREILQLA--CAgEGRHVHYIST 1275
Cdd:PLN02996 94 SYDDLGVKDSNLrEEMWKEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAkkCV-KVKMLLHVST 161
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
560-955 |
1.15e-03 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 43.46 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 560 DIMTYGELNARANRLARLLRRKGVSAETVVAISLPRSFDMIVAWLAVWKAGGAYLPLdpEYPA---------ERIGAMLS 630
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPMgfggresyiAQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 631 DAGARLVVSHSSI----DLPKTANRLNLD---EDFPDDESAD-NLETVThSSQLAYVIYTSGSTGKAKGVLVDH-SGLIN 701
Cdd:PRK09192 126 SAQPAAIITPDELlpwvNEATHGNPLLHVlshAWFKALPEADvALPRPT-PDDIAYLQYSSGSTRFPRGVIITHrALMAN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 702 L---TRD--KIRAcdvtADDCVlQFFSFSFDASIPELVMSLGAGARLLLLPR---YATLPGAELADILRAR--------- 764
Cdd:PRK09192 205 LraiSHDglKVRP----GDRCV-SWLPFYHDMGLVGFLLTPVATQLSVDYLPtrdFARRPLQWLDLISRNRgtisysppf 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 765 --HVTHLTMTPSALLSLpvdDLLSLRTVLVGGEV----PMPELIERWG----KTRRFINAYGPTETTVNASMVDMGGG-- 832
Cdd:PRK09192 280 gyELCARRVNSKDLAEL---DLSCWRVAGIGADMirpdVLHQFAEAFApagfDDKAFMPSYGLAEATLAVSFSPLGSGiv 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 833 --RAGLPVL-----------------------RPAANKQLYVLDDNLELLPFGVPGELHIGGCGIARGYHDRAAlTAERF 887
Cdd:PRK09192 357 veEVDRDRLeyqgkavapgaetrrvrtfvncgKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVL 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 796556827 888 VPDpfatdgraGVLyRTGDRAVLLaDGRIHVSGRLDSQVKIRGYRIEPGEIEARLLAHPAIVSATVAV 955
Cdd:PRK09192 436 AAD--------GWL-DTGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAA 493
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
589-696 |
1.78e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 42.79 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 589 VAISLPRSFDMIVAWLAVWKAGGAYLPL-DPEYP--AERIGAMLSDAGARLVVSHSSI---------DLP-KTANRLNLD 655
Cdd:PRK07769 82 VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSaegvrkffrARPaKERPRVIAV 161
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 796556827 656 EDFPDDESADNLETVTHSSQLAYVIYTSGSTGKAKGVLVDH 696
Cdd:PRK07769 162 DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITH 202
|
|
| SDR |
cd02266 |
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ... |
1229-1340 |
9.71e-03 |
|
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187535 [Multi-domain] Cd Length: 186 Bit Score: 39.04 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 796556827 1229 DCIFHNGAEVH-------HLHRYERLRETNVLGIREILQLACA-----GEGRhVHYISTLSALTprrgsggdprpvcele 1296
Cdd:cd02266 33 DVVVHNAAILDdgrlidlTGSRIERAIRANVVGTRRLLEAARElmkakRLGR-FILISSVAGLF---------------- 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 796556827 1297 svegFVPPAGGYNRSKWVAEHLVNEAGR----RGLPVTIYRPGAISGD 1340
Cdd:cd02266 96 ----GAPGLGGYAASKAALDGLAQQWASegwgNGLPATAVACGTWAGS 139
|
|
| SPR-like_SDR_c |
cd05367 |
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ... |
1145-1286 |
9.72e-03 |
|
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187625 [Multi-domain] Cd Length: 241 Bit Score: 39.58 E-value: 9.72e-03
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gi 796556827 1145 HVFLTGATGFLGTYLLHELL-RDPERKVTCLVRGDDGMSRLrQAFRQYDLpqsvlteRVTIVTGELSKP-GLG--LAAAD 1220
Cdd:cd05367 1 VIILTGASRGIGRALAEELLkRGSPSVVVLLARSEEPLQEL-KEELRPGL-------RVTTVKADLSDAaGVEqlLEAIR 72
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gi 796556827 1221 YDNIVRnaDCIFHNGAEVHHLHRYE--------RLRETNVLGIREILQL---ACAGEG--RHVHYISTLSALTPRRGSG 1286
Cdd:cd05367 73 KLDGER--DLLINNAGSLGPVSKIEfidldelqKYFDLNLTSPVCLTSTllrAFKKRGlkKTVVNVSSGAAVNPFKGWG 149
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