|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-1016 |
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: 704.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 7 PVFQSSADEGGFNNRKKTFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKM 86
Cdd:COG1020 225 PTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 87 VGLFINAVPLRVKGDGDTVFIALAQKLNSDFIKANtSYGYSSLADIQ-ALTKMKEK----LINHMLVYENYPVDDYgkav 161
Cdd:COG1020 303 VGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAY-AHQDLPFERLVeELQPERDLsrnpLFQVMFVLQNAPADEL---- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 162 ddTTDALRITDMEVFEQT-NYDFGLVIIP-GSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNE 239
Cdd:COG1020 378 --ELPGLTLEPLELDSGTaKFDLTLTVVEtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTA 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 240 EERG-MLQEFNKQSSNYTVNKTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRP 318
Cdd:COG1020 456 AERQqLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLER 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 319 SEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDLCFLAD-KNIAAECLDItDKSIYTSQNTSNPDVQY 397
Cdd:COG1020 536 SLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARlPELGVPVLAL-DALALAAEPATNPPVPV 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 398 DLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVY 477
Cdd:COG1020 615 TPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEAR 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 478 LHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVdmLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVG 557
Cdd:COG1020 695 RDPAALAELLARHRVTVLNLTPSLLRALLDAA--PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVD 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 558 CIAHSIDLDHIQNCEIynKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFH-PGAK 636
Cdd:COG1020 773 STYYEVTPPDADGGSV--PIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGAR 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 637 MYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIE----EKYLSAYITGDIEMEGSFV 712
Cdd:COG1020 851 LYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAA 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 713 QEKLAQALPKYMIPSFIIQLKELPLTANGKINRKELPLPDLQRLSVPRYEAPANETEEKLAEIWKEMLGHKRISINEDFF 792
Cdd:COG1020 931 LLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFF 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 793 ELGGHSLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRLIQKRDKQNYPVISKARKQSYYQASSAQKRMFALWETDKD 872
Cdd:COG1020 1011 FGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLL 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 873 SIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEFDYQKLPSDG-------IRPYVK 945
Cdd:COG1020 1091 ALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLlaaaaaaAELLAA 1170
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 946 QFIRPFHLDKSPLIRAGLITYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQPPLQSKDYSEWQ 1016
Cdd:COG1020 1171 AALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALL 1241
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-1016 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 631.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 27 IDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGIEKMVGLFINAVP--------LRV 98
Cdd:PRK12316 1772 LDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPviaaprpdQSV 1851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 99 KGdgdtvFIALAQKLNSdfikANTSYGYSSLADIQALTKMK-EKLINHMLVYENYPVddyGKAVDDTTDA-LRITDMEVF 176
Cdd:PRK12316 1852 AD-----WLQEVQALNL----ALREHEHTPLYDIQRWAGQGgEALFDSLLVFENYPV---AEALKQGAPAgLVFGRVSNH 1919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 177 EQTNYDFGLVIIPGSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERGMLQ-EFNKQSSNY 255
Cdd:PRK12316 1920 EQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILaDWDRTPEAY 1999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 256 TVNKTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSA 335
Cdd:PRK12316 2000 PRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGA 2079
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 336 FLPIDDESPVSRINHILKDSKADILITDLCFLADKNIAA--ECLDITDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSG 413
Cdd:PRK12316 2080 YVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAgvARLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTG 2159
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 414 KPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSlSLIEYIHKNSIT 493
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPE-QLYDEMERHGVT 2238
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 494 YLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHsiDLDHIQNC-E 572
Cdd:PRK12316 2239 ILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLW--KCRPQDPCgA 2316
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 573 IYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGDLGRWMPDGN 651
Cdd:PRK12316 2317 AYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGV 2396
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 652 IEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE---KYLSAYITGDIEMEG--SFVQEKLAQALPKYMIP 726
Cdd:PRK12316 2397 VEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGasgKQLVAYVVPDDAAEDllAELRAWLAARLPAYMVP 2476
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 727 SFIIQLKELPLTANGKINRKELPLPDLQRLSvPRYEAPANETEEKLAEIWKEMLGHKRISINEDFFELGGHSLTAAFTIS 806
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLR-QAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVS 2555
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 807 RIRKTFGTDIKVKELFEQPTIKQLSRLIQKRDKQNYPVISKARKQSYYQASSAQKRMFALWETDKDSIVYNLPIMIELNG 886
Cdd:PRK12316 2556 RVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRG 2635
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 887 KLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELE---FDYQKLPSDGIRPYVKQFI-RPFHLDKSPLIRAG 962
Cdd:PRK12316 2636 VLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRivlEDCAGVADAAIRQRVAEEIqRPFDLARGPLLRVR 2715
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 963 LITYEDRN-LLLLDVHHIAADGVSVGIIRKEFNALYAGHK------LKQPPLQSKDYSEWQ 1016
Cdd:PRK12316 2716 LLALDGQEhVLVITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYAAWQ 2776
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-1016 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 630.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 35 LKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcRVQgIEKMVGLFINAVPLRVKGDGDTVFIALAQKLN 114
Cdd:PRK12467 285 LKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRN-RVE-TERLIGFFVNTQVLKAEVDPQASFLELLQQVK 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 115 SDFIKANT-----------------SYGYSSLADIqaltkmkekLINHMLVYENYPVDDYGkavddTTDALRITDMEVFE 177
Cdd:PRK12467 363 RTALGAQAhqdlpfeqlvealqperSLSHSPLFQV---------MFNHQNTATGGRDREGA-----QLPGLTVEELSWAR 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 178 QT-NYDFGLVIIPGSQ-IKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERG-MLQEFNKQSSN 254
Cdd:PRK12467 429 HTaQFDLALDTYESAQgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERArELVRWNAPATE 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 255 YTVNKTIQdLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGS 334
Cdd:PRK12467 509 YAPDCVHQ-LIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGG 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 335 AFLPIDDESPVSRINHILKDSKADILITDLCFLADKNIAAE----CLDITDKSIYTSQNtSNPDVQYDLEDEVYVIYTSG 410
Cdd:PRK12467 588 AYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGlrslCLDEPADLLCGYSG-HNPEVALDPDNLAYVIYTSG 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 411 TSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKN 490
Cdd:PRK12467 667 STGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQ 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 491 SITYLKMTPTLFSTLMEDvDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHIQN 570
Cdd:PRK12467 747 GVTVLKIVPSHLQALLQA-SRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDF 825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 571 CEIYnkIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHP-GAKMYKTGDLGRWMPD 649
Cdd:PRK12467 826 GNVP--IGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRAD 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 650 GNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKY---LSAYITGDIEMEGSFVQEK-------LAQA 719
Cdd:PRK12467 904 GVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAglqLVAYLVPAAVADGAEHQATrdelkaqLRQV 983
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 720 LPKYMIPSFIIQLKELPLTANGKINRKELPLPDLqrlSVPR--YEAPANETEEKLAEIWKEMLGHKRISINEDFFELGGH 797
Cdd:PRK12467 984 LPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDA---SAVQatFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGH 1060
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 798 SLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRLIQKRDKQNYPVISKARKQSYYQASSAQKRMFALWETDKDSIVYN 877
Cdd:PRK12467 1061 SLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYH 1140
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 878 LPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEFDYQKLPSDG-----IRPYVKQFIR-PF 951
Cdd:PRK12467 1141 IPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADkdeaqLKVYVEAEARqPF 1220
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085927195 952 HLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYA----GHKLKQP--PLQSKDYSEWQ 1016
Cdd:PRK12467 1221 DLEQGPLLRVGLLrLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAaysqGQSLQLPalPIQYADYAVWQ 1292
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
273-748 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 537.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILITdlcfladkniaaeclditdksiytsqntsnpdvqyDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWV 432
Cdd:cd05930 81 EDSGAKLVLT-----------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 433 CDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDmL 512
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE-L 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 513 ASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHIQNCEIynKIGRPIHGINIYIVDRS 592
Cdd:cd05930 205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRV--PIGRPIPNTRVYVLDEN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 593 DQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIG 672
Cdd:cd05930 283 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 673 EIENQLLQLEGIKEAAVVYIE----EKYLSAYITGDIEMEGSF--VQEKLAQALPKYMIPSFIIQLKELPLTANGKINRK 746
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAREdgdgEKRLVAYVVPDEGGELDEeeLRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
..
gi 2085927195 747 EL 748
Cdd:cd05930 443 AL 444
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
264-752 |
1.28e-179 |
|
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: 531.52 E-value: 1.28e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 264 LFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDES 343
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 344 PVSRINHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTSQNTS-NPDVQYDleDEVYVIYTSGTSGKPKGVKVKN 422
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENlEPVSKSD--DLAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 423 KSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLF 502
Cdd:cd17655 160 RGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 503 StLMEDVDMLASCPdLKVIILGGESINIGNVKKLAEKCRW-MKFINHYGPTESTVGCIAHSIDLDHIQNCEIynKIGRPI 581
Cdd:cd17655 240 K-LLDAADDSEGLS-LKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVDASIYQYEPETDQQVSV--PIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 582 HGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQ 661
Cdd:cd17655 316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 662 IKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE----KYLSAYITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPL 737
Cdd:cd17655 396 VKIRGYRIELGEIEARLLQHPDIKEAVVIARKDeqgqNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPL 475
|
490
....*....|....*
gi 2085927195 738 TANGKINRKELPLPD 752
Cdd:cd17655 476 TPNGKVDRKALPEPD 490
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-851 |
6.29e-175 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 567.48 E-value: 6.29e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 28 DETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGIEKMVGLFINAVPLRVKGDGDTVFI 107
Cdd:PRK12467 2865 DATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVS 2944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 108 ALAQKLNSDFIKANtSYGYSSLADIQALTKM-KEKLINHMLVYENYPVDDygkAVDDTTDA-LRITDMEVFEQTNYDFGL 185
Cdd:PRK12467 2945 DWLQQVQAQNLALR-EFEHTPLADIQRWAGQgGEALFDSILVFENYPISE---ALKQGAPSgLRFGAVSSREQTNYPLTL 3020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 186 VIIPGSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDI-SAVNEEERGMLQEFNKQSSNYTVNKTIQDL 264
Cdd:PRK12467 3021 AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELpTLAAHERRQVLHAWNATAAAYPSERLVHQL 3100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 265 FEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESP 344
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 345 VSRINHILKDSKADILITDLCFLADKNIAAECLDIT-DKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNK 423
Cdd:PRK12467 3181 RERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTlDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHG 3260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 424 SLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYlHSLSLIEYIHKNSITYLKMTPTLFS 503
Cdd:PRK12467 3261 ALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQ 3339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 504 TLMEDVDMlASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDhiQNCE-IYNKIGRPIH 582
Cdd:PRK12467 3340 QFAEDAGG-ADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGD--AVCEaPYAPIGRPVA 3416
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 583 GINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFH-PGAKMYKTGDLGRWMPDGNIEFLGRIDNQ 661
Cdd:PRK12467 3417 GRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQ 3496
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 662 IKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE---KYLSAYITGDIEME--GSFVQEKLAQALPKYMIPSFIIQLKELP 736
Cdd:PRK12467 3497 VKIRGFRIELGEIEARLLQHPSVREAVVLARDGaggKQLVAYVVPADPQGdwRETLRDHLAASLPDYMVPAQLLVLAAMP 3576
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 737 LTANGKINRKELPLPDLQRLSvpRYEAPANETEEKLAEIWKEMLGHKRISINEDFFELGGHSLTAAFTISRIRKTFGTDI 816
Cdd:PRK12467 3577 LGPNGKVDRKALPDPDAKGSR--EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKL 3654
|
810 820 830
....*....|....*....|....*....|....*
gi 2085927195 817 KVKELFEQPTIKQLSRLIQKRDKQNYPVISKARKQ 851
Cdd:PRK12467 3655 SLRDLMSAPTIAELAGYSPLGDVPVNLLLDLNRLE 3689
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-849 |
1.51e-167 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 546.09 E-value: 1.51e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 27 IDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGIEKMVGLFINAVPLRVKGDGDTVF 106
Cdd:PRK12316 4320 LDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSV 4399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 107 IALAQKLNSDFIKANtSYGYSSLADIQALTKMK-EKLINHMLVYENYPVDDygkAVDDTTDA-LRITDMEVFEQTNYDFG 184
Cdd:PRK12316 4400 VEWLQQVQRQNLALR-EHEHTPLYEIQRWAGQGgEALFDSLLVFENYPVSE---ALQQGAPGgLRFGEVTNHEQTNYPLT 4475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 185 LVIIPGSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERG-MLQEFNKQSSNYTVNKTIQD 263
Cdd:PRK12316 4476 LAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQrIVALWNRTDAGYPATRCVHQ 4555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 264 LFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDES 343
Cdd:PRK12316 4556 LVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 344 PVSRINHILKDSKADILITDLCFLADKNIAA--ECLDITDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVK 421
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQSHLLQRLPIPDglASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVS 4715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 422 NKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLhSLSLIEYIHKNSITYLKMTPTL 501
Cdd:PRK12316 4716 HGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWD-PERLYAEIHEHRVTVLVFPPVY 4794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 502 FSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIdLDHIQNCEIYNKIGRPI 581
Cdd:PRK12316 4795 LQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKA-RDGDACGAAYMPIGTPL 4873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 582 HGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGDLGRWMPDGNIEFLGRIDN 660
Cdd:PRK12316 4874 GNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDH 4953
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 661 QIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIE---EKYLSAYIT-------GDIEMEGSFVQE---KLAQALPKYMIPS 727
Cdd:PRK12316 4954 QVKIRGFRIELGEIEARLREHPAVREAVVIAQEgavGKQLVGYVVpqdpalaDADEAQAELRDElkaALRERLPEYMVPA 5033
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 728 FIIQLKELPLTANGKINRKELPLPD---LQRLsvprYEAPANETEEKLAEIWKEMLGHKRISINEDFFELGGHSLTAAFT 804
Cdd:PRK12316 5034 HLVFLARMPLTPNGKLDRKALPQPDaslLQQA----YVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 2085927195 805 ISRIRKTFGTDIKVKELFEQPTIKQLSRLIQKRDKQNYPVISKAR 849
Cdd:PRK12316 5110 TSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLE 5154
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-1015 |
1.37e-161 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 528.76 E-value: 1.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 25 FIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcRVQgIEKMVGLFINAVPLRVKGDGDT 104
Cdd:PRK12316 275 FSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRN-RAE-VEGLIGFFVNTQVLRSVFDGRT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 105 VFIALAQKLNsdfikaNTSYGYSSLADI---QALTKMK-EKLINH----MLVYENYP-VDDYGKAvdDTTDALRITDMEV 175
Cdd:PRK12316 353 RVATLLAGVK------DTVLGAQAHQDLpfeRLVEALKvERSLSHsplfQVMYNHQPlVADIEAL--DTVAGLEFGQLEW 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 176 FEQT-NYDFGL-VIIPGSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERG-MLQEFNKQS 252
Cdd:PRK12316 425 KSRTtQFDLTLdTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGqLVEGWNATA 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 253 SNYTVNKTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKT 332
Cdd:PRK12316 505 AEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKA 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 333 GSAFLPIDDESPVSRINHILKDSKADILITDlCFLADK---NIAAECLDITDKSIYTS-QNTSNPDVQYDLEDEVYVIYT 408
Cdd:PRK12316 585 GGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ-SHLGRKlplAAGVQVLDLDRPAAWLEgYSEENPGTELNPENLAYVIYT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 409 SGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIH 488
Cdd:PRK12316 664 SGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELIN 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 489 KNSITYLKMTPTLFSTLMEDVDmLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGcIAHSIDLDHI 568
Cdd:PRK12316 744 REGVDTLHFVPSMLQAFLQDED-VASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAID-VTHWTCVEEG 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 569 QNCEiynKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMP 648
Cdd:PRK12316 822 GDSV---PIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRA 898
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 649 DGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITgdIEMEGSFVQEKLAQA----LPKYM 724
Cdd:PRK12316 899 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVV--LESEGGDWREALKAHlaasLPEYM 976
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 725 IPSFIIQLKELPLTANGKINRKELPLPDlqrLSVPR--YEAPANETEEKLAEIWKEMLGHKRISINEDFFELGGHSLTAA 802
Cdd:PRK12316 977 VPAQWLALERLPLTPNGKLDRKALPAPE---ASVAQqgYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSI 1053
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 803 FTISRIRKTfGTDIKVKELFEQPTIKQLSRlIQKRDKQNypVISKARKQSYYQASSAQKRMFALWETDKDSivYNLPIMI 882
Cdd:PRK12316 1054 QVVSRARQA-GIQLSPRDLFQHQTIRSLAL-VAKAGQAT--AADQGPASGEVALAPVQRWFFEQAIPQRQH--WNQSLLL 1127
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 883 ELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEFDYQKLPSD--GIRPYVKQFIRPFHLDKSPLIR 960
Cdd:PRK12316 1128 QARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASeeELLALCEEAQRSLDLEQGPLLR 1207
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 961 AGLITYED-RNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQPPlQSKDYSEW 1015
Cdd:PRK12316 1208 ALLVDMADgSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPA-RTSSYQAW 1262
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-1016 |
1.15e-159 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 523.37 E-value: 1.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 27 IDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKMVGLFINAVPLRVKGDGDTVF 106
Cdd:PRK12316 2826 LDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN--RAETERLIGFFVNTQVLRAQVDAQLAF 2903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 107 IALAQKLNSDFIKANTSYGYSSLADIQALTKMK----EKLINHMLVYENYPVddyGKAVDDTTDALRITDMEVFEQTNYD 182
Cdd:PRK12316 2904 RDLLGQVKEQALGAQAHQDLPFEQLVEALQPERslshSPLFQVMYNHQSGER---AAAQLPGLHIESFAWDGAATQFDLA 2980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 183 FGLVIIPGSqIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERG-MLQEFNKQSSNYTVNKTI 261
Cdd:PRK12316 2981 LDTWESAEG-LGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGqLLEAWNATAAEYPLERGV 3059
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 262 QDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDD 341
Cdd:PRK12316 3060 HRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDP 3139
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 342 ESPVSRINHILKDSKADILITD--LCFLADKNIAAECLDITDKSIytsqNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVK 419
Cdd:PRK12316 3140 EYPEERLAYMLEDSGAQLLLSQshLRLPLAQGVQVLDLDRGDENY----AEANPAIRTMPENLAYVIYTSGSTGKPKGVG 3215
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 420 VKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTP 499
Cdd:PRK12316 3216 IRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYP 3295
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 TLFSTLMEDVDMlASCPDLKVIILGGESINIGNVKKLAEKcrwMKFINHYGPTESTVGCIAHSIDLDHiqncEIYNKIGR 579
Cdd:PRK12316 3296 SMLQAFLEEEDA-HRCTSLKRIVCGGEALPADLQQQVFAG---LPLYNLYGPTEATITVTHWQCVEEG----KDAVPIGR 3367
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 580 PIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRID 659
Cdd:PRK12316 3368 PIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVD 3447
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 660 NQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEmEGSF---VQEKLAQALPKYMIPSFIIQLKELP 736
Cdd:PRK12316 3448 HQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDE-AGDLreaLKAHLKASLPEYMVPAHLLFLERMP 3526
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 737 LTANGKINRKELPLPDLQrLSVPRYEAPANETEEKLAEIWKEMLGHKRISINEDFFELGGHSLTAAFTISRIRKTfGTDI 816
Cdd:PRK12316 3527 LTPNGKLDRKALPRPDAA-LLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQA-GIRF 3604
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 817 KVKELFEQPTIKQLSRLIQKRDKQNY---PVIS----KARKQSYYQASSAQKRMfalwetdkdsivYNLPIMIELNGKLD 889
Cdd:PRK12316 3605 TPKDLFQHQTIQGLARVARVGGGVAVdqgPVSGetllLPIQQQFFEEPVPERHH------------WNQSLLLKPREALD 3672
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 890 VKKAESVLQEIIGRHEALRTSFdvVSDDvvqiihDTWELEFDYQKLPSD-----------GIRPYVKQFIRPFHLDKSPL 958
Cdd:PRK12316 3673 AAALEAALQALVEHHDALRLRF--VEDA------GGWTAEHLPVELGGAllwraelddaeELERLGEEAQRSLDLADGPL 3744
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 959 IRAGLITYED-RNLLLLDVHHIAADGVSVGIIRKEFNALYA----GHKLKQP--PLQSKDYSEWQ 1016
Cdd:PRK12316 3745 LRALLATLADgSQRLLLVIHHLVVDGVSWRILLEDLQQAYQqllqGEAPRLPakTSSFKAWAERL 3809
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
263-748 |
7.27e-155 |
|
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: 467.06 E-value: 7.27e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 263 DLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDE 342
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 343 SPVSRINHILKDSKADILITDLcflADKNIAAECLD--ITDKSIYTsQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKV 420
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDR---SLAGRAGGLEVavVIDEALDA-GPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 421 KNKSLVnySLwVCDQ--ININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMT 498
Cdd:cd12117 157 THRGVV--RL-VKNTnyVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 499 PTLFSTLM-EDVDMLAScpdLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHIQNCEIynKI 577
Cdd:cd12117 234 AALFNQLAdEDPECFAG---LRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSI--PI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 578 GRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGR 657
Cdd:cd12117 309 GRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 658 IDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIE----EKYLSAYITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLK 733
Cdd:cd12117 389 IDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREdaggDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLD 468
|
490
....*....|....*
gi 2085927195 734 ELPLTANGKINRKEL 748
Cdd:cd12117 469 ELPLTANGKVDRRAL 483
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-1014 |
1.73e-153 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 505.08 E-value: 1.73e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 4 SSKPVFQSSAD-----EGGFNNRKKTFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQc 78
Cdd:PRK12467 1314 GEQPVLELPTDrprpaVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRN- 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 79 RVQgIEKMVGLFINAVPLRVKGDGDTVFIALAQKLNSDFIKANtsyGYSSLADIQALTKMK-EKLINHMLVYE---NYPV 154
Cdd:PRK12467 1393 RAE-TEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQ---AHQDLPFEQLVEALQpERSLSHSPLFQvmfNHQR 1468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 155 DDygKAVDDTTDALRITDMEVFEQT-NYDFGLVIIPGSQ-IKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLK 232
Cdd:PRK12467 1469 DD--HQAQAQLPGLSVESLSWESQTaQFDLTLDTYESSEgLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLG 1546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 233 DISAVNEEER-GMLQEFNKQSSNYTVNKTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSI 311
Cdd:PRK12467 1547 ELDLLDEAERrQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVL 1626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 312 TAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDLCFLADKNIAA--ECLDITDKSIYTS-Q 388
Cdd:PRK12467 1627 VGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDglRSLVLDQEDDWLEgY 1706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 389 NTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQ 468
Cdd:PRK12467 1707 SDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGAR 1786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 469 VHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINH 548
Cdd:PRK12467 1787 LVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNL 1866
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 549 YGPTESTVGcIAHSIdLDHIQNCE-IYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFI 627
Cdd:PRK12467 1867 YGPTETAVD-VTHWT-CRRKDLEGrDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFV 1944
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 628 DNPF-HPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE---KYLSAY-IT 702
Cdd:PRK12467 1945 ADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGangKQLVAYvVP 2024
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 703 GDIEMEGSFV---------QEKLAQALPKYMIPSFIIQLKELPLTANGKINRKELPLPDLQRLSvPRYEAPANETEEKLA 773
Cdd:PRK12467 2025 TDPGLVDDDEaqvalrailKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQ-QAYVAPQSELEQRLA 2103
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 774 EIWKEMLGHKRISINEDFFELGGHSLTAAFTISRIRKTfGTDIKVKELFEQPTIKQLSRLIQKRDKQnyPVISKARKQSY 853
Cdd:PRK12467 2104 AIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDGT--VSIDQGPVTGD 2180
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 854 YQASSAQKRMFAlwetdkDSIV----YNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFdVVSDDVVQIIHDTWELE 929
Cdd:PRK12467 2181 LPLLPIQQMFFA------DDIPerhhWNQSVLLEPREALDAELLEAALQALLVHHDALRLGF-VQEDGGWSAMHRAPEQE 2253
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 930 FD---YQKLPSDG--IRPYVKQFIRPFHLDKSPLIRAGLITYED-RNLLLLDVHHIAADGVSVGIIRKE----FNALYAG 999
Cdd:PRK12467 2254 RRpllWQVVVADKeeLEALCEQAQRSLDLEEGPLLRAVLATLPDgSQRLLLVIHHLVVDGVSWRILLEDlqtaYRQLQGG 2333
|
1050
....*....|....*..
gi 2085927195 1000 HKLKQPPLQS--KDYSE 1014
Cdd:PRK12467 2334 QPVKLPAKTSafKAWAE 2350
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-1016 |
4.96e-153 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 503.93 E-value: 4.96e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 27 IDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKMVGLFINAVPLRVKGDGDTVF 106
Cdd:PRK05691 903 VDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRP--RLETQGLVGFFINTQVLRAQLDGRLPF 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 107 IAL--AQKLNSDFIKANTSYGYSSLadIQALTKMKEK-LINHMLVYENypvddygkavDDTTDALRITDMEVFE------ 177
Cdd:PRK05691 981 TALlaQVRQATLGAQAHQDLPFEQL--VEALPQAREQgLFQVMFNHQQ----------RDLSALRRLPGLLAEElpwhsr 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 178 QTNYDFGLVIIPGSQ--IKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERGMLQEFNkQSSNY 255
Cdd:PRK05691 1049 EAKFDLQLHSEEDRNgrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWG-QAPCA 1127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 256 TVNKTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSA 335
Cdd:PRK05691 1128 PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGA 1207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 336 FLPIDDESPVSRINHILKDSKADILITDLCFLAD----KNIAAECLDITDKSIYTSQntsNPDVQYDLEDEVYVIYTSGT 411
Cdd:PRK05691 1208 YVPLDPDYPAERLAYMLADSGVELLLTQSHLLERlpqaEGVSAIALDSLHLDSWPSQ---APGLHLHGDNLAYVIYTSGS 1284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 412 SGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIF-PVLSGGGQVHFVDKEvYLHSLSLIEYIHKN 490
Cdd:PRK05691 1285 TGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFwPLITGCRLVLAGPGE-HRDPQRIAELVQQY 1363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 491 SITYLKMTPTLFSTLMEDVDmLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTEStvgciahSIDLDHIQn 570
Cdd:PRK05691 1364 GVTTLHFVPPLLQLFIDEPL-AAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTET-------AINVTHWQ- 1434
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 571 CEI----YNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGDLGR 645
Cdd:PRK05691 1435 CQAedgeRSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRAR 1514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 646 WMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE---KYLSAYITGD--IEMEGSFVQEKLAQAL 720
Cdd:PRK05691 1515 WNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGaagAQLVGYYTGEagQEAEAERLKAALAAEL 1594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 721 PKYMIPSFIIQLKELPLTANGKINRKELPLPDLQRlsvPRYEAPANETEEKLAEIWKEMLGHKRISINEDFFELGGHSLT 800
Cdd:PRK05691 1595 PEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ---REHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLL 1671
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 801 AAFTISRIRKTFGTDIKVKELFEQPTI----KQLSRLIQKRDKQNYPVISKARKQSYYQASSAQKRMFALWETDKDSIVY 876
Cdd:PRK05691 1672 ATQIVSRTRQACDVELPLRALFEASELgafaEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAY 1751
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 877 NLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEFDYQ---KLPSDGIRPYVKQFI----- 948
Cdd:PRK05691 1752 NVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQdfsALPADARQQRLQQLAdseah 1831
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 949 RPFHLDKSPLIRAGLITYEDR-NLLLLDVHHIAADGVSVGIIRKEFNALYAG------HKLKQPPLQSKDYSEWQ 1016
Cdd:PRK05691 1832 QPFDLERGPLLRACLVKAAEReHYFVLTLHHIVTEGWAMDIFARELGALYEAflddreSPLEPLPVQYLDYSVWQ 1906
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
272-749 |
1.27e-137 |
|
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: 422.27 E-value: 1.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 272 TPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHI 351
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 352 LKDSKADILITDLcFLADKNIAAECLDITDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLW 431
Cdd:cd17656 81 MLDSGVRVVLTQR-HLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 432 VCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDM 511
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 512 LASCPD-LKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVgCIAHSID-LDHIQNceiYNKIGRPIHGINIYIV 589
Cdd:cd17656 240 INRFPTcVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINpEAEIPE---LPPIGKPISNTWIYIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 590 DRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRV 669
Cdd:cd17656 316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 670 EIGEIENQLLQLEGIKEAAVVYIE----EKYLSAYITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINR 745
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
....
gi 2085927195 746 KELP 749
Cdd:cd17656 476 KALP 479
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
260-749 |
6.60e-137 |
|
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: 419.92 E-value: 6.60e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI 339
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILITdlcfladkniaaeclditdksiytsqntsNPdvqydlEDEVYVIYTSGTSGKPKGVK 419
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT-----------------------------QP------ENLAYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 420 VKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTP 499
Cdd:cd17644 126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 TLFSTLMEDV--DMLASCPDLKVIILGGESINIGNVKKLAEKCR-WMKFINHYGPTESTVGCIAHSIDLDHIQNceIYN- 575
Cdd:cd17644 206 AYWHLLVLELllSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGnFIQLINVYGPTEATIAATVCRLTQLTERN--ITSv 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 576 KIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFH--PGAKMYKTGDLGRWMPDGNIE 653
Cdd:cd17644 284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 654 FLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE----KYLSAYITGDIEMEGSFV--QEKLAQALPKYMIPS 727
Cdd:cd17644 364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqpgnKRLVAYIVPHYEESPSTVelRQFLKAKLPDYMIPS 443
|
490 500
....*....|....*....|..
gi 2085927195 728 FIIQLKELPLTANGKINRKELP 749
Cdd:cd17644 444 AFVVLEELPLTPNGKIDRRALP 465
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
286-689 |
1.62e-136 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 416.67 E-value: 1.62e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVA-TLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDL 364
Cdd:TIGR01733 1 TYRELDERANRLArHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 365 CF---LADKNIAAECLDITD-KSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININS 440
Cdd:TIGR01733 81 ALasrLAGLVLPVILLDPLElAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 441 DSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEY-IHKNSITYLKMTPTLFSTLMEDVdmLASCPDLK 519
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAAlIAEHPVTVLNLTPSLLALLAAAL--PPALASLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 520 VIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHIQNCEIYNkIGRPIHGINIYIVDRSDQLVPVG 599
Cdd:TIGR01733 239 LVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVP-IGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 600 APGEICISGVGLASGYVNNEELTNEKFIDNPFHP--GAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQ 677
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 2085927195 678 LLQLEGIKEAAV 689
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
264-749 |
3.22e-136 |
|
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: 416.96 E-value: 3.22e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 264 LFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDES 343
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 344 PVSRINHILKDSKADILITdlcfladkniaaeclditdksiytsqntsnpdvqyDLEDEVYVIYTSGTSGKPKGVKVKNK 423
Cdd:cd17645 83 PGERIAYMLADSSAKILLT-----------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 424 SLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITyLKMTPTLFS 503
Cdd:cd17645 128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPTGAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 504 TLMEDVDMLAscpdLKVIILGGESInignvKKLAEKCrwMKFINHYGPTESTVGCIAHSIDLDHiQNCeiynKIGRPIHG 583
Cdd:cd17645 207 EQFMQLDNQS----LRVLLTGGDKL-----KKIERKG--YKLVNNYGPTENTVVATSFEIDKPY-ANI----PIGKPIDN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 584 INIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIK 663
Cdd:cd17645 271 TRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 664 IRGFRVEIGEIENQLLQLEGIKEAAVVYIEE----KYLSAYITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTA 739
Cdd:cd17645 351 IRGYRIEPGEIEPFLMNHPLIELAAVLAKEDadgrKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTA 430
|
490
....*....|
gi 2085927195 740 NGKINRKELP 749
Cdd:cd17645 431 NGKVDRKALP 440
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
265-749 |
4.94e-135 |
|
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: 415.97 E-value: 4.94e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 265 FEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESP 344
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 345 VSRINHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKS 424
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 425 LVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFST 504
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 505 LMEDVDML-ASCPDLKVIILGGESINIGnvKKLAEKCRWMKF---INHYGPTESTVgCIAHSIDLDHIQNCEIyNKIGRP 580
Cdd:cd17651 241 LAEHGRPLgVRLAALRYLLTGGEQLVLT--EDLREFCAGLPGlrlHNHYGPTETHV-VTALSLPGDPAAWPAP-PPIGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 581 IHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDN 660
Cdd:cd17651 317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 661 QIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIE----EKYLSAYITGDIEMEGSFV--QEKLAQALPKYMIPSFIIQLKE 734
Cdd:cd17651 397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREdrpgEKRLVAYVVGDPEAPVDAAelRAALATHLPEYMVPSAFVLLDA 476
|
490
....*....|....*
gi 2085927195 735 LPLTANGKINRKELP 749
Cdd:cd17651 477 LPLTPNGKLDRRALP 491
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
263-748 |
4.09e-126 |
|
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: 392.41 E-value: 4.09e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 263 DLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDE 342
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 343 SPVSRINHILKDSKADILITDLCfLADKNIAAECLDITDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKN 422
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTTAD-LAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 423 KSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIF-PVLSGGGQV------HfVDKEvYLHSLslieyIHKNSITYL 495
Cdd:cd17646 161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFwPLVAGARLVvarpggH-RDPA-YLAAL-----IREHGVTTC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 496 KMTPTLFSTLMEDVDmLASCPDLKVIILGGESINIGnvkkLAEKCRWM---KFINHYGPTESTVGCIAHSIDLDHIqncE 572
Cdd:cd17646 234 HFVPSMLRVFLAEPA-AGSCASLRRVFCSGEALPPE----LAARFLALpgaELHNLYGPTEAAIDVTHWPVRGPAE---T 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 573 IYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNI 652
Cdd:cd17646 306 PSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 653 EFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV----YIEEKYLSAYITGDIEMEG---SFVQEKLAQALPKYMI 725
Cdd:cd17646 386 EFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVaraaPAGAARLVGYVVPAAGAAGpdtAALRAHLAERLPEYMV 465
|
490 500
....*....|....*....|...
gi 2085927195 726 PSFIIQLKELPLTANGKINRKEL 748
Cdd:cd17646 466 PAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
261-748 |
3.75e-125 |
|
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: 389.59 E-value: 3.75e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 261 IQDLFEERAEKTPDQTAaVYA-GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI 339
Cdd:cd05918 1 VHDLIEERARSQPDAPA-VCAwDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILItdlcfladkniaaeclditdksiytsqnTSNPDvqydleDEVYVIYTSGTSGKPKGVK 419
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVL----------------------------TSSPS------DAAYVIFTSGSTGKPKGVV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 420 VKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVhFVDKEVYLHSlSLIEYIHKNSITYLKMTP 499
Cdd:cd05918 126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCL-CIPSEEDRLN-DLAGFINRLRVTWAFLTP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 TLFSTLmedvdMLASCPDLKVIILGGESINIGNVKKLAEKCRwmkFINHYGPTESTVGCIAHSIDLD-HIQNceiynkIG 578
Cdd:cd05918 204 SVARLL-----DPEDVPSLRTLVLGGEALTQSDVDTWADRVR---LINAYGPAECTIAATVSPVVPStDPRN------IG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 579 RPIhGINIYIVDRSD--QLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNP-------FHPGAKMYKTGDLGRWMPD 649
Cdd:cd05918 270 RPL-GATCWVVDPDNhdRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 650 GNIEFLGRIDNQIKIRGFRVEIGEIENQLLQ-LEGIKEAAVVYI------EEKYLSAYITGDIEMEGS------------ 710
Cdd:cd05918 349 GSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVkpkdgsSSPQLVAFVVLDGSSSGSgdgdslflepsd 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2085927195 711 -------FVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05918 429 efralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
273-748 |
7.26e-125 |
|
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: 387.59 E-value: 7.26e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILITDlcfladkniaaeclditdksiytsqntsnPdvqydlEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWV 432
Cdd:cd17650 81 EDSGAKLLLTQ-----------------------------P------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 433 CDQININSDS-RSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDM 511
Cdd:cd17650 126 RREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 512 LA-SCPDLKVIILGGESINIGNVKKLAEKCRW-MKFINHYGPTESTVGCIAHSIDLDHIqnCEIYN-KIGRPIHGINIYI 588
Cdd:cd17650 206 NGlDLSAMRLLIVGSDGCKAQDFKTLAARFGQgMRIINSYGVTEATIDSTYYEEGRDPL--GDSANvPIGRPLPNTAMYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 589 VDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFR 668
Cdd:cd17650 284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 669 VEIGEIENQLLQLEGIKEAAVVYIE----EKYLSAYITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKIN 744
Cdd:cd17650 364 IELGEIESQLARHPAIDEAVVAVREdkggEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
....
gi 2085927195 745 RKEL 748
Cdd:cd17650 444 RRAL 447
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
273-748 |
1.27e-122 |
|
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: 382.04 E-value: 1.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILITDlcfladkniaaeclditdksiytsqntsnPDvqydleDEVYVIYTSGTSGKPKGVKVKNKSLVNYsLWV 432
Cdd:cd17643 81 ADSGPSLLLTD-----------------------------PD------DLAYVIYTSGSTGRPKGVVVSHANVLAL-FAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 433 CDQI-NINSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLME-DVD 510
Cdd:cd17643 125 TQRWfGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaADR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 511 MLASCPDLKVIILGGESINIGNVKKLAEKCRWMK--FINHYGPTESTVGCIAHSIDLDHIQNCEIYNkIGRPIHGINIYI 588
Cdd:cd17643 205 DGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRpqLVNMYGITETTVHVTFRPLDAADLPAAAASP-IGRPLPGLRVYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 589 VDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFH-PGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGF 667
Cdd:cd17643 284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 668 RVEIGEIENQLLQLEGIKEAAVVYIE----EKYLSAYITGDIEMEG--SFVQEKLAQALPKYMIPSFIIQLKELPLTANG 741
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVIVREdepgDTRLVAYVVADDGAAAdiAELRALLKELLPDYMVPARYVPLDALPLTVNG 443
|
....*..
gi 2085927195 742 KINRKEL 748
Cdd:cd17643 444 KLDRAAL 450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
273-749 |
1.81e-122 |
|
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: 380.83 E-value: 1.81e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILITDLCFLAdkniaaeclditdksiytsqntsnpdvqydledevYVIYTSGTSGKPKGVKVKNKSLVNYSLWV 432
Cdd:cd17652 81 ADARPALLLTTPDNLA-----------------------------------YVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 433 CDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDvdml 512
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPD---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 513 aSCPDLKVIILGGESINIGNVKKLAEKCRwmkFINHYGPTESTVGCIAHSIDLDhiqncEIYNKIGRPIHGINIYIVDRS 592
Cdd:cd17652 202 -DLPDLRTLVVAGEACPAELVDRWAPGRR---MINAYGPTETTVCATMAGPLPG-----GGVPPIGRPVPGTRVYVLDAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 593 DQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEI 671
Cdd:cd17652 273 LRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 672 GEIENQLLQLEGIKEAAVVYIEE----KYLSAYITGDIE--MEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINR 745
Cdd:cd17652 353 GEVEAALTEHPGVAEAVVVVRDDrpgdKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
....
gi 2085927195 746 KELP 749
Cdd:cd17652 433 RALP 436
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
261-748 |
2.07e-121 |
|
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: 378.58 E-value: 2.07e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 261 IQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPID 340
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 341 DESPVSRINHILKDSKADILITdlcfladkniaaeclditdksiytsqntsnpdvqyDLEDEVYVIYTSGTSGKPKGVKV 420
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 421 KNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDkevylHSLSLIEYIHKNSITYLKMTPT 500
Cdd:cd12115 126 EHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 501 LFSTLMEdVDMLAscPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHIQNCeiynKIGRP 580
Cdd:cd12115 201 AAAELLR-HDALP--ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEV----SIGRP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 581 IHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDN 660
Cdd:cd12115 274 LANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 661 QIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIE----EKYLSAYITGDIEMEGSF--VQEKLAQALPKYMIPSFIIQLKE 734
Cdd:cd12115 354 QVKVRGFRIELGEIEAALRSIPGVREAVVVAIGdaagERRLVAYIVAEPGAAGLVedLRRHLGTRLPAYMVPSRFVRLDA 433
|
490
....*....|....
gi 2085927195 735 LPLTANGKINRKEL 748
Cdd:cd12115 434 LPLTPNGKIDRSAL 447
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
46-834 |
2.01e-120 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 399.42 E-value: 2.01e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 46 LSALIqTAWgvlLQKYNNVNDVVFGAVISGR----QCRVQGiekMVglfINAVPLRVKGDGDTVFIALAQKLNSDFIKA- 120
Cdd:PRK10252 255 ALALV-ALW---LGRLCGRMDYAAGFIFMRRlgsaALTATG---PV---LNVLPLRVHIAAQETLPELATRLAAQLKKMr 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 121 -NTSYGYSSLADIQALTKMKEKL----INHMLVYenYPVDDYGkaVDDTTDALR---ITDMEvfeqtnydFGLVIIPGSQ 192
Cdd:PRK10252 325 rHQRYDAEQIVRDSGRAAGDEPLfgpvLNIKVFD--YQLDFPG--VQAQTHTLAtgpVNDLE--------LALFPDEHGG 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 193 IKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERGMLQEFNkqSSNYTV-NKTIQDLFEERAEK 271
Cdd:PRK10252 393 LSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVN--ATAVEIpETTLSALVAQQAAK 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 272 TPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHI 351
Cdd:PRK10252 471 TPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 352 LKDSKADILITDlcflADKniAAECLDITDKSIYTSQNTSNPDVQYDL-----EDEVYVIYTSGTSGKPKGVKVKNKSLV 426
Cdd:PRK10252 551 LEDARPSLLITT----ADQ--LPRFADVPDLTSLCYNAPLAPQGAAPLqlsqpHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 427 NYSLWVCDQININSDSRSLVTSKYSFDLCYTSIF-PVLSGGGQVhFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTL 505
Cdd:PRK10252 625 NRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFwPFIAGAKLV-MAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAF 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 506 MEDVD---MLASCPDLKVIILGGESINignvkklAEKCR-WMKFI-----NHYGPTESTV---GCIAHSIDLDHIQNCEI 573
Cdd:PRK10252 704 VASLTpegARQSCASLRQVFCSGEALP-------ADLCReWQQLTgaplhNLYGPTEAAVdvsWYPAFGEELAAVRGSSV 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 574 ynKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIE 653
Cdd:PRK10252 777 --PIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVE 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 654 FLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEA---AVVYI-------EEKYLSAYITG------DIEMegsfVQEKLA 717
Cdd:PRK10252 855 YLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINqaaatggDARQLVGYLVSqsglplDTSA----LQAQLR 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 718 QALPKYMIPSFIIQLKELPLTANGKINRKELPLPDLQRLSVPRyeAPANETEEKLAEIWKEMLGHKRISINEDFFELGGH 797
Cdd:PRK10252 931 ERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGR--APKTGTETIIAAAFSSLLGCDVVDADADFFALGGH 1008
|
810 820 830
....*....|....*....|....*....|....*..
gi 2085927195 798 SLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRLI 834
Cdd:PRK10252 1009 SLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLL 1045
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
35-835 |
2.03e-120 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 408.02 E-value: 2.03e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 35 LKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGIEKMVGLFINAVPLRVKGDGDTVFIALAQKLn 114
Cdd:PRK05691 3494 LRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLPAAGQRCSVRQWL- 3572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 115 SDFIKANTS---YGYSSLADIQALTKMK--EKLINHMLVYENYPVD----DYGKAVDDTTDALRItdmevfeQTNYDFGL 185
Cdd:PRK05691 3573 QGLLDSNMElreYEYLPLVAIQECSELPkgQPLFDSLFVFENAPVEvsvlDRAQSLNASSDSGRT-------HTNFPLTA 3645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 186 VIIPGSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERG-MLQEFNKQSSNYTVNKTIQDL 264
Cdd:PRK05691 3646 VCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDfLLDGCNRSERDYPLEQSYVRL 3725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 265 FEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESP 344
Cdd:PRK05691 3726 FEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLP 3805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 345 VSRINHILKDSKADILItdlCFLADKNIAAECLD-----------ITDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSG 413
Cdd:PRK05691 3806 AQRLQRIIELSRTPVLV---CSAACREQARALLDelgcanrprllVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTG 3882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 414 KPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLcytSIFPVLSG---GGQVHFVDKEVYLHSLSLIEYIHKN 490
Cdd:PRK05691 3883 LPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDI---SVWQFLAAplfGARVEIVPNAIAHDPQGLLAHVQAQ 3959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 491 SITYLKMTPTLFS-TLMEDVDMLAScpdLKVIILGGESINignvKKLAEkcRWMK------FINHYGPTESTVGCIAHSI 563
Cdd:PRK05691 3960 GITVLESVPSLIQgMLAEDRQALDG---LRWMLPTGEAMP----PELAR--QWLQrypqigLVNAYGPAECSDDVAFFRV 4030
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 564 DLDHIQNCeiYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGD 642
Cdd:PRK05691 4031 DLASTRGS--YLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGD 4108
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 643 LGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE---KYLSAYIT-GDIEMEGSFVQEKLAQ 718
Cdd:PRK05691 4109 LARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGvngKHLVGYLVpHQTVLAQGALLERIKQ 4188
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 719 ----ALPKYMIPSFIIQLKELPLTANGKINRKELPLPDLQRLSVPRYEAPANETEEKLAEIWKEMLGHKRISINEDFFEL 794
Cdd:PRK05691 4189 rlraELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFEL 4268
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 2085927195 795 GGHSLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRLIQ 835
Cdd:PRK05691 4269 GGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
197-1006 |
2.97e-119 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 404.55 E-value: 2.97e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 197 MTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEEERGMLQE-FNKQSSNYTVNKTIQDLFEERAEKTPDQ 275
Cdd:PRK05691 2125 LTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDsLAGEAGEARLDQTLHGLFAAQAARTPQA 2204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 276 TAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDS 355
Cdd:PRK05691 2205 PALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDS 2284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 356 KADILITDLCFLAD-----KNIAAECLDiTDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSL 430
Cdd:PRK05691 2285 GIGLLLSDRALFEAlgelpAGVARWCLE-DDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQ 2363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 431 WVCDQININSDSRSLVTSKYSFDLCYTSIF-PVLSGG-------GQVhfvDKEvylhslSLIEYIHKNSITYLKMTPTLF 502
Cdd:PRK05691 2364 AVIERFGMRADDCELHFYSINFDAASERLLvPLLCGArvvlraqGQW---GAE------EICQLIREQQVSILGFTPSYG 2434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 503 STLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAhSIDLDHIQNCEIYNKIGRPIH 582
Cdd:PRK05691 2435 SQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLA-CLAPEQLEEGAASVPIGRVVG 2513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 583 GINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGDLGRWMPDGNIEFLGRIDNQ 661
Cdd:PRK05691 2514 ARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFaADGGRLYRTGDLVRLRADGLVEYVGRIDHQ 2593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 662 IKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE---KYLSAYITGDIEMEGSFVQEKLAQA--------LPKYMIPSFII 730
Cdd:PRK05691 2594 VKIRGFRIELGEIESRLLEHPAVREAVVLALDTpsgKQLAGYLVSAVAGQDDEAQAALREAlkahlkqqLPDYMVPAHLI 2673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 731 QLKELPLTANGKINRKELPLPDLQrLSVPRYEAPANETEEKLAEIWKEMLGHKRISINEDFFELGGHSLTAAFTISRIRK 810
Cdd:PRK05691 2674 LLDSLPLTANGKLDRRALPAPDPE-LNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQ 2752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 811 TfGTDIKVKELFEQPTIKQLSRLIQKRDkqnypviSKARKQSYYQASSA----QKRMFalwetdkDSIV-----YNLPIM 881
Cdd:PRK05691 2753 L-GIHFSPRDLFQHQTVQTLAAVATHSE-------AAQAEQGPLQGASGltpiQHWFF-------DSPVpqpqhWNQALL 2817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 882 IELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSddvvqiihDTWELEfdYQKLPSDGI------------RPYVKQFIR 949
Cdd:PRK05691 2818 LEPRQALDPALLEQALQALVEHHDALRLRFSQAD--------GRWQAE--YRAVTAQELlwqvtvadfaecAALFADAQR 2887
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 2085927195 950 PFHLDKSPLIRAGLIT-YEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQPP 1006
Cdd:PRK05691 2888 SLDLQQGPLLRALLVDgPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEP 2945
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
263-748 |
2.26e-118 |
|
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: 370.10 E-value: 2.26e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 263 DLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDE 342
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 343 SPVSRINHILKDSKADILITdlcfladkniaaeclditdksiytsqnTSNPDvqydleDEVYVIYTSGTSGKPKGVKVKN 422
Cdd:cd17653 81 LPSARIQAILRTSGATLLLT---------------------------TDSPD------DLAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 423 KSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSlieyihkNSITYLKMTPTLF 502
Cdd:cd17653 128 RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVA-------RTVDALMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 503 STLMedvdmLASCPDLKVIILGGESINignvKKLAEkcRWMK---FINHYGPTESTVGCIAHSidLDHIQNceiyNKIGR 579
Cdd:cd17653 201 STLS-----PQDFPNLKTIFLGGEAVP----PSLLD--RWSPgrrLYNAYGPTECTISSTMTE--LLPGQP----VTIGK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 580 PIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRID 659
Cdd:cd17653 264 PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGRED 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 660 NQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYIT-GDIEMEGsfVQEKLAQALPKYMIPSFIIQLKELPLT 738
Cdd:cd17653 344 NQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGRLVAFVTpETVDVDG--LRSELAKHLPSYAVPDRIIALDSFPLT 421
|
490
....*....|
gi 2085927195 739 ANGKINRKEL 748
Cdd:cd17653 422 ANGKVDRKAL 431
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
273-748 |
5.75e-114 |
|
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: 359.68 E-value: 5.75e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILITD--LCFLADKNIAAECLDItdksIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSL 430
Cdd:cd12116 81 EDAEPALVLTDdaLPDRLPAGLPVLLLAL----AAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 431 WVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFsTLMEDVD 510
Cdd:cd12116 157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATW-RMLLDAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 511 MLAScPDLKVIIlGGESINIGNVKKLAEKCRwmKFINHYGPTESTVGCIAHSID--LDHIQnceiynkIGRPIHGINIYI 588
Cdd:cd12116 236 WQGR-AGLTALC-GGEALPPDLAARLLSRVG--SLWNLYGPTETTIWSTAARVTaaAGPIP-------IGRPLANTQVYV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 589 VDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGF 667
Cdd:cd12116 305 LDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGH 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 668 RVEIGEIENQLLQLEGIKEAAVVYIEE---KYLSAYITGDIEMEGSF--VQEKLAQALPKYMIPSFIIQLKELPLTANGK 742
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQAAVVVREDggdRRLVAYVVLKAGAAPDAaaLRAHLRATLPAYMVPSAFVRLDALPLTANGK 464
|
....*.
gi 2085927195 743 INRKEL 748
Cdd:cd12116 465 LDRKAL 470
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
273-748 |
9.26e-109 |
|
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: 346.18 E-value: 9.26e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILITDLCfLADKNIAAECLDITDKSiytSQNTS--NPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNysl 430
Cdd:cd12114 81 ADAGARLVLTDGP-DAQLDVAVFDVLILDLD---ALAAPapPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALN--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 431 wVCDQIN----INSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLM 506
Cdd:cd12114 154 -TILDINrrfaVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 507 E-DVDMLASCPDLKVIILGGESINI---GNVKKLAEKCRwmkFINHYGPTESTVGCIAHSIDLDHiqncEIYNKI--GRP 580
Cdd:cd12114 233 DvLEAAQALLPSLRLVLLSGDWIPLdlpARLRALAPDAR---LISLGGATEASIWSIYHPIDEVP----PDWRSIpyGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 581 IHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPfhPGAKMYKTGDLGRWMPDGNIEFLGRIDN 660
Cdd:cd12114 306 LANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 661 QIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI---EEKYLSAYITGDIEMEGSF---VQEKLAQALPKYMIPSFIIQLKE 734
Cdd:cd12114 384 QVKVRGYRIELGEIEAALQAHPGVARAVVVVLgdpGGKRLAAFVVPDNDGTPIApdaLRAFLAQTLPAYMIPSRVIALEA 463
|
490
....*....|....
gi 2085927195 735 LPLTANGKINRKEL 748
Cdd:cd12114 464 LPLTANGKVDRAAL 477
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
269-748 |
3.70e-108 |
|
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: 343.85 E-value: 3.70e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLmeKGAGKNSITAMMI--RPSEYSMIGILGILKTGSAFLPIDDESPVS 346
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAAL--ASLGLDAGDPVVVygHKSPDAIAAFLAALKAGHAYVPLDASSPAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 347 RINHILKDSKADILITDlcfladkniaaeclditdksiytsqntsnpdvqydlEDEV-YVIYTSGTSGKPKGVKVKNKSL 425
Cdd:cd05945 79 RIREILDAAKPALLIAD------------------------------------GDDNaYIIFTSGSTGRPKGVQISHDNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 426 VNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTL 505
Cdd:cd05945 123 VSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 506 MEDVDML-ASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHIQNceiYNK--IGRPIH 582
Cdd:cd05945 203 LLSPTFTpESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDG---YDRlpIGYAKP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 583 GINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIdnpFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQI 662
Cdd:cd05945 280 GAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 663 KIRGFRVEIGEIENQLLQLEGIKEAAVV--YIEEK--YLSAYITGDIEME---GSFVQEKLAQALPKYMIPSFIIQLKEL 735
Cdd:cd05945 357 KLNGYRIELEEIEAALRQVPGVKEAVVVpkYKGEKvtELIAFVVPKPGAEaglTKAIKAELAERLPPYMIPRRFVYLDEL 436
|
490
....*....|...
gi 2085927195 736 PLTANGKINRKEL 748
Cdd:cd05945 437 PLNANGKIDRKAL 449
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
273-749 |
1.42e-104 |
|
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: 334.34 E-value: 1.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILITDlcflADKNIAaeclditdksiytsqntsnpdvqydledevYVIYTSGTSGKPKGVKVKNKSLVNYSLWV 432
Cdd:cd17649 81 EDSGAGLLLTH----HPRQLA------------------------------YVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 433 CDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDML 512
Cdd:cd17649 127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 513 AS--CPDLKVIILGGESINIGNVKK-LAEKCRWmkfINHYGPTESTVGCIAHsidldhiqNCEIYNK-------IGRPIH 582
Cdd:cd17649 207 GDgrPPSLRLYIFGGEALSPELLRRwLKAPVRL---FNAYGPTEATVTPLVW--------KCEAGAAragasmpIGRPLG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 583 GINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGDLGRWMPDGNIEFLGRIDNQ 661
Cdd:cd17649 276 GRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 662 IKIRGFRVEIGEIENQLLQLEGIKEAAVVYIE---EKYLSAYITGDIEMEGSFVQEKLAQA----LPKYMIPSFIIQLKE 734
Cdd:cd17649 356 VKIRGFRIELGEIEAALLEHPGVREAAVVALDgagGKQLVAYVVLRAAAAQPELRAQLRTAlrasLPDYMVPAHLVFLAR 435
|
490
....*....|....*
gi 2085927195 735 LPLTANGKINRKELP 749
Cdd:cd17649 436 LPLTPNGKLDRKALP 450
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
273-749 |
1.57e-102 |
|
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: 328.98 E-value: 1.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGK-NSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHI 351
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 352 LKDSKADILITDLCFLAdkniaaeclditdksiytsqntsnpdvqydledevYVIYTSGTSGKPKGVKVKNKSLVNYSLW 431
Cdd:cd17648 81 LEDTGARVVITNSTDLA-----------------------------------YAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 432 VCDQINI--NSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFStlMEDv 509
Cdd:cd17648 126 LSERYFGrdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQ--QYD- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 510 dmLASCPDLKVIILGGESINIGNVKKLAEKCRwMKFINHYGPTESTVGCIAHSIDLDHIQNceiyNKIGRPIHGINIYIV 589
Cdd:cd17648 203 --LARLPHLKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTVTNHKRFFPGDQRFD----KSLGRPVRNTKCYVL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 590 DRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHP--------GAKMYKTGDLGRWMPDGNIEFLGRIDNQ 661
Cdd:cd17648 276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 662 IKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE---------KYLSAYITGDIEM--EGSFVQEKLAQaLPKYMIPSFII 730
Cdd:cd17648 356 VKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriqKYLVGYYLPEPGHvpESDLLSFLRAK-LPRYMVPARLV 434
|
490
....*....|....*....
gi 2085927195 731 QLKELPLTANGKINRKELP 749
Cdd:cd17648 435 RLEGIPVTINGKLDVRALP 453
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
261-748 |
2.54e-91 |
|
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: 299.03 E-value: 2.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 261 IQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPID 340
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 341 DESPVSRINHILKDSKADILITdlcfladkniaaeclditdksiytsqntsnpdvqydledeVYVIYTSGTSGKPKGVKV 420
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 421 KNKSLVNYSLWVCDQININSDSRSLVTSKYSFDL-CYTSIFPVLSGGGQVHFVDKevyLHSLSLIEYIHKNSITYLKMTP 499
Cdd:COG0318 121 THRNLLANAAAIAAALGLTPGDVVLVALPLFHVFgLTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 TLFSTLMEDVDM----LAScpdLKVIILGGESINIGNVKKLAEKCRWmKFINHYGPTESTVGCIAHSIDLDHiqncEIYN 575
Cdd:COG0318 198 TMLARLLRHPEFarydLSS---LRLVVSGGAPLPPELLERFEERFGV-RIVEGYGLTETSPVVTVNPEDPGE----RRPG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 576 KIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEFL 655
Cdd:COG0318 270 SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 656 GRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYITGDIEMEGSF--VQEKLAQALPKYMIPSFI 729
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGervvAFVVLRPGAELDAeeLRAFLRERLARYKVPRRV 422
|
490
....*....|....*....
gi 2085927195 730 IQLKELPLTANGKINRKEL 748
Cdd:COG0318 423 EFVDELPRTASGKIDRRAL 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
265-665 |
1.36e-90 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 295.76 E-value: 1.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 265 FEERAEKTPDQTA-AVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDES 343
Cdd:pfam00501 1 LERQAARTPDKTAlEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 344 PVSRINHILKDSKADILITDLCFLADKNIAAE----------CLDITDKSIYTSQNTS--------NPDVQYDLEDEVYV 405
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEALgklevvklvlVLDRDPVLKEEPLPEEakpadvppPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 406 IYTSGTSGKPKGVKVKNKSLVN--YSLWVCDQ--ININSDSRSLVTSKYSFDLCYTS-IFPVLSGGGQVHFVDKEVYLHS 480
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVAnvLSIKRVRPrgFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 481 LSLIEYIHKNSITYLKMTPTLFSTLME----DVDMLAScpdLKVIILGGESINIGNVKKLAEKCRWMkFINHYGPTESTV 556
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEagapKRALLSS---LRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 557 GCiahSIDLDHIQNCEIYNKIGRPIHGINIYIVDRSD-QLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPfhpga 635
Cdd:pfam00501 317 VV---TTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDG----- 388
|
410 420 430
....*....|....*....|....*....|
gi 2085927195 636 kMYKTGDLGRWMPDGNIEFLGRIDNQIKIR 665
Cdd:pfam00501 389 -WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
261-748 |
1.27e-86 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 287.95 E-value: 1.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 261 IQDL---FEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSitAMMI--RPSEYSMIGILGILKTGSA 335
Cdd:PRK04813 1 IMDIietIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKS--PIIVfgHMSPEMLATFLGAVKAGHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 336 FLPIDDESPVSRINHILKDSKADILItdlcfladkNIAAECLDITDKSIYTSQNTSN---PDVQYDLE------DEVYVI 406
Cdd:PRK04813 79 YIPVDVSSPAERIEMIIEVAKPSLII---------ATEELPLEILGIPVITLDELKDifaTGNPYDFDhavkgdDNYYII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 407 YTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEY 486
Cdd:PRK04813 150 FTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 487 IHKNSITYLKMTPTLfstlmedVDMlasC-----------PDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTEST 555
Cdd:PRK04813 230 LPQLPINVWVSTPSF-------ADM---ClldpsfneehlPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEAT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 556 VGCIAHSIDLDHIQNceiYNK--IGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDnpfHP 633
Cdd:PRK04813 300 VAVTSIEITDEMLDQ---YKRlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 634 GAKMYKTGDLGRwMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV--YIEEK--YLSAYI---TGDIE 706
Cdd:PRK04813 374 GQPAYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVpyNKDHKvqYLIAYVvpkEEDFE 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2085927195 707 MEGSF---VQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK04813 453 REFELtkaIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
266-748 |
2.46e-80 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 270.86 E-value: 2.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 266 EERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPV 345
Cdd:TIGR01734 7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 346 SRINHILKDSKADILIT----DLCFLADKNIAAECLDitdkSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVK 421
Cdd:TIGR01734 87 ERIEMIIEAAGPELVIHtaelSIDAVGTQIITLSALE----QAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 422 NKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTL 501
Cdd:TIGR01734 163 HDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 502 fstlmedVDMlasC-----------PDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHI-Q 569
Cdd:TIGR01734 243 -------VDM---ClldpnfnqenyPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILdQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 570 NCEIYNKIGRPihGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIdnpFHPGAKMYKTGDLGRwMPD 649
Cdd:TIGR01734 313 YPRLPIGFAKP--DMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 650 GNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEK-----YLSAYI---TGDIEMEGSF---VQEKLAQ 718
Cdd:TIGR01734 387 GQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKdhkveYLIAAIvpeTEDFEKEFQLtkaIKKELKK 466
|
490 500 510
....*....|....*....|....*....|
gi 2085927195 719 ALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:TIGR01734 467 SLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
168-836 |
3.52e-72 |
|
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: 262.31 E-value: 3.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 168 LRITDMEVFEQTNY------DFGLVIIPGS-QIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDISAVNEE 240
Cdd:TIGR03443 138 LAFQDAPDNQQTTYstgsttDLTVFLTPSSpELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 241 ERGMLQE--FNKQSSNYTvnKTIQDLFEERAEKTPDQTAAV-------YAGKH--ITYKELNEKANQVATLLMEKGAGKN 309
Cdd:TIGR03443 218 QKSLLPDptKDLDWSGFR--GAIHDIFADNAEKHPDRTCVVetpsfldPSSKTrsFTYKQINEASNILAHYLLKTGIKRG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 310 SItaMMIrpseYS------MIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILIT-----DLCFLADKNIAAE--- 375
Cdd:TIGR03443 296 DV--VMI----YAyrgvdlVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIViekagTLDQLVRDYIDKElel 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 376 -----CLDITDKSIYT-------SQNTSNPDVQYDlEDEVYVI----------YTSGTSGKPKGVKVKNKSLVNYSLWVC 433
Cdd:TIGR03443 370 rteipALALQDDGSLVggsleggETDVLAPYQALK-DTPTGVVvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 434 DQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDmlA 513
Cdd:TIGR03443 449 KRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQAT--T 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 514 SCPDLKviilggESINIGNV---------KKLAEKCRwmkFINHYGPTE-----STVGCIAHSIDLDHIQNCEIYNKIGR 579
Cdd:TIGR03443 527 PIPSLH------HAFFVGDIltkrdclrlQTLAENVC---IVNMYGTTEtqravSYFEIPSRSSDSTFLKNLKDVMPAGK 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 580 PIHGINIYIVDRSD--QLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-------------HPGAK-------- 636
Cdd:TIGR03443 598 GMKNVQLLVVNRNDrtQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkenNKPERefwlgprd 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 637 -MYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEaAVVYI-----EEKYLSAYI--------- 701
Cdd:TIGR03443 678 rLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRE-NVTLVrrdkdEEPTLVSYIvpqdksdel 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 702 -----------TGDIEMEGSF--------VQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKELPLPDLQRLS-VPRY 761
Cdd:TIGR03443 757 eefksevddeeSSDPVVKGLIkyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAaVAKN 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 762 EAPA------NETEEKLAEIWKEMLGHK--RISINEDFFELGGHSLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRL 833
Cdd:TIGR03443 837 RSASaadeefTETEREIRDLWLELLPNRpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKE 916
|
...
gi 2085927195 834 IQK 836
Cdd:TIGR03443 917 VDR 919
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
7-227 |
4.88e-69 |
|
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: 237.10 E-value: 4.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 7 PVFQSSADEGGFNNRKKTFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGIEKM 86
Cdd:cd19543 205 PKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETM 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 87 VGLFINAVPLRVKGDGDTVFIALAQKLNSDFIKANtSYGYSSLADIQALTKMKEKLINHMLVYENYPVDDyGKAVDDTTD 166
Cdd:cd19543 285 VGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELR-EHEYVPLYEIQAWSEGKQALFDHLLVFENYPVDE-SLEEEQDED 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 167 ALRITDMEVFEQTNYDFGLVIIPGSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19543 363 GLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
401-743 |
2.06e-63 |
|
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: 218.31 E-value: 2.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 401 DEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHS 480
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 481 LSLIEyihKNSITYLKMTPTLFSTLME-DVDMLASCPDLKVIILGGESINIGNVKKLAEKCRwMKFINHYGPTESTVGCI 559
Cdd:cd04433 81 LELIE---REKVTILLGVPTLLARLLKaPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG-IKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 560 AHSIDLDHIQnceiYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNpfhpgakMYK 639
Cdd:cd04433 157 TGPPDDDARK----PGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------WYR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 640 TGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEMEGSF------VQ 713
Cdd:cd04433 226 TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdldaeeLR 305
|
330 340 350
....*....|....*....|....*....|
gi 2085927195 714 EKLAQALPKYMIPSFIIQLKELPLTANGKI 743
Cdd:cd04433 306 AHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-1016 |
1.26e-55 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 211.95 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVY------AGKHITYKELNEKANQVATLLMEKGAGKNSitAMMIRPS--EYsMIGILGILK 331
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDR--AVLLFPSgpDY-VAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 332 TG----SAFLPiddESpvSRINH------ILKDSKADILIT--DLC--FLADKNIAAE------CLDITDKSIytSQNTS 391
Cdd:PRK05691 87 AGviavPAYPP---ES--ARRHHqerllsIIADAEPRLLLTvaDLRdsLLQMEELAAAnapellCVDTLDPAL--AEAWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 392 NPDVQYDleDEVYVIYTSGTSGKPKGVKVKNKSLV-NYSLWVCD-QININSDSR--SLVTSKYSFDLCYTSIFPVLSGGG 467
Cdd:PRK05691 160 EPALQPD--DIAFLQYTSGSTALPKGVQVSHGNLVaNEQLIRHGfGIDLNPDDVivSWLPLYHDMGLIGGLLQPIFSGVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 468 QV-----HFVDKEV-YLHSLSliEYIHKNS----ITYLKMTPTLFSTLMEDVDMlascPDLKVIILGGESINIGNVKKLA 537
Cdd:PRK05691 238 CVlmspaYFLERPLrWLEAIS--EYGGTISggpdFAYRLCSERVSESALERLDL----SRWRVAYSGSEPIRQDSLERFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 538 EK---CRWM--KFINHYGPTESTV---------GCIAHSIDLDH-------------IQNCeiynkiGRPIHGINIYIVD 590
Cdd:PRK05691 312 EKfaaCGFDpdSFFASYGLAEATLfvsggrrgqGIPALELDAEAlarnraepgtgsvLMSC------GRSQPGHAVLIVD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 591 -RSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDnpfHPGAKMYKTGDLGrWMPDGNIEFLGRIDNQIKIRGFRV 669
Cdd:PRK05691 386 pQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 670 EIGEIENQLlqlegikEAAVVYIEEKYLSAYITGDIEMEG--------SFVQEKL-AQALPKYM----------IPSFII 730
Cdd:PRK05691 462 YPQDIEKTV-------EREVEVVRKGRVAAFAVNHQGEEGigiaaeisRSVQKILpPQALIKSIrqavaeacqeAPSVVL 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 731 QLK--ELPLTANGKINRKELPL-------------PDLQRLSVPRYEAPANETEEKLAEIWKEMLGHKRISINEDFFELG 795
Cdd:PRK05691 535 LLNpgALPKTSSGKLQRSACRLrladgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLG 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 796 GHSLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRLIQKRDKQNYPVISK----ARKQSYYQaSSAQKRMFALWETDK 871
Cdd:PRK05691 615 GNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAAiarlPRGQALPQ-SLAQNRLWLLWQLDP 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 872 DSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEF---DYQKLPSDGiRPYVKQFI 948
Cdd:PRK05691 694 QSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALqriDLSDLPEAE-REARAAQI 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 949 R------PFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGH------KLKQPPLQSKDYSEW 1015
Cdd:PRK05691 773 ReeearqPFDLEKGPLLRVTLVRLdDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAW 852
|
.
gi 2085927195 1016 Q 1016
Cdd:PRK05691 853 Q 853
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
285-748 |
4.86e-55 |
|
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: 198.08 E-value: 4.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSkadilitdl 364
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKC--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 365 cflADKNIAAECLDITDKSIYTSQnTSNPDVQYDlEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRS 444
Cdd:cd17654 88 ---HVSYLLQNKELDNAPLSFTPE-HRHFNIRTD-ECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 445 LVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHK-NSITYLKMTPTLF----STLMEDVDMLAScPDLK 519
Cdd:cd17654 163 FLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrHRITVLQATPTLFrrfgSQSIKSTVLSAT-SSLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 520 VIILGGESINIGNV-KKLAEKCRWMKFINHYGPTESTVGCIAHsidldHIQNCEIYNKIGRPIHGINIYIVDRSdqlvpv 598
Cdd:cd17654 242 VLALGGEPFPSLVIlSSWRGKGNRTRIFNIYGITEVSCWALAY-----KVPEEDSPVQLGSPLLGTVIEVRDQN------ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 599 GAPGEICISGVGLASGYVNNEELTNekfidnpfhPGAKMYKTGDLGRwMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQL 678
Cdd:cd17654 311 GSEGTGQVFLGGLNRVCILDDEVTV---------PKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVI 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 679 LQLEGIKEAAVVYIEEKYLSAYITGDiEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd17654 381 ESCLGVESCAVTLSDQQRLIAFIVGE-SSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
273-751 |
5.58e-52 |
|
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: 191.19 E-value: 5.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAG-------KHITYKELNEKANQVATLLMEKGAGKNSItaMMIrpseYS------MIGILGILKTGSAFLPI 339
Cdd:cd17647 2 PERTCVVETPslnssktRSFTYRDINEASNIVAHYLIKTGIKRGDV--VMI----YSyrgvdlMVAVMGVLKAGATFSVI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILITdlcfladkniaaecldITDKSIYTSQNtSNPDVQydledevyviYTSGTSGKPKGVK 419
Cdd:cd17647 76 DPAYPPARQNIYLGVAKPRGLIV----------------IRAAGVVVGPD-SNPTLS----------FTSGSEGIPKGVL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 420 VKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTP 499
Cdd:cd17647 129 GRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 TLFSTLMEDVDmlASCPDLKVIILGGESI---NIGNVKKLAEKCRwmkFINHYGPTE-----STVGCIAHSIDLDHIQNC 571
Cdd:cd17647 209 AMGQLLTAQAT--TPFPKLHHAFFVGDILtkrDCLRLQTLAENVR---IVNMYGTTEtqravSYFEVPSRSSDPTFLKNL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 572 EIYNKIGRPIHGINIYIVDRSD--QLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF------------------ 631
Cdd:cd17647 284 KDVMPAGRGMLNVQLLVVNRNDrtQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkdnnepwr 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 632 ----HPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI----EEKYLSAYITG 703
Cdd:cd17647 364 qfwlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRrdkdEEPTLVSYIVP 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2085927195 704 DIEMEGSF-----------------------------VQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKELPLP 751
Cdd:cd17647 444 RFDKPDDEsfaqedvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
260-748 |
1.84e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 183.85 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI 339
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTS--------------------QNTSNPDVQYDl 399
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGdgpaaplapevgeyeellaaASDTFDFPDID- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 EDEVYV-IYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVtskysfdlcYTSIF----------PVLSGGgq 468
Cdd:PRK06187 166 ENDAAAmLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLV---------IVPMFhvhawglpylALMAGA-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 469 vhfvdKEVYLHSL---SLIEYIHKNSITYLKMTPTLFStlmedvdMLASCPD--------LKVIILGGESINIGNVKKLA 537
Cdd:PRK06187 235 -----KQVIPRRFdpeNLLDLIETERVTFFFAVPTIWQ-------MLLKAPRayfvdfssLRLVIYGGAALPPALLREFK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 538 EKCRwMKFINHYGPTEST-VGCIAHsIDLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPV--GAPGEICISGVGLASG 614
Cdd:PRK06187 303 EKFG-IDLVQGYGMTETSpVVSVLP-PEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 615 YVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-- 692
Cdd:PRK06187 381 YWNRPEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpd 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085927195 693 ---EEKYLsAYITGdieMEGSFVQEK-----LAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK06187 454 ekwGERPV-AVVVL---KPGATLDAKelrafLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
260-748 |
4.15e-49 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 182.67 E-value: 4.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI 339
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILITD-LCFLADKNIAAECLD-----ITDKSIYTS--------------QNTSNPDVQYDL 399
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSsERLDLLHPALPGCHDlrtliIVGDPAHASeghpgeepaswpklLALGDADPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 --EDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDkevY 477
Cdd:TIGR03098 161 idSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD---Y 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 478 LHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTvg 557
Cdd:TIGR03098 238 LLPRDVLKALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEAF-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 558 ciaHSIDLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNP-FHPGAK 636
Cdd:TIGR03098 316 ---RSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpFPGELH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 637 MYKT----GDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYI------TGDIE 706
Cdd:TIGR03098 393 LPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIvlvvtpPGGEE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2085927195 707 MEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:TIGR03098 473 LDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
261-748 |
8.19e-48 |
|
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: 177.76 E-value: 8.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 261 IQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPID 340
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 341 DESPVSRINHILKDSKADILITDLCFladkniaAECLDITDKSIYTsqntsnpdVQYDLEDEVYVIYTSGTSGKPKGVKV 420
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVSF-------TDLLAAGAPLGER--------VALTPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 421 KNKSLV-N-YSLWVCDQININSDSRSLVT----SKYSFDLCYTSifPVLSGGGQV---HFVDKEVylhslslIEYIHKNS 491
Cdd:cd05936 146 THRNLVaNaLQIKAWLEDLLEGDDVVLAAlplfHVFGLTVALLL--PLALGATIVlipRFRPIGV-------LKEIRKHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 492 ITYLKMTPTLFSTLMEDVDMLASCPD-LKVIILGGESINignvKKLAEKCRWM---KFINHYGPTE-STVGCIAHSIDLD 566
Cdd:cd05936 217 VTIFPGVPTMYIALLNAPEFKKRDFSsLRLCISGGAPLP----VEVAERFEELtgvPIVEGYGLTEtSPVVAVNPLDGPR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 567 HIqnceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRW 646
Cdd:cd05936 293 KP------GSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLR-------TGDIGYM 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 647 MPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYItgdIEMEGSFVQEK-----LA 717
Cdd:cd05936 360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGeavkAFV---VLKEGASLTEEeiiafCR 436
|
490 500 510
....*....|....*....|....*....|.
gi 2085927195 718 QALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05936 437 EQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
263-748 |
1.46e-47 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 179.54 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 263 DLFEERAEKTPDQTAAVYAG-----KHITYKELNEKANQVATLLMEKGAGK-NSITAMMIRPSEYsMIGILGILKTGSAF 336
Cdd:COG0365 13 NCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKgDRVAIYLPNIPEA-VIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 lpiddeSPVS----------RINhilkDSKADILITDLCFL------ADKNIAAECLDITDK------------------ 382
Cdd:COG0365 92 ------SPVFpgfgaealadRIE----DAEAKVLITADGGLrggkviDLKEKVDEALEELPSlehvivvgrtgadvpmeg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 383 -----SIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWvcdqininsdsrslvTSKYSFDL--- 454
Cdd:COG0365 162 dldwdELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAT---------------TAKYVLDLkpg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 455 ----CYTSI-----------FPVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPD-- 517
Cdd:COG0365 227 dvfwCTADIgwatghsyivyGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDls 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 518 -LKVIILGGESINignvkklAEKCRWMK------FINHYGPTEsTVGCIAHSIDLDHIQNCEIynkiGRPIHGINIYIVD 590
Cdd:COG0365 307 sLRLLGSAGEPLN-------PEVWEWWYeavgvpIVDGWGQTE-TGGIFISNLPGLPVKPGSM----GKPVPGYDVAVVD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 591 RSDQLVPVGAPGEICISG--VGLASGYVNNEELTNEKFIDNpfHPGakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFR 668
Cdd:COG0365 375 EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYFGR--FPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 669 VEIGEIENQLLQLEGIKEAAVVYI--EEK--YLSAYI------TGDIEMEGSfVQEKLAQALPKYMIPSFIIQLKELPLT 738
Cdd:COG0365 451 IGTAEIESALVSHPAVAEAAVVGVpdEIRgqVVKAFVvlkpgvEPSDELAKE-LQAHVREELGPYAYPREIEFVDELPKT 529
|
570
....*....|
gi 2085927195 739 ANGKINRKEL 748
Cdd:COG0365 530 RSGKIMRRLL 539
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
282-744 |
6.99e-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: 175.48 E-value: 6.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 282 GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILI 361
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 362 TDLCFLADKNIAAECLDITDKsIYT--------------SQNTSNPDVQYDLEDE-------VYVIYTSGTSGKPKGVKV 420
Cdd:cd05911 88 TDPDGLEKVKEAAKELGPKDK-IIVlddkpdgvlsiedlLSPTLGEEDEDLPPPLkdgkddtAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 421 KNKSLVNYSLWVCDQININSDSRSLVTSKYSFD----LCYTSIFPVLsgGGQVHFVDKevyLHSLSLIEYIHKNSITYLK 496
Cdd:cd05911 167 SHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiygLFTTLASLLN--GATVIIMPK---FDSELFLDLIEKYKITFLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 497 MTPTLFStlmedvdMLASCPD--------LKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTEsTVGCIAHSIDLDHI 568
Cdd:cd05911 242 LVPPIAA-------ALAKSPLldkydlssLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTE-TGGILTVNPDGDDK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 569 QNCEiynkiGRPIHGINIYIVDR-SDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWM 647
Cdd:cd05911 314 PGSV-----GRLLPNVEAKIVDDdGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 648 PDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSayitgdiEMEGSFV----QEKL-AQALPK 722
Cdd:cd05911 383 EDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSG-------ELPRAYVvrkpGEKLtEKEVKD 455
|
490 500 510
....*....|....*....|....*....|.
gi 2085927195 723 YM---IPSF------IIQLKELPLTANGKIN 744
Cdd:cd05911 456 YVakkVASYkqlrggVVFVDEIPKSASGKIL 486
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
853-1016 |
9.76e-45 |
|
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: 167.53 E-value: 9.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 853 YYQASSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEF-- 930
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLpv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 931 -DYQKLPSDGIRPYVKQFI-----RPFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLK 1003
Cdd:cd19531 81 vDLSGLPEAEREAEAQRLAreearRPFDLARGPLLRATLLRLgEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
|
170
....*....|....*....
gi 2085927195 1004 QP------PLQSKDYSEWQ 1016
Cdd:cd19531 161 RPsplpplPIQYADYAVWQ 179
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
265-743 |
1.91e-44 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 167.02 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 265 FEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESP 344
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 345 VSRINHILKDSKADILITDLCFLadkniaaeclditdksiytsqntsnpdvqydledevyvIYTSGTSGKPKGVKVKNKS 424
Cdd:cd17631 81 PPEVAYILADSGAKVLFDDLALL--------------------------------------MYTSGTTGRPKGAMLTHRN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 425 LVNYSLWVCDQININSDSRSLVtskySFDLCYTS-----IFPVLSGGGQVHFVDKEVYLHSLSLIEyihKNSITYLKMTP 499
Cdd:cd17631 123 LLWNAVNALAALDLGPDDVLLV----VAPLFHIGglgvfTLPTLLRGGTVVILRKFDPETVLDLIE---RHRVTSFFLVP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 TLfstlmedVDMLASCPD--------LKVIILGGESINIGNVKKLAEkcRWMKFINHYGPTESTVGCIAHSIDlDHIqnc 571
Cdd:cd17631 196 TM-------IQALLQHPRfattdlssLRAVIYGGAPMPERLLRALQA--RGVKFVQGYGMTETSPGVTFLSPE-DHR--- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 572 EIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGN 651
Cdd:cd17631 263 RKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFH-------TGDLGRLDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 652 IEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-EEKYLSAYI-----TGDIEMEGSFVQEKLAQALPKYMI 725
Cdd:cd17631 336 LYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVpDEKWGEAVVavvvpRPGAELDEDELIAHCRERLARYKI 415
|
490
....*....|....*...
gi 2085927195 726 PSFIIQLKELPLTANGKI 743
Cdd:cd17631 416 PKSVEFVDALPRNATGKI 433
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
856-1016 |
2.67e-42 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 154.81 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 856 ASSAQKRMFALwetDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEF---DY 932
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLevvDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 933 QKLPSDGIRPYVKQFI-----RPFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYA----GHKL 1002
Cdd:COG4908 78 SALPEPEREAELEELVaeeasRPFDLARGPLLRAALIrLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAalleGEPP 157
|
170
....*....|....*.
gi 2085927195 1003 KQPPL--QSKDYSEWQ 1016
Cdd:COG4908 158 PLPELpiQYADYAAWQ 173
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
286-748 |
2.84e-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: 158.00 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDLC 365
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 366 FLAdKNIAAeclDITDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSL 445
Cdd:TIGR01923 81 LEE-KDFQA---DSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 446 VtskySFDLCYTS----IFPVLSGGGQVHFVDKEVylhslSLIEYIHKNSITYLKMTPTLFSTLMedvDMLASCPDLKVI 521
Cdd:TIGR01923 157 L----SLPLYHISglsiLFRWLIEGATLRIVDKFN-----QLLEMIANERVTHISLVPTQLNRLL---DEGGHNENLRKI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 522 ILGGESINIgnvkKLAEKCRWMKF--INHYGPTESTVGCIAHSIDLDHIQNceiynKIGRPIHGINIYIvdRSDQLVPVG 599
Cdd:TIGR01923 225 LLGGSAIPA----PLIEEAQQYGLpiYLSYGMTETCSQVTTATPEMLHARP-----DVGRPLAGREIKI--KVDNKEGHG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 600 apgEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLL 679
Cdd:TIGR01923 294 ---EIMVKGANLMKGYLYQGELTPAFEQQGWFN-------TGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLY 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2085927195 680 QLEGIKEAAVVYIEEK--------YLSAYITGDIEMEGSFVQEKLAqalpKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:TIGR01923 364 QHPGIQEAVVVPKPDAewgqvpvaYIVSESDISQAKLIAYLTEKLA----KYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
282-749 |
1.19e-40 |
|
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: 155.53 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 282 GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILI 361
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 362 TDLCfladkniaaeclditdksiytsqntsnpdvqydledevYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSD 441
Cdd:cd05934 81 VDPA--------------------------------------SILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGED 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 442 SRSLVTSK--YSFDLCYtSIFPVLSGGGQVHFVDKevyLHSLSLIEYIHKNSITYLKMTPTLFSTLM---EDVDMLASCp 516
Cdd:cd05934 123 DVYLTVLPlfHINAQAV-SVLAALSVGATLVLLPR---FSASRFWSDVRRYGATVTNYLGAMLSYLLaqpPSPDDRAHR- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 517 dLKVIILGGesinigNVKKLAE--KCRW-MKFINHYGPTESTVGCIAhsiDLDHIQnceIYNKIGRPIHGINIYIVDRSD 593
Cdd:cd05934 198 -LRAAYGAP------NPPELHEefEERFgVRLLEGYGMTETIVGVIG---PRDEPR---RPGSIGRPAPGYEVRIVDDDG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 594 QLVPVGAPGEICISGV---GLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVE 670
Cdd:cd05934 265 QELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAMRNGWFH-------TGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 671 IGEIENQLLQLEGIKEAAVV-----YIEEKYLSAYItgdIEMEGSFVQEKL----AQALPKYMIPSFIIQLKELPLTANG 741
Cdd:cd05934 338 SAEVERAILRHPAVREAAVVavpdeVGEDEVKAVVV---LRPGETLDPEELfafcEGQLAYFKVPRYIRFVDDLPKTPTE 414
|
....*...
gi 2085927195 742 KINRKELP 749
Cdd:cd05934 415 KVAKAQLR 422
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
260-748 |
1.28e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 157.76 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI 339
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTSQNTSNPDVQYDL-------------------E 400
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKtftdflaagdpaerapevdP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 401 DEVYVI-YTSGTSGKPKGVKVKNK-SLVNYSLWvCDQININSDSRSLVTSKYSFDLCYTS--IFPVLSGGG---QVHFVD 473
Cdd:PRK07656 166 DDVADIlFTSGTTGRPKGAMLTHRqLLSNAADW-AEYLGLTEGDRYLAANPFFHVFGYKAgvNAPLMRGATilpLPVFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 474 KEVylhslslIEYIHKNSITYLKMTPTLFSTLME----DVDMLAScpdLKVIILGGESINIGNVKKLAEKCRWMKFINHY 549
Cdd:PRK07656 245 DEV-------FRLIETERITVLPGPPTMYNSLLQhpdrSAEDLSS---LRLAVTGAASMPVALLERFESELGVDIVLTGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 550 GPTEST-VGCIAhSIDLDHIqncEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKF-I 627
Cdd:PRK07656 315 GLSEASgVTTFN-RLDDDRK---TVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIdA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 628 DNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYIT- 702
Cdd:PRK07656 391 DGWLH-------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGevgkAYVVl 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 703 ---GDIEMEG--SFVQEKLAqalpKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK07656 464 kpgAELTEEEliAYCREHLA----KYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
274-748 |
7.96e-39 |
|
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: 150.90 E-value: 7.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 274 DQTAAVYAGKHITYKELNEKANQVATLLMEKGA-GKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILItdlcfladkNIAAeclditdksiytsqntsnpdvqydledevyVIYTSGTSGKPKGVkvknkslvnyslwV 432
Cdd:cd05941 81 TDSEPSLVL---------DPAL------------------------------ILYTSGTTGRPKGV-------------V 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 433 CDQININSDSRSLV-----TSKYSFDLC---------YTSIFPVLSGGGQVHFV---DKEVYLHSLslieyiHKNSITYL 495
Cdd:cd05941 109 LTHANLAANVRALVdawrwTEDDVLLHVlplhhvhglVNALLCPLFAGASVEFLpkfDPKEVAISR------LMPSITVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 496 KMTPTLFSTLMEDVDMLASCPDLKViilggesinignvKKLAEKCRWM-------------KF--------INHYGPTES 554
Cdd:cd05941 183 MGVPTIYTRLLQYYEAHFTDPQFAR-------------AAAAERLRLMvsgsaalpvptleEWeaitghtlLERYGMTEI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 555 TvgcIAHSIDLDhiqNCEIYNKIGRPIHGINIYIVDRS-DQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhp 633
Cdd:cd05941 250 G---MALSNPLD---GERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 634 gakmYKTGDLGRWMPDGNIEFLGRI-DNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEMEGSFV 712
Cdd:cd05941 322 ----FKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAA 397
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2085927195 713 Q-------EKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05941 398 AlsleelkEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
400-745 |
2.29e-38 |
|
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: 146.64 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 EDEVYVIYTSGTSGKPKGVKVKNKSLVNYSL-WVCDQININSDSRSLVTSKYSFDLCYTSIFPVL-SGGGQVHFVDKEVY 477
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDiLQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLiHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 478 LhslSLIEYIHKNSITYLKMTPTLFSTLM-EDVDMLASCPDLKVIILGGESInIGNVKKLAEKCRWMKFINHYGPTE-ST 555
Cdd:cd17635 81 K---SLFKILTTNAVTTTCLVPTLLSKLVsELKSANATVPSLRLIGYGGSRA-IAADVRFIEATGLTNTAQVYGLSEtGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 556 VGCIAHSIDLDHIqnceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpga 635
Cdd:cd17635 157 ALCLPTDDDSIEI------NAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 636 kmyKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEMEG------ 709
Cdd:cd17635 227 ---NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAeldena 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 2085927195 710 -SFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINR 745
Cdd:cd17635 304 iRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
286-748 |
1.26e-37 |
|
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: 146.71 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDLc 365
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 366 fladkniaaeclditdksiytsqntsnpdvqydlEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSL 445
Cdd:cd05972 81 ----------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 446 VTSKYSFDLC-YTSIFPVLSGGGQVhFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEdVDMLA-SCPDLKVIIL 523
Cdd:cd05972 127 NIADPGWAKGaWSSFFGPWLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSyKFSHLRLVVS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 524 GGESINiGNVKKLAEKCRWMKFINHYGPTESTVgCIAHSIDLDHIQNceiynKIGRPIHGINIYIVDRSDQLVPVGAPGE 603
Cdd:cd05972 205 AGEPLN-PEVIEWWRAATGLPIRDGYGQTETGL-TVGNFPDMPVKPG-----SMGRPTPGYDVAIIDDDGRELPPGEEGD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 604 ICI--SGVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQL 681
Cdd:cd05972 278 IAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEH 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085927195 682 EGIKEAAVV-YIEEKYLS---AYItgdIEMEGSFVQEKLAQALPK--------YMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05972 351 PAVAEAAVVgSPDPVRGEvvkAFV---VLTSGYEPSEELAEELQGhvkkvlapYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
268-748 |
7.15e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 145.88 E-value: 7.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 268 RAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSR 347
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 348 INHILKDSKADILITDLCFLADKNIAAEC----LDITDKSIYTSQNTsnpdvqYDLEDEVYVIYTSGTSGKPKGV--KVK 421
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLIPGISVkfaeLMNGPKEEAEIQEE------FDLDEVATIMYTSGTTGKPKGViqTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 422 NkslvNYSLWVCDQININsdsrslVTSKYSFdLCYTSIFPVlSG----------GGQVHFVDKevyLHSLSLIEYIHKNS 491
Cdd:PRK03640 165 N----HWWSAVGSALNLG------LTEDDCW-LAAVPIFHI-SGlsilmrsviyGMRVVLVEK---FDAEKINKLLQTGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 492 ITYLKMTPTLFSTLMEDVDMlASCPD-LKVIILGGESINignvKKLAEKCRWMKF--INHYGPTESTVGCIAHSIDldhi 568
Cdd:PRK03640 230 VTIISVVSTMLQRLLERLGE-GTYPSsFRCMLLGGGPAP----KPLLEQCKEKGIpvYQSYGMTETASQIVTLSPE---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 569 qncEIYNKI---GRPIHGINIYIVDrSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGR 645
Cdd:PRK03640 301 ---DALTKLgsaGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFK-------TGDIGY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 646 WMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIE-EKYLS---AYI--TGDIEMEG--SFVQEKLA 717
Cdd:PRK03640 370 LDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPdDKWGQvpvAFVvkSGEVTEEElrHFCEEKLA 449
|
490 500 510
....*....|....*....|....*....|.
gi 2085927195 718 qalpKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK03640 450 ----KYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
850-1016 |
4.47e-35 |
|
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: 139.78 E-value: 4.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 850 KQSYYQASSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSD-DVVQIIHDTWEL 928
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENgEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 929 EFDYQKLP-SDGIRP--YVKQFIR-----PFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGIIRKEFNALYA- 998
Cdd:pfam00668 81 ELEIIDISdLSESEEeeAIEAFIQrdlqsPFDLEKGPLFRAGLFRIaENRHHLLLSMHHIIVDGVSLGILLRDLADLYQq 160
|
170 180
....*....|....*....|..
gi 2085927195 999 ---GHKLKQPPLQS-KDYSEWQ 1016
Cdd:pfam00668 161 llkGEPLPLPPKTPyKDYAEWL 182
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
407-748 |
7.88e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 136.64 E-value: 7.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 407 YTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRslVTSKYSFDLCYTSIFPVL---SGGGQVHFVdkEVYLHSLSL 483
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDR--LCIPVPLFHCFGSVLGVLaclTHGATMVFP--SPSFDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 484 IEYIHKNSITYLKMTPTLFSTLMEDVDMLAScpDLKVI---ILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIA 560
Cdd:cd05917 85 LEAIEKEKCTALHGVPTMFIAELEHPDFDKF--DLSSLrtgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 561 HSIDlDHIQncEIYNKIGRPIHGINIYIVD-RSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKfIDnpfhpGAKMYK 639
Cdd:cd05917 163 TRTD-DSIE--KRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA-ID-----GDGWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 640 TGDLGRWMPDGNIEFLGRIDNQIkIRGfrveiG------EIENQLLQLEGIKEAAVVYI-EEKY---LSAYITGDIEMEG 709
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMI-IRG-----GeniyprEIEEFLHTHPKVSDVQVVGVpDERYgeeVCAWIRLKEGAEL 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2085927195 710 S------FVQEKLAQalpkYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05917 308 TeedikaYCKGKIAH----YKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
7-245 |
7.89e-35 |
|
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: 139.01 E-value: 7.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 7 PVFQSSADeGGFNNRKKTFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKM 86
Cdd:pfam00668 213 KDYARPAD-RSFKGDRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP--SPDIERM 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 87 VGLFINAVPLRVKGDGDTVFIALAQKLNSDFIKA--NTSYGYSSLADIQALTK--MKEKLINHMLVYENYPVDdygkavD 162
Cdd:pfam00668 290 VGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAepHQGYPFGDLVNDLRLPRdlSRHPLFDPMFSFQNYLGQ------D 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 163 DTTDALRITDMEV------FEQTNYDFGLVIIP-GSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDPTRVLKDIS 235
Cdd:pfam00668 364 SQEEEFQLSELDLsvssviEEEAKYDLSLTASErGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELD 443
|
250
....*....|
gi 2085927195 236 AVNEEERGML 245
Cdd:pfam00668 444 LLSDAEKQKL 453
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
400-748 |
4.62e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 136.80 E-value: 4.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 EDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFdlCYTsiFPVLSgggqVHFV-DKEVYL 478
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSY--DYG--LSVLN----THLLrGATLVL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 479 HSLS-----LIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTE 553
Cdd:cd05922 189 TNDGvlddaFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 554 STvgciAHSIDLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEEltnekFIDNPFHP 633
Cdd:cd05922 269 AT----RRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPP-----YRRKEGRG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 634 GAKMYkTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKY---LSAYITGDIEMEGS 710
Cdd:cd05922 340 GGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLgekLALFVTAPDKIDPK 418
|
330 340 350
....*....|....*....|....*....|....*...
gi 2085927195 711 FVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05922 419 DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
260-748 |
1.22e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 136.99 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI 339
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 -----DDEspvsrINHILKDSKADILITD---------------------LCFLADKNIAAECLDITDksIYTSQNTSNP 393
Cdd:PRK08316 92 nfmltGEE-----LAYILDHSGARAFLVDpalaptaeaalallpvdtlilSLVLGGREAPGGWLDFAD--WAEAGSVAEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 394 DVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLV-NY--SLWVCDqinINSDSRSLvtskYSFDLcYTS----IF--PVLS 464
Cdd:PRK08316 165 DVELADDDLAQILYTSGTESLPKGAMLTHRALIaEYvsCIVAGD---MSADDIPL----HALPL-YHCaqldVFlgPYLY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 465 GGGQVHFVDKEVylhSLSLIEYIHKNSITYLKMTPTLFSTlmedvdmLASCPDLKVIILG-------GESINIGNV-KKL 536
Cdd:PRK08316 237 VGATNVILDAPD---PELILRTIEAERITSFFAPPTVWIS-------LLRHPDFDTRDLSslrkgyyGASIMPVEVlKEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 537 AEKCRWMKFINHYGPTEstvgcIA--HSI-----DLDHIQNCeiynkiGRPIHGINIYIVDRSDQLVPVGAPGEICISGV 609
Cdd:PRK08316 307 RERLPGLRFYNCYGQTE-----IAplATVlgpeeHLRRPGSA------GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 610 GLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAV 689
Cdd:PRK08316 376 QLMLGYWDDPEKTAEAFRGGWFH-------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 690 VYIE-EKYLSAYITGDIEMEGSFVQEK-----LAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK08316 449 IGLPdPKWIEAVTAVVVPKAGATVTEDeliahCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
261-748 |
4.63e-33 |
|
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: 134.80 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 261 IQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPID 340
Cdd:cd05959 6 ATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 341 DESPVSRINHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTSQNTSNPDVQYDLEDEV----------------- 403
Cdd:cd05959 86 TLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVaaeaeqlkpaathaddp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 404 -YVIYTSGTSGKPKGVKVKNKSLVnyslWVCDQ-----ININSDSRSLVTSK--YSFDLCYTSIFPvLSGGGQVHFVDKE 475
Cdd:cd05959 166 aFWLYSSGSTGRPKGVVHLHADIY----WTAELyarnvLGIREDDVCFSAAKlfFAYGLGNSLTFP-LSVGATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 476 VYLHSLslIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPD-LKVIILGGESI--NIGNvkklaekcRWMkfiNHYGpt 552
Cdd:cd05959 241 PTPAAV--FKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSsLRLCVSAGEALpaEVGE--------RWK---ARFG-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 553 estvgciaHSIdLDHIQNCEI-------------YNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNE 619
Cdd:cd05959 306 --------LDI-LDGIGSTEMlhiflsnrpgrvrYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 620 ELTNEKFIdnpfhpgAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKY--- 696
Cdd:cd05959 377 DKTRDTFQ-------GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDglt 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2085927195 697 -LSAYI-----TGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05959 450 kPKAFVvlrpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
237-757 |
8.06e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 134.88 E-value: 8.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 237 VNEEERGMLQEfnkqsSNYTVNKTIQDLFEERAEKTPDQTAAV-YAGKHITYKELNEKANQVATLLMEKG-AGKNSITAM 314
Cdd:PRK06087 6 FNEQRRAAYRQ-----QGYWGDASLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGiEPGDRVAFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 315 MIRPSEYSMIgILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDLCF-----------------------LADKN 371
Cdd:PRK06087 81 LPGWCEFTII-YLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqtrpvdlilplqnqlpqlqqivGVDKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 372 iAAECLDITDKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTS--K 449
Cdd:PRK06087 160 -APATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAplG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 450 YSFDLCYTSIFPVLSGGGQV---HFVDKevylHSLSLIEyihKNSITY-LKMTPTLFSTLMEDVDMLASCPDLKVIILGG 525
Cdd:PRK06087 239 HATGFLHGVTAPFLIGARSVlldIFTPD----ACLALLE---QQRCTCmLGATPFIYDLLNLLEKQPADLSALRFFLCGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 526 ESINignvKKLAEKC--RWMKFINHYGPTEStvgcIAHS-IDLDhiQNCE-IYNKIGRPIHGINIYIVDRSDQLVPVGAP 601
Cdd:PRK06087 312 TTIP----KKVARECqqRGIKLLSVYGSTES----SPHAvVNLD--DPLSrFMHTDGYAAAGVEIKVVDEARKTLPPGCE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 602 GEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRiDNQIKIRGFR-VEIGEIENQLLQ 680
Cdd:PRK06087 382 GEEASRGPNVFMGYLDEPELTARALDEEGW------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQ 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 681 LEGIKEAAVVYIEEKYLS----AYITGDIEMEGSFVQEKLA----QALPKYMIPSFIIQLKELPLTANGKINRKELPLPD 752
Cdd:PRK06087 455 HPKIHDACVVAMPDERLGerscAYVVLKAPHHSLTLEEVVAffsrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI 534
|
....*
gi 2085927195 753 LQRLS 757
Cdd:PRK06087 535 MRRLT 539
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
283-748 |
6.45e-32 |
|
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: 130.24 E-value: 6.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 283 KHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILIT 362
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 363 DLCfladkniaaeclditdksiytsqntsnpdvqydlEDEVYVIYTSGTSGKPKGV----KVKNKSLVNYSLwvCDQINI 438
Cdd:cd05971 85 DGS----------------------------------DDPALIIYTSGTTGPPKGAlhahRVLLGHLPGVQF--PFNLFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 439 NSDSRSLVTSKYS-----FDLCYTSIF---PVLSGGGQVHFVDKevylhslsLIEYIHKNSITYLKMTPTLFSTLMEDVD 510
Cdd:cd05971 129 RDGDLYWTPADWAwigglLDVLLPSLYfgvPVLAHRMTKFDPKA--------ALDLMSRYGVTTAFLPPTALKMMRQQGE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 511 MLASCP-DLKVIILGGESINignvkklAEKCRWMK-----FINH-YGPTESTVgCIAHSIDLDHIQNceiyNKIGRPIHG 583
Cdd:cd05971 201 QLKHAQvKLRAIATGGESLG-------EELLGWAReqfgvEVNEfYGQTECNL-VIGNCSALFPIKP----GSMGKPIPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 584 INIYIVDRSDQLVPVGAPGEICI---SGVGLAsGYVNNEELTNEKFIdnpfhpgAKMYKTGDLGRWMPDGNIEFLGRIDN 660
Cdd:cd05971 269 HRVAIVDDNGTPLPPGEVGEIAVelpDPVAFL-GYWNNPSATEKKMA-------GDWLLTGDLGRKDSDGYFWYVGRDDD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 661 QIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEK----------YLSAYITGDIEMEGSfVQEKLAQALPKYMIPSFII 730
Cdd:cd05971 341 VITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPirgeivkafvVLNPGETPSDALARE-IQELVKTRLAAHEYPREIE 419
|
490
....*....|....*...
gi 2085927195 731 QLKELPLTANGKINRKEL 748
Cdd:cd05971 420 FVNELPRTATGKIRRREL 437
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
275-748 |
1.06e-31 |
|
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: 129.50 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 275 QTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKD 354
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 355 SKADILITDLcfladkniaaeclditdksiytsqntsnpdvqydlEDEVYVIYTSGTSGKPKGVKVKNKSlvnySLWVCD 434
Cdd:cd05919 81 CEARLVVTSA-----------------------------------DDIAYLLYSSGTTGPPKGVMHAHRD----PLLFAD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 435 Q-----ININSDSRSLVTSK--YSFDLCYTSIFPVLSGGGQVHF---VDKEVYLHSLSLieyiHKNSITYlkMTPTLFST 504
Cdd:cd05919 122 AmareaLGLTPGDRVFSSAKmfFGYGLGNSLWFPLAVGASAVLNpgwPTAERVLATLAR----FRPTVLY--GVPTFYAN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 505 LMEDVDMLA-SCPDLKVIILGGESINIGnvkkLAEkcRWMKF-----INHYGPTEstVGCIAHSIDLDHIQnceiYNKIG 578
Cdd:cd05919 196 LLDSCAGSPdALRSLRLCVSAGEALPRG----LGE--RWMEHfggpiLDGIGATE--VGHIFLSNRPGAWR----LGSTG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 579 RPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEFLGRI 658
Cdd:cd05919 264 RPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 659 DNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKY----LSAYITGDiemEGSFVQEKLAQA--------LPKYMIP 726
Cdd:cd05919 337 DDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTglsrLTAFVVLK---SPAAPQESLARDihrhllerLSAHKVP 413
|
490 500
....*....|....*....|..
gi 2085927195 727 SFIIQLKELPLTANGKINRKEL 748
Cdd:cd05919 414 RRIAFVDELPRTATGKLQRFKL 435
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
285-748 |
1.96e-31 |
|
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: 128.23 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADilitdl 364
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 365 cfladkniaaeclditdksiytsqntsnpdvqydLEDEVYVIYTSGTSGKPKGVkvknkslvnyslwvcdQININSDSRS 444
Cdd:cd05912 76 ----------------------------------LDDIATIMYTSGTTGKPKGV----------------QQTFGNHWWS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 445 LVTSKYSFDL----CYTSIFPV--LSG----------GGQVHFVDK--EVYLHSLslieyIHKNSITYLKMTPTLFSTLM 506
Cdd:cd05912 106 AIGSALNLGLteddNWLCALPLfhISGlsilmrsviyGMTVYLVDKfdAEQVLHL-----INSGKVTIISVVPTMLQRLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 507 EDvdMLASCP-DLKVIILGGESINignvKKLAEKC--RWMKFINHYGPTESTVGCIAHSIDLDHiqnceiyNKI---GRP 580
Cdd:cd05912 181 EI--LGEGYPnNLRCILLGGGPAP----KPLLEQCkeKGIPVYQSYGMTETCSQIVTLSPEDAL-------NKIgsaGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 581 IHGINIYIVDRSdqlVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDN 660
Cdd:cd05912 248 LFPVELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 661 QIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYITGDIEMEG----SFVQEKLAqalpKYMIPSFIIQL 732
Cdd:cd05912 318 LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGqvpvAFVVSERPISEeeliAYCSEKLA----KYKVPKKIYFV 393
|
490
....*....|....*.
gi 2085927195 733 KELPLTANGKINRKEL 748
Cdd:cd05912 394 DELPRTASGKLLRHEL 409
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
259-748 |
7.98e-31 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 128.55 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 259 KTIQDLFEERAEKTPDQT----AAVYAGKHITYKELNEKANQVATLLMEKG--AGKNSItaMMIRPSEYSMIG----IL- 327
Cdd:cd05906 10 RTLLELLLRAAERGPTKGityiDADGSEEFQSYQDLLEDARRLAAGLRQLGlrPGDSVI--LQFDDNEDFIPAfwacVLa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 328 GILKTGSAFLPIDDE--SPVSRINHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTSQNTSNPDVQYDL-----E 400
Cdd:cd05906 88 GFVPAPLTVPPTYDEpnARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLpqsrpD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 401 DEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSL-------VTSkysfdLCYTSIFPVLSGGGQVHFVD 473
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLnwvpldhVGG-----LVELHLRAVYLGCQQVHVPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 474 KEVYLHSLSLIEYIHKNSITYLKMtPTLFSTLM-------EDVDMLASCpdLKVIILGGESINIGNVKKLAE-----KCR 541
Cdd:cd05906 243 EEILADPLRWLDLIDRYRVTITWA-PNFAFALLndlleeiEDGTWDLSS--LRYLVNAGEAVVAKTIRRLLRllepyGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 542 WMKFINHYGPTESTVGCI-AHSIDLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEE 620
Cdd:cd05906 320 PDAIRPAFGMTETCSGVIySRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 621 LTNEKFIDNPFhpgakmYKTGDLGrWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIK--------------- 685
Cdd:cd05906 400 ANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEpsftaafavrdpgae 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2085927195 686 --EAAVVYIEEKYLSAYITGDIEMegsfVQEKLAQAL---PKYMIPsfiIQLKELPLTANGKINRKEL 748
Cdd:cd05906 473 teELAIFFVPEYDLQDALSETLRA----IRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
286-748 |
9.04e-31 |
|
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: 126.85 E-value: 9.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVATLLMEKGAGK-NSITAMMIR-PSEYsmIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITd 363
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKgDRVFVLSPRsPELY--FSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 364 lcfladkniAAECLDITDKsiytsqntsnpdvqydlEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSlwvcdqininsdsr 443
Cdd:cd05969 79 ---------TEELYERTDP-----------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYY-------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 444 slVTSKYSFDLCYTSIFPVLSGGGqvhFVDKEVY------LHSLSLIEY------------IHKNSITYLKMTPTLFSTL 505
Cdd:cd05969 119 --FTGKYVLDLHPDDIYWCTADPG---WVTGTVYgiwapwLNGVTNVVYegrfdaeswygiIERVKVTVWYTAPTAIRML 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 506 MEDVDMLASCPD---LKVIILGGESINignvkklAEKCRW------MKFINHYGPTESTVGCIAHSIDLDhIQNceiyNK 576
Cdd:cd05969 194 MKEGDELARKYDlssLRFIHSVGEPLN-------PEAIRWgmevfgVPIHDTWWQTETGSIMIANYPCMP-IKP----GS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 577 IGRPIHGINIYIVDRSDQLVPVGAPGEICISG--VGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEF 654
Cdd:cd05969 262 MGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWF 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 655 LGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE----KYLSAYITGDIEMEGS---------FVQEKLAQALp 721
Cdd:cd05969 335 VGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDplrgEIIKAFISLKEGFEPSdelkeeiinFVRQKLGAHV- 413
|
490 500
....*....|....*....|....*..
gi 2085927195 722 kymIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05969 414 ---APREIEFVDNLPKTRSGKIMRRVL 437
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
285-748 |
1.33e-30 |
|
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: 126.05 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILItdl 364
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 365 cfladkniaaeclditdksiytsqntsnpdVQYDLEDEVYVIYTSGTSGKPKGVkvknkSLVNYSLWVcdqininsdsrS 444
Cdd:cd05935 79 ------------------------------VGSELDDLALIPYTSGTTGLPKGC-----MHTHFSAAA-----------N 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 445 LVTSKYSFDLCYTSIF----PVLSGGGQVHFVDKEVYLHSL----------SLIEYIHKNSITYLKMTPTLFSTLMEDVD 510
Cdd:cd05935 113 ALQSAVWTGLTPSDVIlaclPLFHVTGFVGSLNTAVYVGGTyvlmarwdreTALELIEKYKVTFWTNIPTMLVDLLATPE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 511 MLASC-PDLKVIILGGESINIGNVKKLAEKCRwMKFINHYGPTEStvgCIAHSIDLDHIQNCEIynkIGRPIHGINIYIV 589
Cdd:cd05935 193 FKTRDlSSLKVLTGGGAPMPPAVAEKLLKLTG-LRFVEGYGLTET---MSQTHTNPPLRPKLQC---LGIP*FGVDARVI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 590 DRSD-QLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPfhpGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFR 668
Cdd:cd05935 266 DIETgRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK---GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 669 VEIGEIENQLLQLEGIKEAAVVYIEEKY----LSAYITGDIEMEGSFVQEKL----AQALPKYMIPSFIIQLKELPLTAN 740
Cdd:cd05935 343 VWPAEVEAKLYKHPAI*EVCVISVPDERvgeeVKAFIVLRPEYRGKVTEEDIiewaREQMAAYKYPREVEFVDELPRSAS 422
|
....*...
gi 2085927195 741 GKINRKEL 748
Cdd:cd05935 423 GKILWRLL 430
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
273-748 |
1.36e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 127.79 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMI--RPsEYSMIGILGILkTGSAFLPI------DDESp 344
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSlnRP-EVLMAIGAAQL-AGLRRTALhplgslDDHA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 345 vsrinHILKDSKADILITDLCFLADKNIA--------------AECLDITDKSIYTSQNTSNPDVQYDLEDEV-YVIYTS 409
Cdd:PRK06188 103 -----YVLEDAGISTLIVDPAPFVERALAllarvpslkhvltlGPVPDGVDLLAAAAKFGPAPLVAAALPPDIaGLAYTG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 410 GTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSfDLCYTSIFPVLSGGGQVHFVDK----EVylhsLSLIE 485
Cdd:PRK06188 178 GTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVLAKfdpaEV----LRAIE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 486 YiHKNSITYLkmTPTLFSTLMEDVDM-LASCPDLKVIILGGESINIGnvkKLAEKCRWMK--FINHYGPTESTVgCIAHS 562
Cdd:PRK06188 253 E-QRITATFL--VPTMIYALLDHPDLrTRDLSSLETVYYGASPMSPV---RLAEAIERFGpiFAQYYGQTEAPM-VITYL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 563 IDLDHI-QNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTG 641
Cdd:PRK06188 326 RKRDHDpDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLH-------TG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 642 DLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-EEKY---------LSAYITGDIEMEGSF 711
Cdd:PRK06188 399 DVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVpDEKWgeavtavvvLRPGAAVDAAELQAH 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 2085927195 712 VQEK--LAQAlpkymiPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK06188 479 VKERkgSVHA------PKQVDFVDSLPLTALGKPDKKAL 511
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
404-745 |
1.44e-30 |
|
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: 123.28 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 404 YVIYTSGTSGKPKGVKVKNKSLVNYslWVC--DQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKevyLHSL 481
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIES--FVCneDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK---FNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 482 SLIEYIHKNSITYLKMTPTLFSTLmedVDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVgcIAH 561
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTMLQAL---ARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF--ITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 562 SIDldhiQNCEIYNKIGRPIHGINIYIVDRSDqlvpvGAPGEICISGVGLASGYVNNEELTNEKFidnpfhpgakmYKTG 641
Cdd:cd17633 154 NFN----QESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 642 DLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKY----LSAYITGDiEMEGSFVQEKLA 717
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARfgeiAVALYSGD-KLTYKQLKRFLK 292
|
330 340
....*....|....*....|....*...
gi 2085927195 718 QALPKYMIPSFIIQLKELPLTANGKINR 745
Cdd:cd17633 293 QKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
269-748 |
1.66e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 123.84 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRI 348
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 349 NHILKDSKADILITDLCF-----LADKNIAAECLDITDKSIYTSQNTSNPDVQYDLEDEVY-VIYTSGTSGKPKGVKvkn 422
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFdaivaLETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVM--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 423 KSLVNYSLWVCDQI---NINSDSRSLVTSK-YSFDLCYTSIFPVLSGGGqvhFVDKEVYLHSLSLIEYIHKNSITYLKMT 498
Cdd:PRK06145 169 HSYGNLHWKSIDHVialGLTASERLLVVGPlYHVGAFDLPGIAVLWVGG---TLRIHREFDPEAVLAAIERHRLTCAWMA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 499 PTLFSTLME-------DVDMLASCpdlkviILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGciahsiDLDHIQNC 571
Cdd:PRK06145 246 PVMLSRVLTvpdrdrfDLDSLAWC------IGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSG------DTLMEAGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 572 EIyNKI---GRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmyKTGDLGRWMP 648
Cdd:PRK06145 314 EI-EKIgstGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 649 DGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDI------EMEGSFVQEKLAQALPK 722
Cdd:PRK06145 386 EGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVvlnpgaTLTLEALDRHCRQRLAS 465
|
490 500
....*....|....*....|....*.
gi 2085927195 723 YMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK06145 466 FKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
269-756 |
6.24e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 123.23 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIddeSPVSR- 347
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV---SPLFRe 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 348 --INHILKDSKADILIT--------------------------DLC-----------FLADKNIAAECLDITDKSIYTSQ 388
Cdd:PRK06178 120 heLSYELNDAGAEVLLAldqlapvveqvraetslrhvivtslaDVLpaeptlplpdsLRAPRLAAAGAIDLLPALRACTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 389 NTsnPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLV-----NYSLWVcdqiNINSDSRSLvtskySF---------DL 454
Cdd:PRK06178 200 PV--PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaaaAYAVAV----VGGEDSVFL-----SFlpefwiageNF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 455 CYtsIFPVLSGGGQVHFV--DKEVYLhslsliEYIHKNSITYLKMTPTLFSTLME-----DVDmLASCPDLKVIILgges 527
Cdd:PRK06178 269 GL--LFPLFSGATLVLLArwDAVAFM------AAVERYRVTRTVMLVDNAVELMDhprfaEYD-LSSLRQVRVVSF---- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 528 inignVKKL--AEKCRWMKFINH------YGPTES------TVGCIAHSIDLdhiQNCEIYnkIGRPIHGINIYIVD-RS 592
Cdd:PRK06178 336 -----VKKLnpDYRQRWRALTGSvlaeaaWGMTEThtcdtfTAGFQDDDFDL---LSQPVF--VGLPVPGTEFKICDfET 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 593 DQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIG 672
Cdd:PRK06178 406 GELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLH-------TGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 673 EIENQLLQLEGIKEAAVV--YIEEK--YLSAYIT--GDIEMEGSFVQEKLAQALPKYMIPSFIIqLKELPLTANGKINRK 746
Cdd:PRK06178 479 EVEALLGQHPAVLGSAVVgrPDPDKgqVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQ 557
|
570
....*....|
gi 2085927195 747 ELpLPDLQRL 756
Cdd:PRK06178 558 DL-QALAEEL 566
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
266-748 |
1.46e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 121.12 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 266 EERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLM-EKGAGKNSITAMMIRPS-EYSMIgILGILKTGSAFLPIDDES 343
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSlEYIVL-LFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 344 PVSRINHILKDSKADILitdlcfLADKNIAAECLDITDKS----------IYTSQNTSNPDVQYDLEDEVYVI-YTSGTS 412
Cdd:PRK06839 88 TENELIFQLKDSGTTVL------FVEKTFQNMALSMQKVSyvqrvisitsLKEIEDRKIDNFVEKNESASFIIcYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 413 GKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYsFDLCYTSIF--PVLSGGGQVHFVDKEVYLHSLSLIEyihKN 490
Cdd:PRK06839 162 GKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFafPTLFAGGVIIVPRKFEPTKALSMIE---KH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 491 SITYLKMTPTLFSTLMEDVDMLAscPDLKVIIL---GGESINIGNVKKLAEkcRWMKFINHYGPTES--TVGCIAHSidl 565
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCSKFET--TNLQSVRWfynGGAPCPEELMREFID--RGFLFGQGFGMTETspTVFMLSEE--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 566 DHIQNCeiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGR 645
Cdd:PRK06839 311 DARRKV---GSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC-------TGDLAR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 646 WMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-EEKYLSAYITGDIEMEGSFVQEK-----LAQA 719
Cdd:PRK06839 381 VDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRqHVKWGEIPIAFIVKKSSSVLIEKdviehCRLF 460
|
490 500
....*....|....*....|....*....
gi 2085927195 720 LPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK06839 461 LAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
255-748 |
1.55e-28 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 121.41 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 255 YTVNKTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGK---------NSItammirpsEYsMIG 325
Cdd:COG1021 21 YWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgdrvvvqlpNVA--------EF-VIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 326 ILGILKTGSAflpiddesPV--------SRINHILKDSKADILItdlcfladknIAAECLDITDKSIYTSQNTSNPDVQY 397
Cdd:COG1021 92 FFALFRAGAI--------PVfalpahrrAEISHFAEQSEAVAYI----------IPDRHRGFDYRALARELQAEVPSLRH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 398 -----------DLE----------------DEVYVIYTS-GTSGKPKgvkvknksLV----N---YSLWVCDQI-NINSD 441
Cdd:COG1021 154 vlvvgdageftSLDallaapadlseprpdpDDVAFFQLSgGTTGLPK--------LIprthDdylYSVRASAEIcGLDAD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 442 SRSLVTS--KYSFDLCYTSIFPVLSGGGQVhfvdkeVYLHSLS------LIEyihKNSITYLKMTPTLFSTLMEDVDM-- 511
Cdd:COG1021 226 TVYLAALpaAHNFPLSSPGVLGVLYAGGTV------VLAPDPSpdtafpLIE---RERVTVTALVPPLALLWLDAAERsr 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 512 --LAScpdLKVIILGGesinignvKKLAE----------KCRwmkFINHYGPTESTVGC--IAHSIDLdhiqnceIYNKI 577
Cdd:COG1021 297 ydLSS---LRVLQVGG--------AKLSPelarrvrpalGCT---LQQVFGMAEGLVNYtrLDDPEEV-------ILTTQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 578 GRPI-HGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFLG 656
Cdd:COG1021 356 GRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 657 RIDNQIkIRGfrveiGE------IENQLLQLEGIKEAAVVYIEEKYLS----AYITGD------IEMEgSFVQEklaQAL 720
Cdd:COG1021 430 RAKDQI-NRG-----GEkiaaeeVENLLLAHPAVHDAAVVAMPDEYLGerscAFVVPRgepltlAELR-RFLRE---RGL 499
|
570 580
....*....|....*....|....*...
gi 2085927195 721 PKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:COG1021 500 AAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
407-748 |
2.22e-28 |
|
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: 120.81 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 407 YTSGTSGKPKGVKVKNKSLVNYSLWVCDQININ---SDSRSLVTSKY---SFDLCYTSifpVLSGGGQVhFVDKevYLHS 480
Cdd:cd12119 170 YTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGlseSDVVLPVVPMFhvnAWGLPYAA---AMVGAKLV-LPGP--YLDP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 481 LSLIEYIHKNSITYLKMTPTLFSTLMEDVD----MLAScpdLKVIILGGESINIGNVKKLAEkcRWMKFINHYGPTE-ST 555
Cdd:cd12119 244 ASLAELIEREGVTFAAGVPTVWQGLLDHLEangrDLSS---LRRVVIGGSAVPRSLIEAFEE--RGVRVIHAWGMTEtSP 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 556 VGCIAHS----IDLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPV--GAPGEICISGVGLASGYVNNEELTNEKFIDN 629
Cdd:cd12119 319 LGTVARPpsehSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 630 PFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-----EEKYLsAYITgd 704
Cdd:cd12119 399 WLR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVphpkwGERPL-AVVV-- 468
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2085927195 705 iEMEGSFVQEK-----LAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd12119 469 -LKEGATVTAEellefLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
280-745 |
2.84e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 119.47 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 280 YAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKAdi 359
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 360 litdlcfladkniaaeclditdKSIYTSQNtsnpdvqydlEDEVYVIYTSGTSGKPKGVKVKNKSLVNyslwvcdqiNIN 439
Cdd:cd05914 81 ----------------------KAIFVSDE----------DDVALINYTSGTTGNSKGVMLTYRNIVS---------NVD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 440 SDSRSLVTSK-----------YSFDLCYTSIFPVLSgGGQVHFVDKEvylhSLSLIEYIHKNSITYLKMTPTLFstLMED 508
Cdd:cd05914 120 GVKEVVLLGKgdkilsilplhHIYPLTFTLLLPLLN-GAHVVFLDKI----PSAKIIALAFAQVTPTLGVPVPL--VIEK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 509 VDMLASCP----------------------------------DLKVIILGGESINignvKKLAEKCRWMKF--INHYGPT 552
Cdd:cd05914 193 IFKMDIIPkltlkkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKIN----PDVEEFLRTIGFpyTIGYGMT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 553 EsTVGCIAHSidldhIQNCEIYNKIGRPIHGINIYIVDRSdqlvPVGAPGEICISGVGLASGYVNNEELTNEKFIDNP-F 631
Cdd:cd05914 269 E-TAPIISYS-----PPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGwF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 632 HpgakmykTGDLGRWMPDGNIEFLGRIDNQIKI-RGFRVEIGEIENQLLQLEGIKEAAVVYIEEK-YLSAYITGDIEMEG 709
Cdd:cd05914 339 H-------TGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKlVALAYIDPDFLDVK 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2085927195 710 SF------------VQEKLAQALPKY-MIPSFIIQLKELPLTANGKINR 745
Cdd:cd05914 412 ALkqrniidaikweVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
258-748 |
6.24e-28 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 119.40 E-value: 6.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 258 NKTIQDLFEERAEKTPDQTAAVY---AGK--HITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKT 332
Cdd:PRK08008 6 GQHLRQMWDDLADVYGHKTALIFessGGVvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 333 GSAFLPIDDESPVSRINHILKDSKADILITDLCFL---------AD---KNI--AAECLDITDKSIYTSQNTSNPDVQYD 398
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSAQFYpmyrqiqqeDAtplRHIclTRVALPADDGVSSFTQLKAQQPATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 399 L------EDEVYVIYTSGTSGKPKGVKVKNKSLV---NYSLWvcdQININSDSRSL-VTSKYSFDLCYTSIFPVLSGGGQ 468
Cdd:PRK08008 166 YapplstDDTAEILFTSGTTSRPKGVVITHYNLRfagYYSAW---QCALRDDDVYLtVMPAFHIDCQCTAAMAAFSAGAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 469 vhFVDKEVYLHSlSLIEYIHKNSITYLKMTPTLFSTLMedvdMLASCPD-----LKVIILggeSINIGNVKKLAEKCRW- 542
Cdd:PRK08008 243 --FVLLEKYSAR-AFWGQVCKYRATITECIPMMIRTLM----VQPPSANdrqhcLREVMF---YLNLSDQEKDAFEERFg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 543 MKFINHYGPTESTVGCIAhsidlDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGV---GLASGYVNNE 619
Cdd:PRK08008 313 VRLLTSYGMTETIVGIIG-----DRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 620 ELTNEKfidnpFHPGAKMYkTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV----YIEEK 695
Cdd:PRK08008 388 KATAKV-----LEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVgikdSIRDE 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2085927195 696 YLSAYItgdIEMEGSFVQEK-----LAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK08008 462 AIKAFV---VLNEGETLSEEeffafCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
405-743 |
1.75e-27 |
|
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: 114.52 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 405 VIYTSGTSGKPKGVKVKNK-SLVNYSLWvCDQININSDSRSLVTSKYSFDLCYTS-IFPVLSGGGQVHfvdKEVYLHSLS 482
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRqTLRAAAAW-ADCADLTEDDRYLIINPFFHTFGYKAgIVACLLTGATVV---PVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 483 LIEYIHKNSITYLKMTPTLFSTLMEDVDM----LAScpdLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGC 558
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRkkfdLSS---LRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 559 IAHSIDldhiQNCEIYNKIGRPIHGINIYIVDrsdqlvpvgaPGEICISGVGLASGYVNNEELTnEKFIDNP--FHpgak 636
Cdd:cd17638 158 MCRPGD----DAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEAT-AEAIDADgwLH---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 637 mykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYITG------DIE 706
Cdd:cd17638 219 ---TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGevgkAFVVArpgvtlTEE 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 2085927195 707 MEGSFVQEKLAQalpkYMIPSFIIQLKELPLTANGKI 743
Cdd:cd17638 296 DVIAWCRERLAN----YKVPRFVRFLDELPRNASGKV 328
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
405-748 |
5.53e-27 |
|
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: 112.81 E-value: 5.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 405 VIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVtskySFDLCYTS----IFPVLSGGGQVHFVDKEvylhs 480
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLL----SLPLYHVGglaiLVRSLLAGAELVLLERN----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 481 LSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKcRWMKFINhYGPTEsTVGCIA 560
Cdd:cd17630 76 QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTT-YGMTE-TASQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 561 HSIDLDHIQNceiynKIGRPIHGINIYIVDRsdqlvpvgapGEICISGVGLASGYVNNEeLTNEKFIDNPFHpgakmykT 640
Cdd:cd17630 153 TKRPDGFGRG-----GVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-LVPEFNEDGWFT-------T 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 641 GDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-EEKY---LSAYITGDIEMEGSFVQEKL 716
Cdd:cd17630 210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVpDEELgqrPVAVIVGRGPADPAELRAWL 289
|
330 340 350
....*....|....*....|....*....|..
gi 2085927195 717 AQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd17630 290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
398-746 |
9.49e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 118.10 E-value: 9.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 398 DLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSK--YSFDLCYTSIFPVLSGGGQVHFVDKe 475
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPffHSFGLTVTLWLPLLEGIKVVYHPDP- 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 476 vyLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDV----DMLAScpdLKVIILGGESINignvKKLAEKCRwMKF----IN 547
Cdd:PRK08633 859 --TDALGIAKLVAKHRATILLGTPTFLRLYLRNKklhpLMFAS---LRLVVAGAEKLK----PEVADAFE-EKFgiriLE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 548 HYGPTEST----VGCIAHSIDLDHIQnceIYNK---IGRPIHGINIYIVD-RSDQLVPVGAPGEICISGVGLASGYVNNE 619
Cdd:PRK08633 929 GYGATETSpvasVNLPDVLAADFKRQ---TGSKegsVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDP 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 620 ELTNE--KFIDnpfhpGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQL--EGIKEAAVVYIE-- 693
Cdd:PRK08633 1006 EKTAEviKDID-----GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVFAVTAVPde 1080
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2085927195 694 ---EKYLSAYITGDIEMEGsfVQEKLAQA-LPKYMIPSFIIQLKELPLTANGKINRK 746
Cdd:PRK08633 1081 kkgEKLVVLHTCGAEDVEE--LKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
286-748 |
1.00e-26 |
|
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: 114.40 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVATLLMEKGAGKNSITAMMIrPS--EYSMIgILGILKTGSAFLPIddeSPVSR---INHILKDSKADIL 360
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQL-PNwwEFAVL-YLACLRIGAVTNPI---LPFFReheLAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 361 ITDLCFlADKNIAAEclditdksiytsqntsnPDvqydleDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININS 440
Cdd:cd05903 78 VVPERF-RQFDPAAM-----------------PD------AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 441 DSRSLVTSkysfdlcytsifPVLSGGGQVHFVDKEVYLHSLSLI----------EYIHKNSITYLKMTPTLFSTLMEDVD 510
Cdd:cd05903 134 GDVFLVAS------------PMAHQTGFVYGFTLPLLLGAPVVLqdiwdpdkalALMREHGVTFMMGATPFLTDLLNAVE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 511 MLAS-CPDLKVIILGGESINiGNVKKLAEKCRWMKFINHYGPTE--STVGCIAhSIDLDHIQNCEiynkiGRPIHGINIY 587
Cdd:cd05903 202 EAGEpLSRLRTFVCGGATVP-RSLARRAAELLGAKVCSAYGSTEcpGAVTSIT-PAPEDRRLYTD-----GRPLPGVEIK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 588 IVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEFLGRIDNQIkIR-G 666
Cdd:cd05903 275 VVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYLRITGRSKDII-IRgG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 667 FRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYI---TG---DIEMEGSFVqekLAQALPKYMIPSFIIQLKELP 736
Cdd:cd05903 347 ENIPVLEVEDLLLGHPGVIEAAVVALPDERLGeracAVVvtkSGallTFDELVAYL---DRQGVAKQYWPERLVHVDDLP 423
|
490
....*....|..
gi 2085927195 737 LTANGKINRKEL 748
Cdd:cd05903 424 RTPSGKVQKFRL 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
285-748 |
1.08e-26 |
|
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: 115.10 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDL 364
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 365 CFLADKNIAAECLDIT--------DKSIYTSQNTSNPDVQYDL-----------EDEVYVIYTSGTSGKPKGVKVKNKSL 425
Cdd:cd05926 95 GELGPASRAASKLGLAilelaldvGVLIRAPSAESLSNLLADKknaksegvplpDDLALILHTSGTTGRPKGVPLTHRNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 426 VNYSLWVCDQININSDSRSL-VTSKYSFDLCYTSIFPVLSGGGQVHFVDKevyLHSLSLIEYIHKNSITYLKMTPTLFST 504
Cdd:cd05926 175 AASATNITNTYKLTPDDRTLvVMPLFHVHGLVASLLSTLAAGGSVVLPPR---FSASTFWPDVRDYNATWYTAVPTIHQI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 505 LMEDVDMLASCPD--LKVIILGGESINIGNVKKLAEKcrwmkF----INHYGPTEStvgciAHSIDLDHI-QNCEIYNKI 577
Cdd:cd05926 252 LLNRPEPNPESPPpkLRFIRSCSASLPPAVLEALEAT-----FgapvLEAYGMTEA-----AHQMTSNPLpPGPRKPGSV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 578 GRPiHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGR 657
Cdd:cd05926 322 GKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLDADGYLFLTGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 658 IDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-EEKY---LSAYItgdIEMEGSFVQEK-----LAQALPKYMIPSF 728
Cdd:cd05926 395 IKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpDEKYgeeVAAAV---VLREGASVTEEelrafCRKHLAAFKVPKK 471
|
490 500
....*....|....*....|
gi 2085927195 729 IIQLKELPLTANGKINRKEL 748
Cdd:cd05926 472 VYFVDELPKTATGKIQRRKV 491
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
857-1018 |
2.42e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.57 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 857 SSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEFDYQKLP 936
Cdd:PRK12467 53 SYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDDLA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 937 SDG-------IRPYVK-QFIRPFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGH------K 1001
Cdd:PRK12467 133 NEQgraresqIEAYINeEVARPFDLANGPLLRVRLLRLaDDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepS 212
|
170
....*....|....*..
gi 2085927195 1002 LKQPPLQSKDYSEWQVS 1018
Cdd:PRK12467 213 LPALPIQYADYAIWQRS 229
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
352-748 |
5.56e-26 |
|
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: 113.20 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 352 LKDSKADILitdlcfLADKNIAAECLDITDKSIYTSQNTSNpdvqYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLW 431
Cdd:cd05909 109 LEDLRAKIS------KADKCKAFLAGKFPPKWLLRIFGVAP----VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 432 VCDQININSDSR--SLVTSKYSFDLCYTSIFPVLSGGGQVHFVDKevyLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDV 509
Cdd:cd05909 179 ITAIFDPNPEDVvfGALPFFHSFGLTGCLWLPLLSGIKVVFHPNP---LDYKKIPELIYDKKATILLGTPTFLRGYARAA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 510 --DMLAScpdLKVIILGGESINiGNVKKLAEKCRWMKFINHYGPTESTvGCIAHSIDLDHiqnceiyNK---IGRPIHGI 584
Cdd:cd05909 256 hpEDFSS---LRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTECS-PVISVNTPQSP-------NKegtVGRPLPGM 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 585 NIYIVDRSDQL-VPVGAPGEICISGVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEFLGRIDNQIK 663
Cdd:cd05909 324 EVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDG-------WYDTGDIGKIDGEGFLTITGRLSRFAK 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 664 IRGFRVEIGEIENQLLQLEGIK-EAAVVYIE-----EKYLSAYITGDIEMEGsfVQEKLAQA-LPKYMIPSFIIQLKELP 736
Cdd:cd05909 397 IAGEMVSLEAIEDILSEILPEDnEVAVVSVPdgrkgEKIVLLTTTTDTDPSS--LNDILKNAgISNLAKPSYIHQVEEIP 474
|
410
....*....|..
gi 2085927195 737 LTANGKINRKEL 748
Cdd:cd05909 475 LLGTGKPDYVTL 486
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
273-743 |
6.43e-26 |
|
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: 113.83 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 273 PDQTAAVYAG------KHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI----DDE 342
Cdd:cd17634 67 GDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfggfAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 343 SPVSRINhilkDSKADILITDLCFLAD------KNIAAECLDITDKSIYT--------------------------SQNT 390
Cdd:cd17634 147 AVAGRII----DSSSRLLITADGGVRAgrsvplKKNVDDALNPNVTSVEHvivlkrtgsdidwqegrdlwwrdliaKASP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 391 SNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWvcdqininsdsrslvTSKYSFDL-------CYTSIF--- 460
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAAT---------------TMKYVFDYgpgdiywCTADVGwvt 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 461 --------PVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLM-EDVDMLA--SCPDLKVIILGGESIN 529
Cdd:cd17634 288 ghsyllygPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMaAGDDAIEgtDRSSLRILGSVGEPIN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 530 IGN----VKKLA-EKCrwmKFINHYGPTESTVGCIAhsidldhIQNCEIYNKIG---RPIHGINIYIVDRSDQLVPVGAP 601
Cdd:cd17634 368 PEAyewyWKKIGkEKC---PVVDTWWQTETGGFMIT-------PLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 602 GEICISGV--GLASGYVNNEEltneKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLL 679
Cdd:cd17634 438 GNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLV 513
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2085927195 680 QLEGIKEAAVVYIEE----KYLSAYIT---GDIEMEGSF--VQEKLAQALPKYMIPSFIIQLKELPLTANGKI 743
Cdd:cd17634 514 AHPKVAEAAVVGIPHaikgQAPYAYVVlnhGVEPSPELYaeLRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
4-227 |
8.79e-26 |
|
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: 111.39 E-value: 8.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 4 SSKPVFQSSADEGGFNNRKKTFIIDETCTSMlKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGI 83
Cdd:cd19536 200 LATLPALSEAVGGGPEQDSELLVSVPLPVRS-RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 84 EKMVGLFINAVPLRVKGDGDTVfIALAQKLNSDFIKAnTSYGYSSLADIQALTKmKEKLINHMLVYENYPVDDyGKAVDD 163
Cdd:cd19536 279 ERLLGLFLNTLPLRVTLSEETV-EDLLKRAQEQELES-LSHEQVPLADIQRCSE-GEPLFDSIVNFRHFDLDF-GLPEWG 354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 164 TTDALRITDMEVFEQTNYDFGLVIIP-GSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19536 355 SDEGMRRGLLFSEFKSNYDVNLSVLPkQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
259-748 |
1.37e-25 |
|
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: 111.65 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 259 KTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSiTAMMIRPS--EYsMIGILGILKTGSAf 336
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGD-RVVVQLPNvaEF-VVLFFALLRLGAV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 lpiddesPV--------SRINHILKDSKADILITDlcflaDKNiaaeclditdkSIYTSQNTSNpDVQYDLEDEVYVIYT 408
Cdd:cd05920 92 -------PVlalpshrrSELSAFCAHAEAVAYIVP-----DRH-----------AGFDHRALAR-ELAESIPEVALFLLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 409 SGTSGKPKGVKVKNKSLVnYSLWVCDQI-NINSDSRSLVT--SKYSFDLCYTSIFPVLSGGGQVHFVDKEVYLHSLSLIE 485
Cdd:cd05920 148 GGTTGTPKLIPRTHNDYA-YNVRASAEVcGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPLIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 486 yihKNSITYLKMTPTLFSTLMEDV----DMLAScpdLKVIILGGESINIGNVKKLAEK--CRWMKFinhYGPTESTVgCI 559
Cdd:cd05920 227 ---REGVTVTALVPALVSLWLDAAasrrADLSS---LRLLQVGGARLSPALARRVPPVlgCTLQQV---FGMAEGLL-NY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 560 AHSIDLDHIqnceIYNKIGRPIH-GINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmY 638
Cdd:cd05920 297 TRLDDPDEV----IIHTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------Y 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 639 KTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYIT-GDIEMEGSFVQ 713
Cdd:cd05920 367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGerscAFVVlRDPPPSAAQLR 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 2085927195 714 EKLAQA-LPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05920 447 RFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
267-748 |
1.56e-25 |
|
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: 111.94 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 267 ERAEKTPDQTAAVYA--GKHITYKELNEKANQVATLLMEKGAGKNSiTAMMIRPS--EYSMIgILGILKTGSAFLPIDDE 342
Cdd:cd05904 13 LFASAHPSRPALIDAatGRALTYAELERRVRRLAAGLAKRGGRKGD-VVLLLSPNsiEFPVA-FLAVLSLGAVVTTANPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 343 SPVSRINHILKDSKADILITDLCF---LADKNIAAECLD------ITDKSIYTSQNTSNPDVQYDLEDEVYVI-YTSGTS 412
Cdd:cd05904 91 STPAEIAKQVKDSGAKLAFTTAELaekLASLALPVVLLDsaefdsLSFSDLLFEADEAEPPVVVIKQDDVAALlYSSGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 413 GKPKGVKVKNKSLV-NYSLWVCDQ-ININSDSRSLVTSK----YSFDLCYTSIfpvLSGGGQV----HFVDKEVylhsLS 482
Cdd:cd05904 171 GRSKGVMLTHRNLIaMVAQFVAGEgSNSDSEDVFLCVLPmfhiYGLSSFALGL---LRLGATVvvmpRFDLEEL----LA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 483 LIEyihKNSITYLKMTPTLF-----STLMEDVDMLAscpdLKVIILGGESINignvKKLAEKCR----WMKFINHYGPTE 553
Cdd:cd05904 244 AIE---RYKVTHLPVVPPIVlalvkSPIVDKYDLSS----LRQIMSGAAPLG----KELIEAFRakfpNVDLGQGYGMTE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 554 STvgCIAHSIDLDHIQNCEiYNKIGRPIHGINIYIVDRSD-QLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFh 632
Cdd:cd05904 313 ST--GVVAMCFAPEKDRAK-YGSVGRLVPNVEAKIVDPETgESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 633 pgakmYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKylsayITGDIEM----- 707
Cdd:cd05904 389 -----LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDE-----EAGEVPMafvvr 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2085927195 708 -EGSFVQEKLAQA-LPKYMIP-------SFIiqlKELPLTANGKINRKEL 748
Cdd:cd05904 459 kPGSSLTEDEIMDfVAKQVAPykkvrkvAFV---DAIPKSPSGKILRKEL 505
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
260-748 |
1.63e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 111.79 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKgAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI 339
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEK-ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILITDLCFLADKnIAAEC--LDITDKSIYTSQNTSNPDVQYDLEDE-VYVIYTSGTSGKPK 416
Cdd:PRK07638 81 DIKWKQDELKERLAISNADMIVTERYKLNDL-PDEEGrvIEIDEWKRMIEKYLPTYAPIENVQNApFYMGFTSGSTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 417 GVKVKNKSLVNYSLWVCDQININSDSR-----SLVTSKYSFDLCYTsifpvLSGGGQVHFVDKEVYLHSLsliEYIHKNS 491
Cdd:PRK07638 160 AFLRAQQSWLHSFDCNVHDFHMKREDSvliagTLVHSLFLYGAIST-----LYVGQTVHLMRKFIPNQVL---DKLETEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 492 ITYLKMTPTLFSTLMEdVDMLASCPDLkvIILGGESINIGNVKKLAEKCRWMKFINHYGPTE-STVGCIAHSidldhiQN 570
Cdd:PRK07638 232 ISVMYTVPTMLESLYK-ENRVIENKMK--IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASElSFVTALVDE------ES 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 571 CEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEkfidnpfhPGAKMYKT-GDLGRWMPD 649
Cdd:PRK07638 303 ERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE--------LNADGWMTvRDVGYEDEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 650 GNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYITG--DIEMEGSFVQEKlaqaLPKY 723
Cdd:PRK07638 375 GFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGekpvAIIKGsaTKQQLKSFCLQR----LSSF 450
|
490 500
....*....|....*....|....*
gi 2085927195 724 MIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK07638 451 KIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
842-1018 |
1.80e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 114.67 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 842 YPVISKARKQSYYQASSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQI 921
Cdd:PRK12316 38 FPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 922 IHD--TWELEF-DYQKLPSDGIRPYV-----KQFIRPFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGIIRKE 992
Cdd:PRK12316 118 VPLdrPLEVEFeDCSGLPEAEQEARLrdeaqRESLQPFDLCEGPLLRVRLLRLgEEEHVLLLTLHHIVSDGWSMNVLIEE 197
|
170 180 190
....*....|....*....|....*....|..
gi 2085927195 993 FNALYAGH------KLKQPPLQSKDYSEWQVS 1018
Cdd:PRK12316 198 FSRFYSAYatgaepGLPALPIQYADYALWQRS 229
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
2-227 |
2.02e-25 |
|
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: 110.48 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 2 NMSSKPVFQSSAD-EGGFNNRKKTFiiDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRV 80
Cdd:cd19547 199 DLTPSPFSTAPADrEGEFDTVVHEF--PEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 81 QGIEKMVGLFINAVPLRVKGDGDTVFIALAQKLNSDfIKANTSYGYSSLADIQALTKMKE----KLINHMLVYENYPVDD 156
Cdd:cd19547 277 EGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRD-LATTAAHGHVPLAQIKSWASGERlsggRVFDNLVAFENYPEDN 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 157 ygkaVDDTTDALRITDMEVFEQTNYDFGLVIIPGSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19547 356 ----LPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
285-745 |
3.09e-25 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 109.92 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDL 364
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 365 cfladkniaaeclditdksiytsqntsnpDVQYDLEDEVYV-IYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSR 443
Cdd:cd05973 81 -----------------------------ANRHKLDSDPFVmMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 444 --SLVTSKYSFDLCYTSIFPVLSG-------GGqvhFVDKEVYlhslsliEYIHKNSITYLKMTPTLFSTLMEDVDMLAS 514
Cdd:cd05973 132 fwNAADPGWAYGLYYAITGPLALGhptilleGG---FSVESTW-------RVIERLGVTNLAGSPTAYRLLMAAGAEVPA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 515 CPD--LKVIILGGESINiGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHIQNceiyNKIGRPIHGINIYIVDRS 592
Cdd:cd05973 202 RPKgrLRRVSSAGEPLT-PEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVHA----GSAGRAMPGWRVAVLDDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 593 DQLVPVGAPGEICI----SGVGLASGYVNNEELTnekfidnpfhPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFR 668
Cdd:cd05973 277 GDELGPGEPGRLAIdianSPLMWFRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 669 VEIGEIENQLLQLEGIKEAAVVYIEE----KYLSAYITGDIEMEGSfvqEKLAQALPKYM--------IPSFIIQLKELP 736
Cdd:cd05973 347 IGPFDVESALIEHPAVAEAAVIGVPDpertEVVKAFVVLRGGHEGT---PALADELQLHVkkrlsahaYPRTIHFVDELP 423
|
....*....
gi 2085927195 737 LTANGKINR 745
Cdd:cd05973 424 KTPSGKIQR 432
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
857-1016 |
4.44e-25 |
|
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: 109.28 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 857 SSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQII--HDTWELEFDYQK 934
Cdd:cd19538 5 SFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLIleEDEATPKLEIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 935 LPSDGIRPYVKQFIR-PFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGH-KLKQP-----P 1006
Cdd:cd19538 85 VDEEELESEINEAVRyPFDLSEEPPFRATLFeLGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARcKGEAPelaplP 164
|
170
....*....|
gi 2085927195 1007 LQSKDYSEWQ 1016
Cdd:cd19538 165 VQYADYALWQ 174
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
29-227 |
4.88e-25 |
|
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: 108.93 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 29 ETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGIEKMVGLFINAVPLRVKGDGDTVFIA 108
Cdd:cd19542 205 RRSLAKLEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 109 LAQKLNSDFIkANTSYGYSSLADIQ-ALTKMKEK-LINHMLVYENYPvddygkAVDDTTDALRITDMEVFEQ--TNYDFG 184
Cdd:cd19542 285 LLRQLQQQYL-RSLPHQHLSLREIQrALGLWPSGtLFNTLVSYQNFE------ASPESELSGSSVFELSAAEdpTEYPVA 357
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2085927195 185 LVIIP-GSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19542 358 VEVEPsGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
263-748 |
7.08e-25 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 110.28 E-value: 7.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 263 DLFEERAEKTPDQTAAVYAGKH-----ITYKELNEKANQVATLLMEKGAGKNSiTAMMIRPSEYSM-IGILGILKTGSAF 336
Cdd:cd05970 21 DVVDAMAKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGD-TVMLTLKRRYEFwYSLLALHKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 LP----IDDESPVSRINhilkdsKADILItdLCFLADKNI-------AAECldiTDKSIYTSQNTSNPDVQYDLEDEV-- 403
Cdd:cd05970 100 IPathqLTAKDIVYRIE------SADIKM--IVAIAEDNIpeeiekaAPEC---PSKPKLVWVGDPVPEGWIDFRKLIkn 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 404 --------------------YVIYTSGTSGKPKGVKVKNK----SLVNYSLWVcdqiNINSDSRSLVTSKYSFDLC-YTS 458
Cdd:cd05970 169 aspdferptansypcgedilLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQ----NVREGGLHLTVADTGWGKAvWGK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 459 IFPVLSGGGQVHFVDKEVYLHSlSLIEYIHKNSITYLKMTPTLFSTLM-EDVDM--LAScpdLKVIILGGESINIGNVKK 535
Cdd:cd05970 245 IYGQWIAGAAVFVYDYDKFDPK-ALLEKLSKYGVTTFCAPPTIYRFLIrEDLSRydLSS---LRYCTTAGEALNPEVFNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 536 LAEKCRwMKFINHYGPTESTVgCIAHsidldhIQNCEIY-NKIGRPIHGINIYIVDRSDQLVPVGAPGEICIS-----GV 609
Cdd:cd05970 321 FKEKTG-IKLMEGFGQTETTL-TIAT------FPWMEPKpGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 610 GLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGrWM-PDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAA 688
Cdd:cd05970 393 GLFGGYYKDAEKTAEVWHDGYYH-------TGDAA-WMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECA 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085927195 689 VVYIEE----KYLSAYITGDIEMEGSFVQEKLAQALPK-----YMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05970 465 VTGVPDpirgQVVKATIVLAKGYEPSEELKKELQDHVKkvtapYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
269-748 |
1.78e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 108.36 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAV--YAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVS 346
Cdd:PRK09088 5 ARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 347 RINHILKDSKADILitdlcfLADKNIAAECLDITDKSIYTSQ---NTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNK 423
Cdd:PRK09088 85 ELDALLQDAEPRLL------LGDDAVAAGRTDVEDLAAFIASadaLEPADTPSIPPERVSLILFTSGTSGQPKGVMLSER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 424 SLvnyslwvcDQININSDSRSLVTSKYSFdLC----------YTSIFPVLSGGGQVHFVD------KEVYLHSLSLieyi 487
Cdd:PRK09088 159 NL--------QQTAHNFGVLGRVDAHSSF-LCdapmfhiiglITSVRPVLAVGGSILVSNgfepkrTLGRLGDPAL---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 488 hknSITYLKMTPTLfstlmedVDMLASCPDLKVIILGG-ESINIGNVKKLAEKCRW-----MKFINHYGPTES-TVgcIA 560
Cdd:PRK09088 226 ---GITHYFCVPQM-------AQAFRAQPGFDAAALRHlTALFTGGAPHAAEDILGwlddgIPMVDGFGMSEAgTV--FG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 561 HSIDLDHIQNceiynKIGR---PIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFidnpfhPGAKM 637
Cdd:PRK09088 294 MSVDCDVIRA-----KAGAagiPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 638 YKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI------EEKYLSAYITGDIEMEGSF 711
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMadaqwgEVGYLAIVPADGAPLDLER 442
|
490 500 510
....*....|....*....|....*....|....*..
gi 2085927195 712 VQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK09088 443 IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
285-707 |
4.54e-24 |
|
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: 106.53 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPS-EYSMIGiLGILKTGSAFLPIDDESPVSRINHILKDSKADILITD 363
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRpEWTIAD-LAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 364 lcfladkniaaeclditdksiytsqntsnpdvqyDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSR 443
Cdd:cd05907 85 ----------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 444 SLvtskySF-DLC------YTSIFPVLSGGGQVHFVDKEVYLHSLSLIEYihknsiTYLKMTPTLF------------ST 504
Cdd:cd05907 131 HL-----SFlPLAhvferrAGLYVPLLAGARIYFASSAETLLDDLSEVRP------TVFLAVPRVWekvyaaikvkavPG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 505 LMEDVDMLASCPDLKVIILGGESINignvkklAEKCRWMK-----FINHYGPTEST-VGCIAHSIDLDHiqnceiyNKIG 578
Cdd:cd05907 200 LKRKLFDLAVGGRLRFAASGGAPLP-------AELLHFFRalgipVYEGYGLTETSaVVTLNPPGDNRI-------GTVG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 579 RPIHGINIYIVDRsdqlvpvgapGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRI 658
Cdd:cd05907 266 KPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRK 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2085927195 659 DNQIKIRGFR-VEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEM 707
Cdd:cd05907 330 KDLIITSGGKnISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEA 379
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
259-748 |
5.44e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 107.54 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 259 KTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMI--RPsEYsMIGILGILKTGSAF 336
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCgnRI-EF-LDVFLGCAWLGAIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 LPIDDESPVSRINHILKDSKADILITDLCFLAD-KNIAAECLDITDKSIYTSQNTSNPDVQYDLE--------------- 400
Cdd:PRK06155 99 VPINTALRGPQLEHILRNSGARLLVVEAALLAAlEAADPGDLPLPAVWLLDAPASVSVPAGWSTAplppldapapaaavq 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 401 --DEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTskysFDLCYT----SIFPVLSGGGQVHFVDK 474
Cdd:PRK06155 179 pgDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTT----LPLFHTnalnAFFQALLAGATYVLEPR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 475 evylHSLS-----LIEyiHKNSITYL--KMTPTLFSTLMEDVDmlaSCPDLKVIILGGESINIgnVKKLAEKCRwMKFIN 547
Cdd:PRK06155 255 ----FSASgfwpaVRR--HGATVTYLlgAMVSILLSQPARESD---RAHRVRVALGPGVPAAL--HAAFRERFG-VDLLD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 548 HYGPTESTVgCIAHSIDLDHIqnceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISG---VGLASGYVNNEELTNE 624
Cdd:PRK06155 323 GYGSTETNF-VIAVTHGSQRP------GSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 625 KFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKylsayITGD 704
Cdd:PRK06155 396 AWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSE-----LGED 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 705 IEMEGSFVQEKLA-----------QALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK06155 464 EVMAAVVLRDGTAlepvalvrhcePRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
269-748 |
1.11e-23 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 107.33 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAG------KHITYKELNEKANQVATLLMEKGAGKNSITAM---MIRPSEYSMigiLGILKTG------ 333
Cdd:TIGR02188 67 LEARPDKVAIIWEGdepgevRKITYRELHREVCRFANVLKSLGVKKGDRVAIympMIPEAAIAM---LACARIGaihsvv 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 334 -SAFLPiddESPVSRINhilkDSKADILITdlcflAD-----------KNIAAECLDITDKSIYTS---QNTSNPDVQY- 397
Cdd:TIGR02188 144 fGGFSA---EALADRIN----DAGAKLVIT-----ADeglrggkviplKAIVDEALEKCPVSVEHVlvvRRTGNPVVPWv 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 398 -----------------------DLEDEVYVIYTSGTSGKPKGVKvknKSLVNYSLWVCdqininsdsrslVTSKYSFDL 454
Cdd:TIGR02188 212 egrdvwwhdlmakasaycepepmDSEDPLFILYTSGSTGKPKGVL---HTTGGYLLYAA------------MTMKYVFDI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 455 CYTSIF------------------PVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCP 516
Cdd:TIGR02188 277 KDGDIFwctadvgwitghsyivygPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKH 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 517 DLKVI-ILG--GESIN----------IGNvkklaEKCrwmKFINHYGPTESTVGCIAH---SIDLdhiqnceiynKIG-- 578
Cdd:TIGR02188 357 DLSSLrLLGsvGEPINpeawmwyykvVGK-----ERC---PIVDTWWQTETGGIMITPlpgATPT----------KPGsa 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 579 -RPIHGINIYIVDRSDQLVP-VGAPGEICISGV--GLASGYVNNeeltNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEF 654
Cdd:TIGR02188 419 tLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGD----HERFVDTYFSPFPGYYFTGDGARRDKDGYIWI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 655 LGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV----YIEEKYLSAYITgdiEMEGSFVQEKLAQALPKY---MI-- 725
Cdd:TIGR02188 495 TGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVgipdDIKGQAIYAFVT---LKDGYEPDDELRKELRKHvrkEIgp 571
|
570 580
....*....|....*....|....*.
gi 2085927195 726 ---PSFIIQLKELPLTANGKINRKEL 748
Cdd:TIGR02188 572 iakPDKIRFVPGLPKTRSGKIMRRLL 597
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
260-760 |
1.87e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 105.98 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPI 339
Cdd:PRK06164 11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILITDLCF--------LAD---------KNIAAECLDITD-------------KSIYTSQN 389
Cdd:PRK06164 91 NTRYRSHEVAHILGRGRARWLVVWPGFkgidfaaiLAAvppdalpplRAIAVVDDAADAtpapapgarvqlfALPDPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 390 TSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQV 469
Cdd:PRK06164 171 AAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 470 HFVDKEVYLHSLSLIEYiHKnsITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKcRWMKFINHY 549
Cdd:PRK06164 251 VCEPVFDAARTARALRR-HR--VTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPALGELAALARA-RGVPLTGLY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 550 GPTESTVGCIAHSIDLDHiqnCEIYNKIGRPIHG-INIYIVD-RSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFI 627
Cdd:PRK06164 327 GSSEVQALVALQPATDPV---SVRIEGGGRPASPeARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 628 DNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEM 707
Cdd:PRK06164 404 DDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPT 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 708 EGSFVQEK-----LAQALPKYMIPSFIIQLKELPLT--ANG-KINRKELPLPDLQRLSVPR 760
Cdd:PRK06164 478 DGASPDEAglmaaCREALAGFKVPARVQVVEAFPVTesANGaKIQKHRLREMAQARLAAER 538
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
255-751 |
2.88e-23 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 105.23 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 255 YTVNKTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGS 334
Cdd:PRK13382 39 RREGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 335 AFLPIDDESPVSRINHILKDSKADILITDLCFLA--DKNIAAEClditdksiYTSQNTSNPDVQYDLEDEVYV------- 405
Cdd:PRK13382 119 DILLLNTSFAGPALAEVVTREGVDTVIYDEEFSAtvDRALADCP--------QATRIVAWTDEDHDLTVEVLIaahagqr 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 406 -----------IYTSGTSGKPKGVKVKN-------KSLVN----------------YSLWVCDQININSDSRSLVTSKYS 451
Cdd:PRK13382 191 peptgrkgrviLLTSGTTGTPKGARRSGpggigtlKAILDrtpwraeeptvivapmFHAWGFSQLVLAASLACTIVTRRR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 452 FDLCYTsifpvlsgggqvhfvdkevylhsLSLIEyihKNSITYLKMTPTLFSTLMEDVDML---ASCPDLKVIILGGESI 528
Cdd:PRK13382 271 FDPEAT-----------------------LDLID---RHRATGLAVVPVMFDRIMDLPAEVrnrYSGRSLRFAAASGSRM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 529 NIGNVKKLAEKcrwmkF----INHYGPTESTVGCIAHSIDLD-HIqnceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGE 603
Cdd:PRK13382 325 RPDVVIAFMDQ-----FgdviYNNYNATEAGMIATATPADLRaAP------DTAGRPAEGTEIRILDQDFREVPTGEVGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 604 ICISGVGLASGYVNNEeltnekfiDNPFHPGakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEG 683
Cdd:PRK13382 394 IFVRNDTQFDGYTSGS--------TKDFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPD 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 684 IKEAAVVYIE-EKY---LSAYITgdIEMEGSFVQEKLAQA----LPKYMIPSFIIQLKELPLTANGKINRKELPLP 751
Cdd:PRK13382 464 VAEAAVIGVDdEQYgqrLAAFVV--LKPGASATPETLKQHvrdnLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
269-748 |
5.70e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 104.27 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEK-GAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSR 347
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 348 INHILKDSKADILITDLCFL-----ADKNIAAECLDITDKSIYTSQNTSNP-----DVQYDLE----------------- 400
Cdd:PRK08314 100 LAHYVTDSGARVAIVGSELApkvapAVGNLRLRHVIVAQYSDYLPAEPEIAvpawlRAEPPLQalapggvvawkealaag 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 401 ----------DEVYVI-YTSGTSGKPKGV----KVKNKSLVNYSLWVcdqiNINSDSRSLvtskysfdlcytSIFPVLSG 465
Cdd:PRK08314 180 lappphtagpDDLAVLpYTSGTTGVPKGCmhthRTVMANAVGSVLWS----NSTPESVVL------------AVLPLFHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 466 GGQVHFVDKEVYLHSLSLI----------EYIHKNSITYLKMTPTLFstlmedVDMLAScPD--------LKVIILGGES 527
Cdd:PRK08314 244 TGMVHSMNAPIYAGATVVLmprwdreaaaRLIERYRVTHWTNIPTMV------VDFLAS-PGlaerdlssLRYIGGGGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 528 INIGNVKKLAEKCRwMKFINHYGPTEStvgcIA--HSIDLDHI-QNCeiynkIGRPIHGINIYIVD-RSDQLVPVGAPGE 603
Cdd:PRK08314 317 MPEAVAERLKELTG-LDYVEGYGLTET----MAqtHSNPPDRPkLQC-----LGIPTFGVDARVIDpETLEELPPGEVGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 604 ICISGVGLASGYVNNEELTNEKFIDnpfHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEG 683
Cdd:PRK08314 387 IVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPA 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2085927195 684 IKEAAVVYIEEKY----LSAYITGDIEMEGSFVQEKLA----QALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK08314 464 IQEACVIATPDPRrgetVKAVVVLRPEARGKTTEEEIIawarEHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
259-748 |
6.17e-23 |
|
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: 103.74 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 259 KTIQDLFEERAEKTPDQTA-AVYAGKH-ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAF 336
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAiADPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 LPIDDESPVSRINHILKDSKA-------DILITDLCFLADKNIAAECLDITDKSIYtSQNTSNPDVQYDLEDEVYVIYTS 409
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMtaaviavDAQVMDAIFQSGVRVLALSDLVGLGEPE-SAGPLIEDPPREPEQPAFVFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 410 GTSGKPKGVKVKNKSLVNYSLWVCDQINI--NSDSRSLVTSKYSFDLCYTSIFPV-LSGGGQVHFVDKEVYLHSLSLIEy 486
Cdd:cd05923 160 GTTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAaLALDGTYVVVEEFDPADALKLIE- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 487 ihKNSITYLKMTPTLFSTLMEDVDML-ASCPDLKVIILGGESINIGNVKKLaEKCRWMKFINHYGPTEStvgcIAHSIDL 565
Cdd:cd05923 239 --QERVTSLFATPTHLDALAAAAEFAgLKLSSLRHVTFAGATMPDAVLERV-NQHLPGEKVNIYGTTEA----MNSLYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 566 DHIQNCEiynkiGRPihGIN-----IYIVDRSDQLVPVGAPGEICISGVGLAS--GYVNNEELTNEKFIDNpfhpgakMY 638
Cdd:cd05923 312 DARTGTE-----MRP--GFFsevriVRIGGSPDEALANGEEGELIVAAAADAAftGYLNQPEATAKKLQDG-------WY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 639 KTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-EEKYLSAYITGDIEMEGSFVQEKLA 717
Cdd:cd05923 378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVaDERWGQSVTACVVPREGTLSADELD 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 2085927195 718 Q-----ALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05923 458 QfcrasELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
274-751 |
7.27e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 104.21 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 274 DQTAAVYAGKH----ITYKELNEKANQVATLLMEKGAGKNS-ITAMMIR-PSEYsmIGILGILKTGSAFLPIDD---ESP 344
Cdd:PRK04319 59 DKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDrVFIFMPRiPELY--FALLGALKNGAIVGPLFEafmEEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 345 V-SRINhilkDSKADILIT-----------DL-----CFLADKNIAAE--CLDITDKSIYTSQNTSNPDVqyDLEDEVYV 405
Cdd:PRK04319 137 VrDRLE----DSEAKVLITtpallerkpadDLpslkhVLLVGEDVEEGpgTLDFNALMEQASDEFDIEWT--DREDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 406 IYTSGTSGKPKGV-KVKNKSLVNYslwvcdqininsdsrslVTSKYSFDL-------C-----------YTSIFPVLSGG 466
Cdd:PRK04319 211 HYTSGSTGKPKGVlHVHNAMLQHY-----------------QTGKYVLDLheddvywCtadpgwvtgtsYGIFAPWLNGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 467 GQVhfVDkEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASC---PDLKVIILGGESINignvkklAEKCRW- 542
Cdd:PRK04319 274 TNV--ID-GGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKydlSSLRHILSVGEPLN-------PEVVRWg 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 543 -----MKFINHYGPTEStvGCIAhsidldhIQN---CEIY-NKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGvGLAS 613
Cdd:PRK04319 344 mkvfgLPIHDNWWMTET--GGIM-------IANypaMDIKpGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKK-GWPS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 614 ---GYVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAV- 689
Cdd:PRK04319 414 mmrGIWNNPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVi 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 690 -----VYIEekYLSAYITGDIEMEGS---------FVQEKL-AQALPKYmipsfiIQLKE-LPLTANGKINRK-----EL 748
Cdd:PRK04319 487 gkpdpVRGE--IIKAFVALRPGYEPSeelkeeirgFVKKGLgAHAAPRE------IEFKDkLPKTRSGKIMRRvlkawEL 558
|
...
gi 2085927195 749 PLP 751
Cdd:PRK04319 559 GLP 561
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
269-749 |
1.52e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 102.77 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRI 348
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 349 NHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTSQNT-SNPDVQydlEDEVYVIYTSGTSGKPKGV--KVKNKSL 425
Cdd:PRK13383 125 AAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESgGRPAVA---APGRIVLLTSGTTGKPKGVprAPQLRSA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 426 VNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQV----HFvDKEVYLHSLSLieyiHKNSItyLKMTPTL 501
Cdd:PRK13383 202 VGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVlthrHF-DAEAALAQASL----HRADA--FTAVPVV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 502 FSTLMEDVDMLAS---CPDLKVIILGGESINignvKKLAEkcRWMK-----FINHYGPTESTVGCIAHSIDLDhiqncEI 573
Cdd:PRK13383 275 LARILELPPRVRArnpLPQLRVVMSSGDRLD----PTLGQ--RFMDtygdiLYNGYGSTEVGIGALATPADLR-----DA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 574 YNKIGRPIHGINIYIVDRSDQlvPVG--APGEICISGVGLASGYVNNeelTNEKFIDNpfhpgakMYKTGDLGRWMPDGN 651
Cdd:PRK13383 344 PETVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGGELAGTRYTDG---GGKAVVDG-------MTSTGDMGYLDNAGR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 652 IEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-EEKY---LSAYITG--DIEMEGSFVQEKLAQALPKYMI 725
Cdd:PRK13383 412 LFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVpDERFghrLAAFVVLhpGSGVDAAQLRDYLKDRVSRFEQ 491
|
490 500
....*....|....*....|....
gi 2085927195 726 PSFIIQLKELPLTANGKINRKELP 749
Cdd:PRK13383 492 PRDINIVSSIPRNPTGKVLRKELP 515
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
283-715 |
3.38e-22 |
|
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: 101.28 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 283 KHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILIT 362
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 363 DlcfladkniaaeclditdksiytsqNTSNpdvqydleDEVYVIYTSGTSGKPKGVKVKNKSLVN--YSLWVCDQININS 440
Cdd:cd17640 84 E-------------------------NDSD--------DLATIIYTSGTTGNPKGVMLTHANLLHqiRSLSDIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 441 DSRSLVTSKYSFD-LCYTSIFpvlSGGGQVHFVDKEVYLHSLSLIeyihknSITYLKMTPTLFSTLMEDVD--------- 510
Cdd:cd17640 131 RFLSILPIWHSYErSAEYFIF---ACGCSQAYTSIRTLKDDLKRV------KPHYIVSVPRLWESLYSGIQkqvsksspi 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 511 --MLA----SCPDLKVIILGG-----------ESINIgnvkklaekcrwmKFINHYGPTESTVGCIAHSIDldhiqnCEI 573
Cdd:cd17640 202 kqFLFlfflSGGIFKFGISGGgalpphvdtffEAIGI-------------EVLNGYGLTETSPVVSARRLK------CNV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 574 YNKIGRPIHGINIYIVD-RSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNI 652
Cdd:cd17640 263 RGSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGEL 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085927195 653 EFLGRIDNQIKIR-GFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEMEGSFVQEK 715
Cdd:cd17640 337 VLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPNFEELEKWAKES 400
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
255-748 |
3.92e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 102.03 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 255 YTVNKTIQDL---FEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILK 331
Cdd:PRK06710 17 STISYDIQPLhkyVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 332 TGSAFLPIDDESPVSRINHILKDSKAD-ILITDLCFLADKNIA-------------AECLDITDKSIY------------ 385
Cdd:PRK06710 97 AGGIVVQTNPLYTERELEYQLHDSGAKvILCLDLVFPRVTNVQsatkiehvivtriADFLPFPKNLLYpfvqkkqsnlvv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 386 --------------TSQNTSNPDVQYDLEDEVYVI-YTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKY 450
Cdd:PRK06710 177 kvsesetihlwnsvEKEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 451 SFDLCY--TSI--FPVLSGGGQVHFVDKEVYLhslsLIEYIHKNSITYLKMTPTLF-----STLMEDVDMlascPDLKVI 521
Cdd:PRK06710 257 PFFHVYgmTAVmnLSIMQGYKMVLIPKFDMKM----VFEAIKKHKVTLFPGAPTIYiallnSPLLKEYDI----SSIRAC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 522 ILGGESINIgNVKKLAEKCRWMKFINHYGPTESTVgcIAHSidlDHIQNCEIYNKIGRPIHGINIYIVD-RSDQLVPVGA 600
Cdd:PRK06710 329 ISGSAPLPV-EVQEKFETVTGGKLVEGYGLTESSP--VTHS---NFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 601 PGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQ 680
Cdd:PRK06710 403 IGEIVVKGPQIMKGYWNKPEETAAVLQDGWLH-------TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 681 LEGIKEAAVVYIEEKY----LSAYITGDIEMEGSfvQEKLAQALPKYM----IPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK06710 476 HEKVQEVVTIGVPDPYrgetVKAFVVLKEGTECS--EEELNQFARKYLaaykVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
572-840 |
5.90e-22 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 97.51 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 572 EIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPF-HPGAKMYKTGDLGRWMPDG 650
Cdd:COG3433 15 EPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYpAQPGRQADDLRLLLRRGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 651 NIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE-----KYLSAYITGDIEMEGSFVQEKLAQALPKYMI 725
Cdd:COG3433 95 PGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGagvglLLIVGAVAALDGLAAAAALAALDKVPPDVVA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 726 PSFIIQLKELPLTANGKINRKELPLPDLQRLSVPRYEAPA---NETEEKLAEIWKEMLGHK--RISINEDFFELGGHSLT 800
Cdd:COG3433 175 ASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPAletALTEEELRADVAELLGVDpeEIDPDDNLFDLGLDSIR 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2085927195 801 AAFTISRIRKTfGTDIKVKELFEQPTIKQLSRLIQKRDKQ 840
Cdd:COG3433 255 LMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAA 293
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
269-748 |
7.73e-22 |
|
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: 101.10 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAG------KHITYKELNEKANQVATLLMEKGAGKNSITAM---MIRPSEYSM-----IG-ILGILKTG 333
Cdd:cd05966 63 LKERGDKVAIIWEGdepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIympMIPELVIAMlacarIGaVHSVVFAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 334 -SAflpiddESPVSRINhilkDSKADILITdlcflAD-----------KNIAAECLDITD--KSIYTSQNTSNP------ 393
Cdd:cd05966 143 fSA------ESLADRIN----DAQCKLVIT-----ADggyrggkviplKEIVDEALEKCPsvEKVLVVKRTGGEvpmteg 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 394 -DVQY----------------DLEDEVYVIYTSGTSGKPKGVKvknKSLVNYSLWVCdqininsdsrslVTSKYSFDLCY 456
Cdd:cd05966 208 rDLWWhdlmakqspecepewmDSEDPLFILYTSGSTGKPKGVV---HTTGGYLLYAA------------TTFKYVFDYHP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 457 TSIF------------------PVLSGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPDL 518
Cdd:cd05966 273 DDIYwctadigwitghsyivygPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 519 KVI-ILG--GESIN----------IGNvkklaEKCR-----WMkfinhygpTESTVGCIAH---SIDLdhiqnceiynKI 577
Cdd:cd05966 353 SSLrVLGsvGEPINpeawmwyyevIGK-----ERCPivdtwWQ--------TETGGIMITPlpgATPL----------KP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 578 G---RPIHGINIYIVDRSDQLVPVGAPGEICISGV--GLASGYVNNEEltneKFIDNPFHPGAKMYKTGDLGRWMPDGNI 652
Cdd:cd05966 410 GsatRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYY 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 653 EFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKylsayITGD------IEMEGSFVQEKLAQALPK---- 722
Cdd:cd05966 486 WITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHD-----IKGEaiyafvTLKDGEEPSDELRKELRKhvrk 560
|
570 580 590
....*....|....*....|....*....|
gi 2085927195 723 ----YMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05966 561 eigpIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
259-748 |
1.46e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 99.95 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 259 KTIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLM-----EKGagkNSITAMMIRPSEYSmIGILGILKTG 333
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgelqlKKG---DRVALMMPNCLQYP-IATFGVLRAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 334 SAFLPIDDESPVSRINHILKDSKADIL--ITDLCFLADKNIA------------AECLDITDKSI--------------Y 385
Cdd:PRK08751 101 LTVVNVNPLYTPRELKHQLIDSGASVLvvIDNFGTTVQQVIAdtpvkqvittglGDMLGFPKAALvnfvvkyvkklvpeY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 386 TSQNT-------------SNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLV----NYSLWVCDQININSDSRSLVTS 448
Cdd:PRK08751 181 RINGAirfrealalgrkhSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqQAHQWLAGTGKLEEGCEVVITA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 449 ---KYSFDLCYTSIFpVLSGGGQVHFVDKEVYLHSLslIEYIHKNSITYLKMTPTLFSTLM-----EDVDMlascPDLKV 520
Cdd:PRK08751 261 lplYHIFALTANGLV-FMKIGGCNHLISNPRDMPGF--VKELKKTRFTAFTGVNTLFNGLLntpgfDQIDF----SSLKM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 521 IILGGESINignvKKLAEkcRWMK-----FINHYGPTESTVGCIAHSIDLDHiqnceiYN-KIGRPIHGINIYIVDRSDQ 594
Cdd:PRK08751 334 TLGGGMAVQ----RSVAE--RWKQvtgltLVEAYGLTETSPAACINPLTLKE------YNgSIGLPIPSTDACIKDDAGT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 595 LVPVGAPGEICISGVGLASGYVNNEELTNEKF-IDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGE 673
Cdd:PRK08751 402 VLAIGEIGELCIKGPQVMKGYWKRPEETAKVMdADGWLH-------TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 674 IENQLLQLEGIKEAAVVYI-EEKYLSAY----ITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK08751 475 IEDVIAMMPGVLEVAAVGVpDEKSGEIVkvviVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
268-748 |
1.73e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 99.38 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 268 RAEKTPDQTAAVYA--GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPV 345
Cdd:PRK13391 6 HAQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 346 SRINHILKDSKADILITDlcfLADKNIAAE----CLDITDKSIYTSQNTSNPDVQYD----------LEDEVY---VIYT 408
Cdd:PRK13391 86 AEAAYIVDDSGARALITS---AAKLDVARAllkqCPGVRHRLVLDGDGELEGFVGYAeavaglpatpIADESLgtdMLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 409 SGTSGKPKGVK--------VKNKSLVNY--SLWvcdqiNINSDSRSLVTSK--YSFDLCYTSIfpVLSGGGQV----HFv 472
Cdd:PRK13391 163 SGTTGRPKGIKrplpeqppDTPLPLTAFlqRLW-----GFRSDMVYLSPAPlyHSAPQRAVML--VIRLGGTVivmeHF- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 473 DKEvylHSLSLIEyihKNSITYLKMTPTLFS---TLMEDVDMLASCPDLKVIILGGESINIgNVKKlaEKCRWMKFINH- 548
Cdd:PRK13391 235 DAE---QYLALIE---EYGVTHTQLVPTMFSrmlKLPEEVRDKYDLSSLEVAIHAAAPCPP-QVKE--QMIDWWGPIIHe 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 549 -YGPTESTVGCIAHSID-LDHiqnceiYNKIGRPIHGInIYIVDRSDQLVPVGAPGEICISGvGLASGYVNNEELTNEKf 626
Cdd:PRK13391 306 yYAATEGLGFTACDSEEwLAH------PGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEA- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 627 idnpFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIE 706
Cdd:PRK13391 377 ----RHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQ 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 707 -MEGS-----FVQEKLA---QALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK13391 453 pVDGVdpgpaLAAELIAfcrQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
250-707 |
1.97e-21 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 99.79 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 250 KQSSNYTVNKTIQDLFEERAEKTPDQTAAVY----AGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIG 325
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 326 ILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDLCFLADK--NIAAECLDIT------------DKSIYT----- 386
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKllEVRDELPSLRhivvldprglrdDPRLLSldell 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 387 --SQNTSNPD------VQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLvtskysfdlcytS 458
Cdd:COG1022 162 alGREVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL------------S 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 459 IFP------------VLSGGGQVHFVdkevylhslSLIEYIHKNsityLKMT-PTLFST---LMEDV-----DMLASCPD 517
Cdd:COG1022 230 FLPlahvfertvsyyALAAGATVAFA---------ESPDTLAED----LREVkPTFMLAvprVWEKVyagiqAKAEEAGG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 518 LKVII---------------LGGESINIG-NVK-KLAEK-------------CRWM--------KFINH----------- 548
Cdd:COG1022 297 LKRKLfrwalavgrryararLAGKSPSLLlRLKhALADKlvfsklrealggrLRFAvsggaalgPELARffralgipvle 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 549 -YGPTESTVGCIAHSIDldhiqnceiYNKI---GRPIHGINIYIvdrsdqlvpvGAPGEICISGVGLASGYVNNEELTNE 624
Cdd:COG1022 377 gYGLTETSPVITVNRPG---------DNRIgtvGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 625 KFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIKIRGfrveiGE------IENQLLQLEGIKEAAVVYIEEKYLS 698
Cdd:COG1022 438 AFDADGW------LHTGDIGELDEDGFLRITGRKKDLIVTSG-----GKnvapqpIENALKASPLIEQAVVVGDGRPFLA 506
|
....*....
gi 2085927195 699 AYITGDIEM 707
Cdd:COG1022 507 ALIVPDFEA 515
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
269-748 |
1.41e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 96.77 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAG-KNSITAMMIRPSEYsMIGILGILKTGSAFLPIDDESPVSR 347
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGfGDRVLILMLNRTEF-VESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 348 INHILKDSKADILITDlCFLADKNIAAECLDITDKSIYTSQNTSNPDVqYDLEDEV------------------YVIYTS 409
Cdd:PRK07786 106 IAFLVSDCGAHVVVTE-AALAPVATAVRDIVPLLSTVVVAGGSSDDSV-LGYEDLLaeagpahapvdipndspaLIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 410 GTSGKPKGVKVKNKSLVNYSLWV--CDQININSDSrSLVTSKYSFDLCYTSIFPVLSGGGQVhfvdkevYLHSL------ 481
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTGQAMTClrTNGADINSDV-GFVGVPLFHIAGIGSMLPGLLLGAPT-------VIYPLgafdpg 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 482 SLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTE-STVGCIa 560
Cdd:PRK07786 256 QLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEmSPVTCM- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 561 hsidLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykT 640
Cdd:PRK07786 335 ----LLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------S 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 641 GDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV-YIEEKY------LSAYITGDIEME----G 709
Cdd:PRK07786 404 GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIgRADEKWgevpvaVAAVRNDDAALTledlA 483
|
490 500 510
....*....|....*....|....*....|....*....
gi 2085927195 710 SFVQEKLAqalpKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK07786 484 EFLTDRLA----RYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
857-1016 |
1.87e-20 |
|
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: 95.17 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 857 SSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHD-TWELEFDYQKL 935
Cdd:cd19066 5 SPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDkTVRFRIEIIDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 936 -----PSDGIRPYVKQ-FIRPFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQ---- 1004
Cdd:cd19066 85 rnladPEARLLELIDQiQQTIYDLERGPLVRVALFrLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKptlp 164
|
170
....*....|...
gi 2085927195 1005 -PPLQSKDYSEWQ 1016
Cdd:cd19066 165 pPVGSYADYAAWL 177
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
857-1016 |
2.01e-20 |
|
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: 95.22 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 857 SSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSF--DVVSDDVVQIIHDTWELEFDYQK 934
Cdd:cd19532 5 SFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEHVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 935 LPSDGIrpyVKQFI-----RPFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQPPLQ 1008
Cdd:cd19532 85 ISDEAE---VEEEFerlknHVYDLESGETMRIVLLSLsPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQ 161
|
....*...
gi 2085927195 1009 SKDYSEWQ 1016
Cdd:cd19532 162 YLDFAARQ 169
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
267-748 |
2.20e-20 |
|
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: 96.06 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 267 ERAEKTPDQTAAVYA--GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESP 344
Cdd:cd17642 25 KRYASVPGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 345 VSRINHILKDSKADIL------ITDLCFLADKNIAAECLDITD--------KSIYT--SQNTSNPDVQYDL--------E 400
Cdd:cd17642 105 ERELDHSLNISKPTIVfcskkgLQKVLNVQKKLKIIKTIIILDskedykgyQCLYTfiTQNLPPGFNEYDFkppsfdrdE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 401 DEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSR-----SLVTSKYSFDlCYTSIFPVLSGGGQV--HFVD 473
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPdtailTVIPFHHGFG-MFTTLGYLICGFRVVlmYKFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 474 KEVYLHSLslieyiHKNSITYLKMTPTLF-----STLMEDVDMlascPDLKVIILGGESINIGNVKKLAEKCRwMKFINH 548
Cdd:cd17642 264 EELFLRSL------QDYKVQSALLVPTLFaffakSTLVDKYDL----SNLHEIASGGAPLSKEVGEAVAKRFK-LPGIRQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 549 -YGPTESTVGCIahsidldhIQNcEIYNK---IGRPIHGINIYIVD-RSDQLVPVGAPGEICISGVGLASGYVNNEELTN 623
Cdd:cd17642 333 gYGLTETTSAIL--------ITP-EGDDKpgaVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 624 EKFI-DNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI---EEKYLSA 699
Cdd:cd17642 404 ALIDkDGWLH-------SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdeDAGELPA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2085927195 700 YI----TGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd17642 477 AVvvleAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
264-748 |
2.93e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 95.06 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 264 LFEERAEKTPDQTAAV-YAGKHITYKELNEKANQVATLLmeKGAGKNSITAmmiRPSEYSMIGILGILKTGSAFLPIDDE 342
Cdd:PRK07787 4 LNPAAVAAAADIADAVrIGGRVLSRSDLAGAATAVAERV--AGARRVAVLA---TPTLATVLAVVGALIAGVPVVPVPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 343 SPVSRINHILKDSKADILitdlcfLADKNIAAECLDITDKSIYTSQNTSNPDVqyDLEDEVYVIYTSGTSGKPKGVKVKN 422
Cdd:PRK07787 79 SGVAERRHILADSGAQAW------LGPAPDDPAGLPHVPVRLHARSWHRYPEP--DPDAPALIVYTSGTTGPPKGVVLSR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 423 KS-------LVNYSLWVCDQIninsdsrsLVTSKYSFD---LCYTSIFPVLSGGGQVHFV--DKEVYLHSLSLieyihkn 490
Cdd:PRK07787 151 RAiaadldaLAEAWQWTADDV--------LVHGLPLFHvhgLVLGVLGPLRIGNRFVHTGrpTPEAYAQALSE------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 491 SITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRwMKFINHYGPTESTVGCIAHsIDLDHIQN 570
Cdd:PRK07787 216 GGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTG-HRPVERYGMTETLITLSTR-ADGERRPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 571 CeiynkIGRPIHGINIYIVDRSDQLVPVGAP--GEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMP 648
Cdd:PRK07787 294 W-----VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 649 DGNIEFLGR--IDnQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYITGDIEMEGSFVQEKLAQALPK 722
Cdd:PRK07787 363 DGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGqrivAYVVGADDVAADELIDFVAQQLSV 441
|
490 500
....*....|....*....|....*.
gi 2085927195 723 YMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK07787 442 HKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
258-743 |
3.26e-20 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 95.89 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 258 NKTIQDLFEERAEKTPDQTAAV------YAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIrPSEYSMIGI-LGIL 330
Cdd:PRK13295 23 DRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQL-PNWWEFTVLyLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 331 KTGSAFLPIddeSPVSR---INHILKDSKADILITDLCF---------------LADKN----IAAECLDITDKSIYTSQ 388
Cdd:PRK13295 102 RIGAVLNPL---MPIFRereLSFMLKHAESKVLVVPKTFrgfdhaamarrlrpeLPALRhvvvVGGDGADSFEALLITPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 389 NTSNPDVQYDLE------DEV-YVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFD--LCYTSI 459
Cdd:PRK13295 179 WEQEPDAPAILArlrpgpDDVtQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQtgFMYGLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 460 FPVLSGGgqvHFVDKEVYlHSLSLIEYIHKNSITYlKMTPTLFST-LMEDVDMLA-SCPDLKVIILGGESINIGNVKKlA 537
Cdd:PRK13295 259 MPVMLGA---TAVLQDIW-DPARAAELIRTEGVTF-TMASTPFLTdLTRAVKESGrPVSSLRTFLCAGAPIPGALVER-A 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 538 EKCRWMKFINHYGPTES---TVGCIAHSIDLdhiqnceIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASG 614
Cdd:PRK13295 333 RAALGAKIVSAWGMTENgavTLTKLDDPDER-------ASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 615 YVNNEELTNEKFiDNPFhpgakmyKTGDLGRWMPDGNIEFLGRIDNQIkIRGFR-VEIGEIENQLLQLEGIKEAAVVYIE 693
Cdd:PRK13295 406 YLKRPQLNGTDA-DGWF-------DTGDLARIDADGYIRISGRSKDVI-IRGGEnIPVVEIEALLYRHPAIAQVAIVAYP 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2085927195 694 EKYLS----AYIT----GDIEMEGsfVQEKL-AQALPKYMIPSFIIQLKELPLTANGKI 743
Cdd:PRK13295 477 DERLGeracAFVVprpgQSLDFEE--MVEFLkAQKVAKQYIPERLVVRDALPRTPSGKI 533
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
286-748 |
6.21e-20 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 94.84 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVATLL-----MEKGagkNSITAMMIRPSEYSMIgILGILKTGSAFLPIDDESPVSRINHILKDSKADIL 360
Cdd:cd05928 43 SFRELGSLSRKAANVLsgacgLQRG---DRVAVILPRVPEWWLV-NVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 361 ITD--LCFLADkNIAAECLDITDK---------------SIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNK 423
Cdd:cd05928 119 VTSdeLAPEVD-SVASECPSLKTKllvseksrdgwlnfkELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 424 SL-----VNYSLWV----CDQININSDS---RSLVTSKYSFDLCYTSIFpvlsgggqVHF---VDKEVYLHSLSlieyih 488
Cdd:cd05928 198 SLglglkVNGRYWLdltaSDIMWNTSDTgwiKSAWSSLFEPWIQGACVF--------VHHlprFDPLVILKTLS------ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 489 KNSITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKCRwMKFINHYGPTESTVGCIAHsidldhi 568
Cdd:cd05928 264 SYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG-LDIYEGYGQTETGLICANF------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 569 QNCEIY-NKIGRPIHGINIYIVDRSDQLVPVGAPGEICIS-----GVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGD 642
Cdd:cd05928 336 KGMKIKpGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAATIRGD-------FYLTGD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 643 LGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVY----IEEKYLSAYI-------TGDIEMEGSF 711
Cdd:cd05928 409 RGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSspdpIRGEVVKAFVvlapqflSHDPEQLTKE 488
|
490 500 510
....*....|....*....|....*....|....*..
gi 2085927195 712 VQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05928 489 LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
857-1016 |
8.07e-20 |
|
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: 93.26 E-value: 8.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 857 SSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWE--LEFDYQK 934
Cdd:cd19540 5 SFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEarPDLTVVD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 935 LPSDGIRPYVKQFI-RPFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGIIRKEFNALY----AGHKLKQPPL- 1007
Cdd:cd19540 85 VTEDELAARLAEAArRGFDLTAELPLRARLFRLgPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRAPDWAPLp 164
|
170
....*....|
gi 2085927195 1008 -QSKDYSEWQ 1016
Cdd:cd19540 165 vQYADYALWQ 174
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
857-1016 |
8.97e-20 |
|
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: 93.21 E-value: 8.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 857 SSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVvqiiHDTWELEFDYQKLP 936
Cdd:cd19539 5 SFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGV----PRQEILPPGPAPLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 937 SDGIRPYVKQFIR------------PFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHK-- 1001
Cdd:cd19539 81 VRDLSDPDSDRERrleellreresrGFDLDEEPPIRAVLGRFdPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkg 160
|
170
....*....|....*....
gi 2085927195 1002 ----LKQPPLQSKDYSEWQ 1016
Cdd:cd19539 161 paapLPELRQQYKEYAAWQ 179
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
854-1015 |
1.87e-19 |
|
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: 92.27 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 854 YQASSAQKRMF--ALweTDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDD-VVQIIHDTWELEF 930
Cdd:cd19543 2 YPLSPMQEGMLfhSL--LDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGePLQVVLKDRKLPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 931 DYQKLPSDGIRPyVKQFI---------RPFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGH 1000
Cdd:cd19543 80 RELDLSHLSEAE-QEAELealaeedreRGFDLARAPLMRLTLIrLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAAL 158
|
170 180
....*....|....*....|
gi 2085927195 1001 KLKQPPLQS-----KDYSEW 1015
Cdd:cd19543 159 GEGQPPSLPpvrpyRDYIAW 178
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
264-748 |
3.94e-19 |
|
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: 91.98 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 264 LFEERAEKT-PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMI--RPSEYSMIgiLGILKTGSAFLPID 340
Cdd:cd12118 8 SFLERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLApnTPAMYELH--FGVPMAGAVLNALN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 341 DESPVSRINHILKDSKADILITDLCFladkniAAECLDITDKSiytsqntsNPDVQYdLEDEVYVI---YTSGTSGKPKG 417
Cdd:cd12118 86 TRLDAEEIAFILRHSEAKVLFVDREF------EYEDLLAEGDP--------DFEWIP-PADEWDPIalnYTSGTTGRPKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 418 VKVKNK-----SLVNYSLWVCDQininsDSRSLVTskysfdL--------CYT-SIFPVlsGGGQV---HFVDKEVYlhs 480
Cdd:cd12118 151 VVYHHRgaylnALANILEWEMKQ-----HPVYLWT------LpmfhcngwCFPwTVAAV--GGTNVclrKVDAKAIY--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 481 lsliEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGNVKKLAEKcrwMKF-INH-YGPTEsTVGC 558
Cdd:cd12118 215 ----DLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEE---LGFdVTHvYGLTE-TYGP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 559 I---AHSIDLDHIQNCEIYNKIGR---PIHGINIYIVDRSDQLVPVGAP----GEICISGVGLASGYVNNEELTNEKFID 628
Cdd:cd12118 287 AtvcAWKPEWDELPTEERARLKARqgvRYVGLEEVDVLDPETMKPVPRDgktiGEIVFRGNIVMKGYLKNPEATAEAFRG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 629 NPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEM- 707
Cdd:cd12118 367 GWFH-------SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELk 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2085927195 708 EGSFVQEK-----LAQALPKYMIPSfIIQLKELPLTANGKINRKEL 748
Cdd:cd12118 440 EGAKVTEEeiiafCREHLAGFMVPK-TVVFGELPKTSTGKIQKFVL 484
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
44-227 |
9.03e-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: 89.66 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 44 ITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGIEKMVGLFINAVPLRVKGDGDTVFIALAQKLNSDFIKANTs 123
Cdd:cd19545 213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIP- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 124 YGYSSLADIQAL---TKMKEKLiNHMLVYENypvddygkAVDDTTDALRITDMEVFEQTNYDF---GLVI---IPGSQIK 194
Cdd:cd19545 292 FEHTGLQNIRRLgpdARAACNF-QTLLVVQP--------ALPSSTSESLELGIEEESEDLEDFssyGLTLecqLSGSGLR 362
|
170 180 190
....*....|....*....|....*....|...
gi 2085927195 195 AEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19545 363 VRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
269-749 |
9.94e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 91.14 E-value: 9.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRI 348
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 349 NHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTSQNTSNPDVQYDLEDEV-----------------YVIYTSGT 411
Cdd:PRK07788 139 AEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLiagsstaplpkppkpggIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 412 SGKPKGV-KVKNKSLVNYSLWVcDQININSDSRSLVTSkysfdlcytsifPVLSGGGQVHFV---------------DKE 475
Cdd:PRK07788 219 TGTPKGApRPEPSPLAPLAGLL-SRVPFRAGETTLLPA------------PMFHATGWAHLTlamalgstvvlrrrfDPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 476 VYLhslsliEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPD---LKVIILGGESINIGNVKKLAEKcrwmkF----INH 548
Cdd:PRK07788 286 ATL------EDIAKHKATALVVVPVMLSRILDLGPEVLAKYDtssLKIIFVSGSALSPELATRALEA-----FgpvlYNL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 549 YGPTESTVGCIAHSIDLDHIQNCeiynkIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEeltNEKFID 628
Cdd:PRK07788 355 YGSTEVAFATIATPEDLAEAPGT-----VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR---DKQIID 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 629 NpfhpgakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEK----YLSAYI--- 701
Cdd:PRK07788 427 G-------LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEefgqRLRAFVvka 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 702 ---TGDIEMEGSFVQEKLAqalpKYMIPSFIIQLKELPLTANGKINRKELP 749
Cdd:PRK07788 500 pgaALDEDAIKDYVRDNLA----RYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
267-666 |
1.10e-18 |
|
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: 90.76 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 267 ERAEKTPDQTAAVYA------GKHITYKELNEKANQVATLLMEKGA-GKnsiTAMMIRPS--EYsMIGILGILKTGSAFL 337
Cdd:cd05931 1 RRAAARPDRPAYTFLddeggrEETLTYAELDRRARAIAARLQAVGKpGD---RVLLLAPPglDF-VAAFLGCLYAGAIAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 338 PIDDESP---VSRINHILKDSKADILITDLCFLAD--KNIAAECLDITDKSIYTSQNTSN-----PDVQYDLEDEVYVIY 407
Cdd:cd05931 77 PLPPPTPgrhAERLAAILADAGPRVVLTTAAALAAvrAFAASRPAAGTPRLLVVDLLPDTsaadwPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 408 TSGTSGKPKGVKVKNKSLV-NyslwvCDQI--NINSDSRSLVTSKYSF--D--LCYTSIFPVLSGGgQVHFVDKEVYLHS 480
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLaN-----VRQIrrAYGLDPGDVVVSWLPLyhDmgLIGGLLTPLYSGG-PSVLMSPAAFLRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 481 -LSLIEYIHKNSITY-----------LKMTPtlfSTLMEDVDmLAScpdLKVIILGGESINIGNVKKLAEK-----CRWM 543
Cdd:cd05931 231 pLRWLRLISRYRATIsaapnfaydlcVRRVR---DEDLEGLD-LSS---WRVALNGAEPVRPATLRRFAEAfapfgFRPE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 544 KFINHYGPTESTV---------GCIAHSIDLDHIQNCEIYNKI-----------GRPIHGINIYIVDR-SDQLVPVGAPG 602
Cdd:cd05931 304 AFRPSYGLAEATLfvsggppgtGPVVLRVDRDALAGRAVAVAAddpaarelvscGRPLPDQEVRIVDPeTGRELPDGEVG 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085927195 603 EICISGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRwMPDGNIEFLGRIDNQIKIRG 666
Cdd:cd05931 384 EIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRG 446
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
260-748 |
1.16e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 91.09 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMI--RPsEYSMIgILGILKTG--SA 335
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMenRP-EYLAA-WLGLAKLGavVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 336 FL-----------PIDdespVSRINHI---------LKDSKADILITDLCFLADKNIAAECLDITD-KSIYTSQNTSNPD 394
Cdd:PRK08279 116 LLntqqrgavlahSLN----LVDAKHLivgeelveaFEEARADLARPPRLWVAGGDTLDDPEGYEDlAAAAAGAPTTNPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 395 VQYD--LEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTskysfdL---------CYTSifPVL 463
Cdd:PRK08279 192 SRSGvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCC------LplyhntggtVAWS--SVL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 464 SGGGQV---------HFVDkEVYLHSLSLIEYIHknsitylkmtptlfstlmEDVDMLASCPD--------LKVIILGGE 526
Cdd:PRK08279 264 AAGATLalrrkfsasRFWD-DVRRYRATAFQYIG------------------ELCRYLLNQPPkptdrdhrLRLMIGNGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 527 SINIgnvkklaekcrWMKFINH---------YGPTESTVGCIahsidldhiqNceIYNK---IGR--PIHGINIYIVD-- 590
Cdd:PRK08279 325 RPDI-----------WDEFQQRfgiprilefYAASEGNVGFI----------N--VFNFdgtVGRvpLWLAHPYAIVKyd 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 591 -------RSDQ--LVPVGaPGEI--CISGVGLAS---GYvNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLG 656
Cdd:PRK08279 382 vdtgepvRDADgrCIKVK-PGEVglLIGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 657 RIDNQIKIRGFRVEIGEIENQLLQLEGIKEaAVVY------IEEKYLSAYIT--GDIEMEGSFVQEKLAQALPKYMIPSF 728
Cdd:PRK08279 460 RLGDTFRWKGENVATTEVENALSGFPGVEE-AVVYgvevpgTDGRAGMAAIVlaDGAEFDLAALAAHLYERLPAYAVPLF 538
|
570 580
....*....|....*....|
gi 2085927195 729 IIQLKELPLTANGKINRKEL 748
Cdd:PRK08279 539 VRLVPELETTGTFKYRKVDL 558
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
25-227 |
1.48e-18 |
|
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: 89.39 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 25 FIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKMVGLFINAVPLRVKGDGDT 104
Cdd:cd19066 225 FFLRSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP--DEAVEDTIGLFLNLLPLRIDTSPDA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 105 VFIALAQKLNSDFIKA--NTSYGYSSLADI--QALTKMKEKLINHMLVYENYPVDDyGKAVDDTTDALRITdmeVFEQTN 180
Cdd:cd19066 303 TFPELLKRTKEQSREAieHQRVPFIELVRHlgVVPEAPKHPLFEPVFTFKNNQQQL-GKTGGFIFTTPVYT---SSEGTV 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2085927195 181 YDFGLVIIPGS--QIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19066 379 FDLDLEASEDPdgDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
265-748 |
4.38e-18 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 89.31 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 265 FEERA-EKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMI--RPSEYSMIgiLGILKTGSAFLPIDD 341
Cdd:PLN03102 19 FLKRAsECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLApnTPAMYEMH--FAVPMAGAVLNPINT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 342 ESPVSRINHILKDSKADILITDLCFLAdknIAAECLDI--TDKS-----------IYTSQNTSNPDVQY----------- 397
Cdd:PLN03102 97 RLDATSIAAILRHAKPKILFVDRSFEP---LAREVLHLlsSEDSnlnlpvifiheIDFPKRPSSEELDYecliqrgeptp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 398 ----------DLEDEVYVIYTSGTSGKPKGVKVKNK--------SLVNYS-------LWVCDQININSdsrslvtskysf 452
Cdd:PLN03102 174 slvarmfriqDEHDPISLNYTSGTTADPKGVVISHRgaylstlsAIIGWEmgtcpvyLWTLPMFHCNG------------ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 453 dlcYTSIFPVLSGGGQV----HFVDKEVYlhslsliEYIHKNSITYLKMTPTLFSTLME--DVDMLASCPDLKVIIlGGE 526
Cdd:PLN03102 242 ---WTFTWGTAARGGTSvcmrHVTAPEIY-------KNIEMHNVTHMCCVPTVFNILLKgnSLDLSPRSGPVHVLT-GGS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 527 SINIGNVKKLAEkcRWMKFINHYGPTESTvGCIAHSI------DLDHIQNCEIYNKIGrpIHGINIYIVDRSDQLVPVGA 600
Cdd:PLN03102 311 PPPAALVKKVQR--LGFQVMHAYGLTEAT-GPVLFCEwqdewnRLPENQQMELKARQG--VSILGLADVDVKNKETQESV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 601 P------GEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEI 674
Cdd:PLN03102 386 PrdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLN-------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 675 ENQLLQLEGIKEAAVVYIEEKYLS----AYI------TGDIEMEGSFVQ------EKLAQALPKYMIPSFIIQLKELPLT 738
Cdd:PLN03102 459 ENVLYKYPKVLETAVVAMPHPTWGetpcAFVvlekgeTTKEDRVDKLVTrerdliEYCRENLPHFMCPRKVVFLQELPKN 538
|
570
....*....|
gi 2085927195 739 ANGKINRKEL 748
Cdd:PLN03102 539 GNGKILKPKL 548
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
390-748 |
4.75e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.09 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 390 TSNPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKysfdLCY----TSIFPVLSG 465
Cdd:PLN02860 162 TTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAP----LCHigglSSALAMLMV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 466 GGQVHFVDKevyLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDML---ASCPDLKVIILGGESIN---IGNVKKL--- 536
Cdd:PLN02860 238 GACHVLLPK---FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSmtwKVFPSVRKILNGGGSLSsrlLPDAKKLfpn 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 537 ---------AEKCRWMKFINHYGPTESTVGCIAHSIDLDHIQNCEIYNK--IGRPIHGINIYI-VDRSDQLvpvgapGEI 604
Cdd:PLN02860 315 aklfsaygmTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGvcVGKPAPHVELKIgLDESSRV------GRI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 605 CISGVGLASGY-----VNNEELTNEKFIDnpfhpgakmykTGDLGrWMPD-GNIEFLGRIDNQIKIRGFRVEIGEIENQL 678
Cdd:PLN02860 389 LTRGPHVMLGYwgqnsETASVLSNDGWLD-----------TGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 679 LQLEGIKEAAVVYIEEKYLS-----------AYITGDIEME---GSFV--QEKL-----AQALPKYMIP-SFIIQLKELP 736
Cdd:PLN02860 457 SQHPGVASVVVVGVPDSRLTemvvacvrlrdGWIWSDNEKEnakKNLTlsSETLrhhcrEKNLSRFKIPkLFVQWRKPFP 536
|
410
....*....|..
gi 2085927195 737 LTANGKINRKEL 748
Cdd:PLN02860 537 LTTTGKIRRDEV 548
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
260-748 |
5.54e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 88.53 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAG--KHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFL 337
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 338 PIDDESP---VSRINHILKDSKadILITDLCFLADKN-------IAAECLDITDKSIYTSQN--TSNPDVQYDL--EDEV 403
Cdd:PRK05857 95 MADGNLPiaaIERFCQITDPAA--ALVAPGSKMASSAvpealhsIPVIAVDIAAVTRESEHSldAASLAGNADQgsEDPL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 404 YVIYTSGTSGKPKGVKVKNKSL-----------VNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGqvhfv 472
Cdd:PRK05857 173 AMIFTSGTTGEPKAVLLANRTFfavpdilqkegLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGE----- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 473 dkevylHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLAS-CPDLKVIILGGESINIGNVKKL-AEKCRWMKFinhYG 550
Cdd:PRK05857 248 ------NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANAtVPSLRLVGYGGSRAIAADVRFIeATGVRTAQV---YG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 551 PTEStvGCIAHSIDLDHIQNCEI-YNKIGRPIHGINIYIVDR--SDQLVPVGAP----GEICISGVGLASGYVNNEELTN 623
Cdd:PRK05857 319 LSET--GCTALCLPTDDGSIVKIeAGAVGRPYPGVDVYLAATdgIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 624 EKFIDNpfhpgakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYI-- 701
Cdd:PRK05857 397 EVLIDG-------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVgl 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 702 --TGDIEMEGSFVQEKLAQALPKY-------MIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK05857 470 avVASAELDESAARALKHTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
395-748 |
1.26e-17 |
|
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: 87.16 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 395 VQYDLEDEVYVI-YTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTS--IFPVLSGGGQVHF 471
Cdd:cd05908 100 VLCELADELAFIqFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAfhLAPLIAGMNQYLM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 472 VDKEVYLHSLSLIEYIHKNSIT--------YLKMTPTLFSTLMEDVDMlascPDLKVIILGGESINIGNVKKLAEKCRWM 543
Cdd:cd05908 180 PTRLFIRRPILWLKKASEHKATivsspnfgYKYFLKTLKPEKANDWDL----SSIRMILNGAEPIDYELCHEFLDHMSKY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 544 KF-----INHYGPTESTVG-CIAH--------SIDLDHI-------------QNCEIYNKIGRPIHGINIYIVDRSDQLV 596
Cdd:cd05908 256 GLkrnaiLPVYGLAEASVGaSLPKaqspfktiTLGRRHVthgepepevdkkdSECLTFVEVGKPIDETDIRICDEDNKIL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 597 PVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGrWMPDGNIEFLGRIDNQIKIRGFRVEIGEIEN 676
Cdd:cd05908 336 PDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIER 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 677 QLLQLEGIKEAAVVYI---EEKYLSAYITGDIEMEGS---FVqeKLAQALPKYMIPSFIIQLKE------LPLTANGKIN 744
Cdd:cd05908 409 IAEELEGVELGRVVACgvnNSNTRNEEIFCFIEHRKSeddFY--PLGKKIKKHLNKRGGWQINEvlpirrIPKTTSGKVK 486
|
....
gi 2085927195 745 RKEL 748
Cdd:cd05908 487 RYEL 490
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
405-745 |
1.72e-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: 85.01 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 405 VIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLV------TSKYSFDLCytsifpVLSGGGQVHFVDKEVYL 478
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNmlplfhIAGLNLALA------TFHAGGANVVMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 479 HSLSLIEyihKNSITYLKMTPTLFSTLMEDVDmlASCPDLKV--IILGGESINigNVKKLAEKCRwMKFINHYGPTE-ST 555
Cdd:cd17637 79 EALELIE---EEKVTLMGSFPPILSNLLDAAE--KSGVDLSSlrHVLGLDAPE--TIQRFEETTG-ATFWSLYGQTEtSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 556 VGCIAHSIDLDhiqnceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFiDNPFHpga 635
Cdd:cd17637 151 LVTLSPYRERP--------GSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWH--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 636 kmyKTGDLGRWMPDGNIEFLGRIDNQ--IKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEM-EGSFV 712
Cdd:cd17637 219 ---HTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLkPGATL 295
|
330 340 350
....*....|....*....|....*....|....*...
gi 2085927195 713 QEK-----LAQALPKYMIPSFIIQLKELPLTANGKINR 745
Cdd:cd17637 296 TADeliefVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
398-747 |
2.10e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 86.98 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 398 DLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSL----WVCDQininSDSRSLVTS------KYSFDLCYTsiFPVLSGGG 467
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkaWVPGL----GDGPERVLAalpmfhAYGLTLCLT--LAVSIGGE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 468 QVHFVDKEVYLhslsLIEYIHKNSITYLKMTPTLFSTLME-----DVDmLAScpdLKVIILGGESINIGNVKKLaEKCRW 542
Cdd:PRK05605 291 LVLLPAPDIDL----ILDAMKKHPPTWLPGVPPLYEKIAEaaeerGVD-LSG---VRNAFSGAMALPVSTVELW-EKLTG 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 543 MKFINHYGPTESTVGCIAHSIDLDHIQNceiynKIGRPIHGINIYIVDRSD--QLVPVGAPGEICISGVGLASGYVNNEE 620
Cdd:PRK05605 362 GLLVEGYGLTETSPIIVGNPMSDDRRPG-----YVGVPFPDTEVRIVDPEDpdETMPDGEEGELLVRGPQVFKGYWNRPE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 621 LTnEKFidnpFHPGakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-----EEK 695
Cdd:PRK05605 437 ET-AKS----FLDG--WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLpredgSEE 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2085927195 696 YLSAYI-----TGDIEMEGSFVQEKLAqalpKYMIPSFIIQLKELPLTANGKINRKE 747
Cdd:PRK05605 510 VVAAVVlepgaALDPEGLRAYCREHLT----RYKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
398-687 |
2.84e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.41 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 398 DLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLV----TSKYSFDLCytSIFPVLSGggqVHFVD 473
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSflppFHAYGFNSC--TLFPLLSG---VPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 474 KEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASC-PDLKVIILGGESINIGNVKKLAEKCRWMKFINHYGPT 552
Cdd:PRK06334 256 AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESClPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 553 ESTVGCIAHSIDLDHIQNCeiynkIGRPIHGINIYIVDRSDQL-VPVGAPGEICISGVGLASGYVNNEEltNEKFIDnpf 631
Cdd:PRK06334 336 ECSPVITINTVNSPKHESC-----VGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE--- 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 632 HPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEA 687
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA 461
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
269-748 |
3.79e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 85.86 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRI 348
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 349 NHILKDSKADILITDLCFLAD-KNIAAECLDIT--------------DKSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSG 413
Cdd:PRK07470 97 AYLAEASGARAMICHADFPEHaAAVRAASPDLThvvaiggaragldyEALVARHLGARVANAAVDHDDPCWFFFTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 414 KPKGVKVKNKSL---VNYSLwvCDQI-NINSDSRSLVTSkysfdlcytsifPvLSGGGQVH------------------F 471
Cdd:PRK07470 177 RPKAAVLTHGQMafvITNHL--ADLMpGTTEQDASLVVA------------P-LSHGAGIHqlcqvargaatvllpserF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 472 VDKEVYlhslSLIEyihKNSITYLKMTPTLFSTLMED--VDML--AScpdLKVIILGGESINIGNvKKLAEKCRWMKFIN 547
Cdd:PRK07470 242 DPAEVW----ALVE---RHRVTNLFTVPTILKMLVEHpaVDRYdhSS---LRYVIYAGAPMYRAD-QKRALAKLGKVLVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 548 HYGPTESTvGCIA------HSID---LDHIQNCeiynkiGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNN 618
Cdd:PRK07470 311 YFGLGEVT-GNITvlppalHDAEdgpDARIGTC------GFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 619 EELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI------ 692
Cdd:PRK07470 384 PEANAKAFRDGWFR-------TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVpdpvwg 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 693 EEKYLSAYITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK07470 457 EVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
258-743 |
4.21e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.02 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 258 NKTIQDLFEERAEKTPDQTAAVYAGKHI--TYKELNEKANQVATLLMEKGAGK---------NS------------ITAM 314
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKgdrvgiwapNVpewvltqfatakIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 315 MI------RPSE--YSMIgilgilKTGSAFLPIDDE----SPVSRINHI---LKDSKADIL-------ITDLCFLADKN- 371
Cdd:PRK08315 95 LVtinpayRLSEleYALN------QSGCKALIAADGfkdsDYVAMLYELapeLATCEPGQLqsarlpeLRRVIFLGDEKh 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 372 --------IAAECLDITDKSIYTSQNTSNPDvqydleDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSR 443
Cdd:PRK08315 169 pgmlnfdeLLALGRAVDDAELAARQATLDPD------DPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 444 slvtskysfdLCytsiFPV---------------LS-GGGQVHFVDKevyLHSLSLIEYIHKNSITYLKMTPTLFSTLME 507
Cdd:PRK08315 243 ----------LC----IPVplyhcfgmvlgnlacVThGATMVYPGEG---FDPLATLAAVEEERCTALYGVPTMFIAELD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 508 DVDM----LAScpdLKVIILGGESINIGNVKKLAEKCRwMKFIN-HYGPTE-STVGCIAhSIDLDHIQNCEiynKIGRPI 581
Cdd:PRK08315 306 HPDFarfdLSS---LRTGIMAGSPCPIEVMKRVIDKMH-MSEVTiAYGMTEtSPVSTQT-RTDDPLEKRVT---TVGRAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 582 HGINIYIVD-RSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKfIDnpfhPGAKMYkTGDLGRWMPDGNIEFLGRIDN 660
Cdd:PRK08315 378 PHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-ID----ADGWMH-TGDLAVMDEEGYVNIVGRIKD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 661 QIkIRGfrveiG------EIENQLLQLEGIKEAAVVYI-EEKY---LSAYItgdIEMEGS---------FVQEKLAqalp 721
Cdd:PRK08315 452 MI-IRG-----GeniyprEIEEFLYTHPKIQDVQVVGVpDEKYgeeVCAWI---ILRPGAtlteedvrdFCRGKIA---- 518
|
570 580
....*....|....*....|..
gi 2085927195 722 KYMIPSFIIQLKELPLTANGKI 743
Cdd:PRK08315 519 HYKIPRYIRFVDEFPMTVTGKI 540
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
282-748 |
4.37e-17 |
|
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: 85.10 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 282 GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILI 361
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 362 TDLCFLadkniaaeclditdksiytsqntsnpdvqydledevyvIYTSGTSGKPKGVKVKNKSLVNYSLWVCdQININSD 441
Cdd:cd05940 81 VDAALY--------------------------------------IYTSGTTGLPKAAIISHRRAWRGGAFFA-GSGGALP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 442 SRSLvtskYSFDLCYTS------IFPVLSGGGQVHFVDK--------EVYLHSLSLIEYIHKnSITYLKMTPtlfstlme 507
Cdd:cd05940 122 SDVL----YTCLPLYHStalivgWSACLASGATLVIRKKfsasnfwdDIRKYQATIFQYIGE-LCRYLLNQP-------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 508 dvdmlaSCPD-----LKVIILGGESINIgnvkklaekcrWMKFINH---------YGPTESTVGciahSIDLDHIQNCei 573
Cdd:cd05940 189 ------PKPTerkhkVRMIFGNGLRPDI-----------WEEFKERfgvpriaefYAATEGNSG----FINFFGKPGA-- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 574 ynkIGR----PIHGINIYIVD---RSDQL----------VPVGAPGE-IC-ISGVGLASGYVNNEElTNEKFIDNPFHPG 634
Cdd:cd05940 246 ---IGRnpslLRKVAPLALVKydlESGEPirdaegrcikVPRGEPGLlISrINPLEPFDGYTDPAA-TEKKILRDVFKKG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 635 AKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEaAVVY------IEEKYLSAYITgdIEME 708
Cdd:cd05940 322 DAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEE-ANVYgvqvpgTDGRAGMAAIV--LQPN 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2085927195 709 GSFVQEKLA----QALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05940 399 EEFDLSALAahleKNLPGYARPLFLRLQPEMEITGTFKQQKVDL 442
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
280-748 |
4.78e-17 |
|
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: 85.18 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 280 YAGKHITYKELNEKANQVAT-LLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAflpiddespVSRINHILKDskaD 358
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHwLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLSG---D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 359 ILItdlcfladkniaaECLDITDKSIytsqntsnpdVQYDLEDEVYVIYTSGTSGKPKGVKVKN-KSLVNYSLWVCDQIN 437
Cdd:cd05937 69 PLI-------------HCLKLSGSRF----------VIVDPDDPAILIYTSGTTGLPKAAAISWrRTLVTSNLLSHDLNL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 438 INSDSRSLVTSKY---SFDLCYTSIfpvLSGGGQVHFVDK--------EVYLHSLSLIEYIHKnSITYLKMTPTLFSTLM 506
Cdd:cd05937 126 KNGDRTYTCMPLYhgtAAFLGACNC---LMSGGTLALSRKfsasqfwkDVRDSGATIIQYVGE-LCRYLLSTPPSPYDRD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 507 EDVDMlASCPDLKVIILGG--ESINIGNVKKL-AEKCRWMKFINHY-GPTesTVGCIAHSIDLDH--IQNCEIYNKI--- 577
Cdd:cd05937 202 HKVRV-AWGNGLRPDIWERfrERFNVPEIGEFyAATEGVFALTNHNvGDF--GAGAIGHHGLIRRwkFENQVVLVKMdpe 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 578 -GRPIHGINIYIVDRsdqlVPVGAPGEICI----SGVGLASGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNI 652
Cdd:cd05937 279 tDDPIRDPKTGFCVR----APVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRW 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 653 EFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-----EEKYLSAYITGDIE--MEGSFVQEKLAQ----ALP 721
Cdd:cd05937 355 YFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghDGRAGCAAITLEESsaVPTEFTKSLLASlarkNLP 434
|
490 500
....*....|....*....|....*..
gi 2085927195 722 KYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05937 435 SYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
260-690 |
9.24e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 84.65 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYA--GKHITYKELNEKANQVATLLMEKGAGKNSITAMMI-RPSEYSMIgILGILKTGSAF 336
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLpNVAEYGIV-ALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 LPIDDESPVSRINHILKDSKADILITD-------------LCFLADKNIAA-----ECLDITDKSIYTSQNTSNpdVQYD 398
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTNdtnygkvkglglpVIVLGEEKIEGavnwkELLEAADRAGDTSDNEEI--LQTD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 399 LedeVYVIYTSGTSGKPKGVKVKNKSLVNYslwVCDQI-NINSDSRSLVTSK--YSFDLCY--TSI-FPVLSGGGQVHFV 472
Cdd:PLN02330 186 L---CALPFSSGTTGISKGVMLTHRNLVAN---LCSSLfSVGPEMIGQVVTLglIPFFHIYgiTGIcCATLRNKGKVVVM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 473 DK---EVYLHSLSLIEyihknsITYLKMTPTLFSTLM-----EDVDMlaSCPDLKVIILGGESINIGNVKKLAEKCRWMK 544
Cdd:PLN02330 260 SRfelRTFLNALITQE------VSFAPIVPPIILNLVknpivEEFDL--SKLKLQAIMTAAAPLAPELLTAFEAKFPGVQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 545 FINHYGPTESTVGCIAHSiDLDHIQNCEIYNKIGRPIHGINIYIVD-RSDQLVPVGAPGEICISGVGLASGYVNNEELTN 623
Cdd:PLN02330 332 VQEAYGLTEHSCITLTHG-DPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETD 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085927195 624 eKFIDNP--FHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV 690
Cdd:PLN02330 411 -RTIDEDgwLH-------TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVV 471
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
272-759 |
1.30e-16 |
|
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: 84.46 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 272 TPDQTAAVYAG-----KHITYKELNEKANQVATLLMEKGAGK-NSITAMMIRPSEySMIGILGILKTGSAFLPI----DD 341
Cdd:cd05968 74 TRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKgDRVGIYLPMIPE-IVPAFLAVARIGGIVVPIfsgfGK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 342 ESPVSRinhiLKDSKADILIT-DLCFLADKNI--------AAECLDITDKSI------------------YTSQNTSNPD 394
Cdd:cd05968 153 EAAATR----LQDAEAKALITaDGFTRRGREVnlkeeadkACAQCPTVEKVVvvrhlgndftpakgrdlsYDEEKETAGD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 395 --VQYDLEDEVYVIYTSGTSGKPKG-VKVKNKSLVNYSLWVCDQININSDSRSLVTSKYSFDLCYTSIFPVLSGGGQVHF 471
Cdd:cd05968 229 gaERTESEDPLMIIYTSGTTGKPKGtVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 472 VDKEV-YLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCPDLKVI-ILG--GESINignvkklAEKCRWM---- 543
Cdd:cd05968 309 YDGAPdHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLrVLGstGEPWN-------PEPWNWLfetv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 544 -----KFINHYGPTESTvGCIAHSIDLDHIQNCEiYNKigrPIHGINIYIVDRSDQLVPvGAPGEICISG--VGLASGYV 616
Cdd:cd05968 382 gkgrnPIINYSGGTEIS-GGILGNVLIKPIKPSS-FNG---PVPGMKADVLDESGKPAR-PEVGELVLLApwPGMTRGFW 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 617 NNEEltneKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIE--- 693
Cdd:cd05968 456 RDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPhpv 531
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085927195 694 --EKYLSAYITGDIEMEGSFVQEKLAQ----ALPKYMIPSFIIQLKELPLTANGKINRKEL-------PLPDLQRLSVP 759
Cdd:cd05968 532 kgEAIVCFVVLKPGVTPTEALAEELMErvadELGKPLSPERILFVKDLPKTRNAKVMRRVIraaylgkELGDLSSLENP 610
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
854-1019 |
1.40e-16 |
|
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: 83.27 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 854 YQASSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDV-VQIIH--------- 923
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQpVQVVHrqaqvpvte 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 924 -DTWELEFDYQKLpsdgiRPYVKQ-FIRPFHLDKSPLIRAGLI--TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALY-- 997
Cdd:cd19536 82 lDLTPLEEQLDPL-----RAYKEEtKIRRFDLGRAPLVRAALVrkDERERFLLVISDHHSILDGWSLYLLVKEILAVYnq 156
|
170 180
....*....|....*....|....*
gi 2085927195 998 --AGHKLKQPPLQS-KDYSEWQVSS 1019
Cdd:cd19536 157 llEYKPLSLPPAQPyRDFVAHERAS 181
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
535-750 |
1.57e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 83.16 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 535 KLAEKCRWMkfINHYGPTEStvGCIAHSIDLdhiqncEIYNKIGRPIHGINIYIVDRSDQlvpvgaPGEICISgvglasg 614
Cdd:PRK08308 231 KLRERTTYM--MQQYGCSEA--GCVSICPDM------KSHLDLGNPLPHVSVSAGSDENA------PEEIVVK------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 615 yvnneelTNEKFIdnpfhpgakmyKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV---- 690
Cdd:PRK08308 288 -------MGDKEI-----------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkd 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 691 -YIEEKYLSAYITgDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKELPL 750
Cdd:PRK08308 350 pVAGERVKAKVIS-HEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
260-748 |
1.74e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 83.92 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNS-ITAMMIRPSEYSmIGILGILKTGSAFLP 338
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGArVAIMMPNVLQYP-VAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 339 IDDESPVSRINHILKDSKADILITDlcfladKNIAAECLDITDKS-----IYTS-------------------------- 387
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAEAIVVL------ENFATTVQQVLAKTavkhvVVASmgdllgfkghivnfvvrrvkkmvpaw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 388 -----------------QNTSNPDVQYDleDEVYVIYTSGTSGKPKGVKVKNKSLV----NYSLWVCDQININSDSRSLV 446
Cdd:PRK07059 177 slpghvrfndalaegarQTFKPVKLGPD--DVAFLQYTGGTTGVSKGATLLHRNIVanvlQMEAWLQPAFEKKPRPDQLN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 447 TS-----KYSFDLCYTSIFPVLSGGgqvhfvdkevylHSL---------SLIEYIHKNSITYLKMTPTLFSTLM--EDVD 510
Cdd:PRK07059 255 FVcalplYHIFALTVCGLLGMRTGG------------RNIlipnprdipGFIKELKKYQVHIFPAVNTLYNALLnnPDFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 511 MLaSCPDLKVIILGGESINignvKKLAEkcRWMK-----FINHYGPTESTVGCIAHSIDLDHIQNCeiynkIGRPIHGIN 585
Cdd:PRK07059 323 KL-DFSKLIVANGGGMAVQ----RPVAE--RWLEmtgcpITEGYGLSETSPVATCNPVDATEFSGT-----IGLPLPSTE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 586 IYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIKIR 665
Cdd:PRK07059 391 VSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 666 GFRVEIGEIENQLLQLEGIKEAAVVYIEEKY----LSAYIT-GDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTAN 740
Cdd:PRK07059 465 GFNVYPNEIEEVVASHPGVLEVAAVGVPDEHsgeaVKLFVVkKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNV 544
|
....*...
gi 2085927195 741 GKINRKEL 748
Cdd:PRK07059 545 GKILRREL 552
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
285-748 |
1.93e-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: 83.00 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPiddespvsrinhilkdskADILIT-- 362
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTpd 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 363 DLCFLADKNIAAECLditdksiyTSQNTSnpdvqydLEDEVYVIYTSGTSGKPKGVKVKNKSL----VNYSLWVCDQ--- 435
Cdd:cd05974 63 DLRDRVDRGGAVYAA--------VDENTH-------ADDPMLLYFTSGTTSKPKLVEHTHRSYpvghLSTMYWIGLKpgd 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 436 ININSDSRSLVTSKYSfdlcytSIFPVLSGGGQVhFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDvDMLASC 515
Cdd:cd05974 128 VHWNISSPGWAKHAWS------CFFAPWNAGATV-FLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ-DLASFD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 516 PDLKVIILGGESIN---IGNVKKLaekcrWMKFI-NHYGPTESTVgCIAHSIDldhiQNCEIyNKIGRPIHGINIYIVDr 591
Cdd:cd05974 200 VKLREVVGAGEPLNpevIEQVRRA-----WGLTIrDGYGQTETTA-LVGNSPG----QPVKA-GSMGRPLPGYRVALLD- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 592 sdqlvPVGAP---GEICIS-----GVGLASGYVNNEELTNEKFidnpfhpGAKMYKTGDLGRWMPDGNIEFLGRIDNQIK 663
Cdd:cd05974 268 -----PDGAPateGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 664 IRGFRVEIGEIENQLLQLEGIKEAAVV----YIEEKYLSAYITGDIEMEGS---------FVQEKLAqalPKYMIPSfiI 730
Cdd:cd05974 336 SSDYRISPFELESVLIEHPAVAEAAVVpspdPVRLSVPKAFIVLRAGYEPSpetaleifrFSRERLA---PYKRIRR--L 410
|
490
....*....|....*...
gi 2085927195 731 QLKELPLTANGKINRKEL 748
Cdd:cd05974 411 EFAELPKTISGKIRRVEL 428
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
280-748 |
4.36e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 82.26 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 280 YAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADI 359
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 360 LITDLCFL--ADKNIAAECLDITDKSI----------YTSQNTSNPDvqYDLEDEV---YVIYTSGTSGKPKGVK----- 419
Cdd:PRK08276 87 LIVSAALAdtAAELAAELPAGVPLLLVvagpvpgfrsYEEALAAQPD--TPIADETagaDMLYSSGTTGRPKGIKrplpg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 420 -----VKNKSLVNYSLWVCdqinINSDSRSLVTSK--YSFDLCYTSIfpVLSGGGQVHFVDKEVYLHSLSLIEyihKNSI 492
Cdd:PRK08276 165 ldpdeAPGMMLALLGFGMY----GGPDSVYLSPAPlyHTAPLRFGMS--ALALGGTVVVMEKFDAEEALALIE---RYRV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 493 TYLKMTPTLFstlmedVDMLASCPD---------LKVIILGGESINIgNVKKlaekcrwmKFINHYGP--------TEST 555
Cdd:PRK08276 236 THSQLVPTMF------VRMLKLPEEvrarydvssLRVAIHAAAPCPV-EVKR--------AMIDWWGPiiheyyasSEGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 556 VGCIAHSID-LDHiqnceiYNKIGRPIHGInIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEkfIDNPfhpg 634
Cdd:PRK08276 301 GVTVITSEDwLAH------PGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA--ARNP---- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 635 aKMYKT-GDLGRWMPDGnieFLGRIDNQIK--IRGfRVEI--GEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIE-ME 708
Cdd:PRK08276 368 -HGWVTvGDVGYLDEDG---YLYLTDRKSDmiISG-GVNIypQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQpAD 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2085927195 709 GSFVQEKLA--------QALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK08276 443 GADAGDALAaeliawlrGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
259-765 |
1.83e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 80.59 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 259 KTIQDLFEERAEKTPDQTAAVYA--GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAF 336
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 LPIDDESPVSRINHILKDSKADILITDLCF----------------------------------------------LADK 370
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICADAFktsdyhamlqellpglaegqpgalacerlpelrgvvslapapppgfLAWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 371 NIAAECLDITDKSIYTSQNTSNPDvqydleDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSLVtsKY 450
Cdd:PRK12583 178 ELQARGETVSREALAERQASLDRD------DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCV--PV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 451 SFDLCYTSIFPVL----SGGGQVHFVDkevYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDM----LAScpdLKVII 522
Cdd:PRK12583 250 PLYHCFGMVLANLgcmtVGACLVYPNE---AFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRgnfdLSS---LRTGI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 523 LGGESINIGNVKKLAEKCRWMKFINHYGPTE----STVGCIAHSIDLDhiqnceiYNKIGRPIHGINIYIVDRSDQLVPV 598
Cdd:PRK12583 324 MAGAPCPIEVMRRVMDEMHMAEVQIAYGMTEtspvSLQTTAADDLERR-------VETVGRTQPHLEVKVVDPDGATVPR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 599 GAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakMYkTGDLGRWMPDGNIEFLGRIDNQIkIRGFR-VEIGEIENQ 677
Cdd:PRK12583 397 GEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 678 LLQLEGIKEAAVVYI-EEKY---LSAYI------TGDIEMEGSFVQEKLAQalpkYMIPSFIIQLKELPLTANGKINRke 747
Cdd:PRK12583 470 LFTHPAVADVQVFGVpDEKYgeeIVAWVrlhpghAASEEELREFCKARIAH----FKVPRYFRFVDEFPMTVTGKVQK-- 543
|
570
....*....|....*...
gi 2085927195 748 lplPDLQRLSVPRYEAPA 765
Cdd:PRK12583 544 ---FRMREISIEELALPV 558
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
396-691 |
1.91e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 80.83 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 396 QYDL-----EDEVYVIYTSGTSGKPKGVKVKNKSLV-------------NYSL--------------------------- 430
Cdd:PLN02614 214 QYDLpikkkSDICTIMYTSGTTGDPKGVMISNESIVtliagvirllksaNAALtvkdvylsylplahifdrvieecfiqh 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 431 ------WVCDQININSDSRSLVTSKYS-----FDLCYTSIFPVLSGGGqvhFVDKEVYLHSLSLIEYIHKNSITYLKMTP 499
Cdd:PLN02614 294 gaaigfWRGDVKLLIEDLGELKPTIFCavprvLDRVYSGLQKKLSDGG---FLKKFVFDSAFSYKFGNMKKGQSHVEASP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 tLFSTLMEDVDMLASCPDLKvIILGGESINIGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDldhiqNCEIYNKIGR 579
Cdd:PLN02614 371 -LCDKLVFNKVKQGLGGNVR-IILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPD-----ELDMLGTVGP 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 580 PIHGINIYIVD----RSDQLVPVgAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFL 655
Cdd:PLN02614 444 PVPNVDIRLESvpemEYDALAST-PRGEICIRGKTLFSGYYKREDLTKEVLIDGWLH-------TGDVGEWQPNGSMKII 515
|
330 340 350
....*....|....*....|....*....|....*..
gi 2085927195 656 GRIDNQIKI-RGFRVEIGEIENQLLQLEGIkEAAVVY 691
Cdd:PLN02614 516 DRKKNIFKLsQGEYVAVENIENIYGEVQAV-DSVWVY 551
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
270-748 |
2.03e-15 |
|
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: 80.82 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 270 EKTPDQTAAVY------AGKHITYKELNEKANQVATLLMEKGAGKNS--ITAM-MIRPSEYSMIGILGILKTGS----AF 336
Cdd:cd05967 62 AGRGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDrvIIYMpMIPEAAIAMLACARIGAIHSvvfgGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 LPiddESPVSRINHilkdSKADILITDLCFLaDKNIAAECLDITDKSIYTSQNTSN-------PDVQYDL---------- 399
Cdd:cd05967 142 AA---KELASRIDD----AKPKLIVTASCGI-EPGKVVPYKPLLDKALELSGHKPHhvlvlnrPQVPADLtkpgrdldws 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 ----------------EDEVYVIYTSGTSGKPKGVKVKNKS---LVNYSLWVCDQININ------SDSRSLVTSKYSfdl 454
Cdd:cd05967 214 ellakaepvdcvpvaaTDPLYILYTSGTTGKPKGVVRDNGGhavALNWSMRNIYGIKPGdvwwaaSDVGWVVGHSYI--- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 455 CYTsifPVLSG-------GGQVHFVDKEVYLhslSLIEyihKNSITYLKMTPTLFSTL---------MEDVDMlaSCpdL 518
Cdd:cd05967 291 VYG---PLLHGattvlyeGKPVGTPDPGAFW---RVIE---KYQVNALFTAPTAIRAIrkedpdgkyIKKYDL--SS--L 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 519 KVIILGGESINIgNVKKLAEKCRWMKFINHYGPTES-------TVGCIAHSIDLdhiqnceiyNKIGRPIHGINIYIVDR 591
Cdd:cd05967 358 RTLFLAGERLDP-PTLEWAENTLGVPVIDHWWQTETgwpitanPVGLEPLPIKA---------GSPGKPVPGYQVQVLDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 592 SDQLVPVGAPGEICISGV---GLASGYVNNEELTNEKFIDNpfHPGakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFR 668
Cdd:cd05967 428 DGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYLSK--FPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 669 VEIGEIENQLLQLEGIKEAAVVYIEEKylsayITGDIEM-------EGSFVQEKLAQALPKYM------IPSF--IIQLK 733
Cdd:cd05967 504 LSTGEMEESVLSHPAVAECAVVGVRDE-----LKGQVPLglvvlkeGVKITAEELEKELVALVreqigpVAAFrlVIFVK 578
|
570
....*....|....*
gi 2085927195 734 ELPLTANGKINRKEL 748
Cdd:cd05967 579 RLPKTRSGKILRRTL 593
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
282-748 |
2.30e-15 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 80.16 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 282 GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPS-EYsmIGI-LGILKTGSAFLPIDDESPVSRINHILKDSKADI 359
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRlEF--VALwLGLAKIGVETALINSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 360 LITDLcfladkniaaecLDITDKSIYTSQNTSnPDVqyDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININ 439
Cdd:cd05939 79 LIFNL------------LDPLLTQSSTEPPSQ-DDV--NFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 440 SDsrslvtskysfDLCYTSIFPVLSGGGQV---------------------HFVDKEVYlHSLSLIEYIHKnSITYLKMT 498
Cdd:cd05939 144 PE-----------DVVYDCLPLYHSAGGIMgvgqallhgstvvirkkfsasNFWDDCVK-YNCTIVQYIGE-ICRYLLAQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 499 PTLFSTLMEDVDMLAScPDLKVIILGgESINIGNVKKLAEkcrwmkfinHYGPTEstvgCIAHSIDLD-HIQNCEIYNKI 577
Cdd:cd05939 211 PPSEEEQKHNVRLAVG-NGLRPQIWE-QFVRRFGIPQIGE---------FYGATE----GNSSLVNIDnHVGACGFNSRI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 578 GRPIHGINIYIVDR--------SDQLVPVGAPGEiciSGVGLAS-----------GYVNnEELTNEKFIDNPFHPGAKMY 638
Cdd:cd05939 276 LPSVYPIRLIKVDEdtgelirdSDGLCIPCQPGE---PGLLVGKiiqndplrrfdGYVN-EGATNKKIARDVFKKGDSAF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 639 KTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEaAVVY------IEEKYLSAYI---TGDIEMEg 709
Cdd:cd05939 352 LSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLED-VVVYgvevpgVEGRAGMAAIvdpERKVDLD- 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 2085927195 710 SFVQEkLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05939 430 RFSAV-LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
857-1016 |
2.60e-15 |
|
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: 79.61 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 857 SSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEFDYQKL- 935
Cdd:cd20483 5 STFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVIDLs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 936 ----PSDGIRPYVKQFIR-PFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALY---AGHK----L 1002
Cdd:cd20483 85 eaadPEAALDQLVRNLRRqELDIEEGEVIRGWLVkLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalRAGRdlatV 164
|
170
....*....|....
gi 2085927195 1003 KQPPLQSKDYSEWQ 1016
Cdd:cd20483 165 PPPPVQYIDFTLWH 178
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
260-742 |
2.73e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 79.93 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPS-EYsMIGILGILKTGSAFLP 338
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRiEY-VEAMLGAFKARAVPVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 339 I-----DDEspvsrINHILKDSKADILITDLCFlADKniAAECLDITDK-----------------------SIYTSQNT 390
Cdd:PRK07798 83 VnyryvEDE-----LRYLLDDSDAVALVYEREF-APR--VAEVLPRLPKlrtlvvvedgsgndllpgavdyeDALAAGSP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 391 SNPDVQYDlEDEVYVIYTSGTSGKPKGVkvknkslvnysLWVCDQI------NINSDSRSLVTSKYS------------- 451
Cdd:PRK07798 155 ERDFGERS-PDDLYLLYTGGTTGMPKGV-----------MWRQEDIfrvllgGRDFATGEPIEDEEElakraaagpgmrr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 452 FDLC-------YTSIFPVLSGGGQVHFVDKEVyLHSLSLIEYIHKNSITYLKMTPTLFSTLMedVDMLAS-----CPDLK 519
Cdd:PRK07798 223 FPAPplmhgagQWAAFAALFSGQTVVLLPDVR-FDADEVWRTIEREKVNVITIVGDAMARPL--LDALEArgpydLSSLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 520 VIILGGESINiGNVKklAEKCRWMK---FINHYGPTESTVGCIAHSIDLDhiqnceiyNKIGRPIHGIN--IYIVDRSDQ 594
Cdd:PRK07798 300 AIASGGALFS-PSVK--EALLELLPnvvLTDSIGSSETGFGGSGTVAKGA--------VHTGGPRFTIGprTVVLDEDGN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 595 LVPVG--APGEICISGVgLASGYVNNEELTNEKFidnPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIG 672
Cdd:PRK07798 369 PVEPGsgEIGWIARRGH-IPLGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 673 EIENQLLQLEGIKEAAVVYI-EEKY---------LSAYITGDIEMEGSFVQEKLAqalpKYMIPSFIIQLKELPLTANGK 742
Cdd:PRK07798 445 EVEEALKAHPDVADALVVGVpDERWgqevvavvqLREGARPDLAELRAHCRSSLA----GYKVPRAIWFVDEVQRSPAGK 520
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
763-837 |
3.04e-15 |
|
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: 71.42 E-value: 3.04e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2085927195 763 APANETEEKLAEIWKEMLGHK--RISINEDFF-ELGGHSLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRLIQKR 837
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
401-748 |
5.50e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 79.04 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 401 DEVYVI-YTSGTSGKPKGVKVKNKSLVNYSLWvCDQI---NINSDSRSLVTSK-----YSFDL-CytsIFPVLSGGgqvh 470
Cdd:PRK05677 207 DDVAVLqYTGGTTGVAKGAMLTHRNLVANMLQ-CRALmgsNLNEGCEILIAPLplyhiYAFTFhC---MAMMLIGN---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 471 fvdkevylHSL---------SLIEYIHKNSITYLKMTPTLFSTL-----MEDVDMLAscpdLKVIILGGESInignvkKL 536
Cdd:PRK05677 279 --------HNIlisnprdlpAMVKELGKWKFSGFVGLNTLFVALcnneaFRKLDFSA----LKLTLSGGMAL------QL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 537 AEKCRWMKFIN-----HYGPTE-STVGCIAhsiDLDHIQnceiYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVG 610
Cdd:PRK05677 341 ATAERWKEVTGcaiceGYGMTEtSPVVSVN---PSQAIQ----VGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 611 LASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV 690
Cdd:PRK05677 414 VMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAI 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085927195 691 YI-EEKylsayiTGdiEMEGSFVQEKLAQALPK-------------YMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK05677 488 GVpDEK------SG--EAIKVFVVVKPGETLTKeqvmehmranltgYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
275-748 |
7.25e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 78.59 E-value: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 275 QTAAVYAG-KHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILK 353
Cdd:PRK12406 1 MYATIISGdRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 354 DSKADILI--TDLCFLADKNIAAEC--------------LDITDKSIYTSQNT---------SNPDVQYDLEDEVYVIYT 408
Cdd:PRK12406 81 DSGARVLIahADLLHGLASALPAGVtvlsvptppeiaaaYRISPALLTPPAGAidwegwlaqQEPYDGPPVPQPQSMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 409 SGTSGKPKGVKVKN---KSLVNYSLWVCDQININSDSRSLVT------SKYSFdlcytSIFPVLSGGGQV---HFVDKEV 476
Cdd:PRK12406 161 SGTTGHPKGVRRAAptpEQAAAAEQMRALIYGLKPGIRALLTgplyhsAPNAY-----GLRAGRLGGVLVlqpRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 477 ylhsLSLIEyihKNSITYLKMTPTLFSTLME---------DVDML-------ASCPdlkviilggesiniGNVKKlAEKC 540
Cdd:PRK12406 236 ----LQLIE---RHRITHMHMVPTMFIRLLKlpeevrakyDVSSLrhvihaaAPCP--------------ADVKR-AMIE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 541 RWMKFIN-HYGPTESTVGCIAHSID-LDHIqnceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLAS-GYVN 617
Cdd:PRK12406 294 WWGPVIYeYYGSTESGAVTFATSEDaLSHP------GTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 618 NEE----LTNEKFIdnpfhpgakmyKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI- 692
Cdd:PRK12406 368 KPEkraeIDRGGFI-----------TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIp 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 693 -EE--KYLSAYITGD--IEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK12406 437 dAEfgEALMAVVEPQpgATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
573-748 |
1.44e-14 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 77.72 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 573 IYNKIGRPIHGIN-IYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGN 651
Cdd:PRK10946 351 IFTTQGRPMSPDDeVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGY 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 652 IEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYITGDIEMEGSFVQEKL-AQALPKYMIP 726
Cdd:PRK10946 425 ITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGekscAFLVVKEPLKAVQLRRFLrEQGIAEFKLP 504
|
170 180
....*....|....*....|..
gi 2085927195 727 SFIIQLKELPLTANGKINRKEL 748
Cdd:PRK10946 505 DRVECVDSLPLTAVGKVDKKQL 526
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
400-748 |
1.89e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 77.57 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 EDEVYVIYTSGTSGKPKGVKVKNKSLV-NYSLWVcdqininsdsrSLVTSKYSFDLC---YTSIFPVLSGGGQVHFVDKE 475
Cdd:PLN02574 198 DDVAAIMYSSGTTGASKGVVLTHRNLIaMVELFV-----------RFEASQYEYPGSdnvYLAALPMFHIYGLSLFVVGL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 476 VYLHSL----------SLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASCP--DLKVIILGGESINIGNVKKLAEKCRWM 543
Cdd:PLN02574 267 LSLGSTivvmrrfdasDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVlkSLKQVSCGAAPLSGKFIQDFVQTLPHV 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 544 KFINHYGPTEST-VGciAHSIDLDHIQNceiYNKIGRPIHGINIYIVD-RSDQLVPVGAPGEICISGVGLASGYVNNEEL 621
Cdd:PLN02574 347 DFIQGYGMTESTaVG--TRGFNTEKLSK---YSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKA 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 622 TNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYlsayi 701
Cdd:PLN02574 422 TQSTIDKDGW------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKE----- 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 702 TGDIEMegSFVQEKLAQALPKYMIPSF-------------IIQLKELPLTANGKINRKEL 748
Cdd:PLN02574 491 CGEIPV--AFVVRRQGSTLSQEAVINYvakqvapykkvrkVVFVQSIPKSPAGKILRREL 548
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
285-704 |
1.99e-14 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 77.26 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVAtllmekgagkNSITAMMIRPSEYSMIGI------------LGILKTGSAFLPIDDESPVSRINHIL 352
Cdd:cd05927 6 ISYKEVAERADNIG----------SALRSLGGKPAPASFVGIysinrpewiiseLACYAYSLVTVPLYDTLGPEAIEYIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILItdlcflADKNIA----AECLDITDKSIYtsqntsnPDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNY 428
Cdd:cd05927 76 NHAEISIVF------CDAGVKvyslEEFEKLGKKNKV-------PPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 429 SLWVCDQINInsdsrslvTSKYSFDLCYTSIFP------------VLSGGGQVHFVDKEVYLhslsLIEYIHKNSITYLK 496
Cdd:cd05927 143 VAGVFKILEI--------LNKINPTDVYISYLPlahifervvealFLYHGAKIGFYSGDIRL----LLDDIKALKPTVFP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 497 MTPTLFSTLMEDV--DMLASCPDLKVIILGGESINIGNVKK--------------------LAEKCRWM----------- 543
Cdd:cd05927 211 GVPRVLNRIYDKIfnKVQAKGPLKRKLFNFALNYKLAELRSgvvraspfwdklvfnkikqaLGGNVRLMltgsaplspev 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 544 -KFINH---------YGPTESTVGC-IAHSIDLDhiqnceiYNKIGRPIHGINIYIVDRS----DQLVPVGApGEICISG 608
Cdd:cd05927 291 lEFLRValgcpvlegYGQTECTAGAtLTLPGDTS-------VGHVGGPLPCAEVKLVDVPemnyDAKDPNPR-GEVCIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 609 VGLASGYVNNEELTNEKF-IDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKI-RGFRVEIGEIENqllqlegike 686
Cdd:cd05927 363 PNVFSGYYKDPEKTAEALdEDGWLH-------TGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIEN---------- 425
|
490
....*....|....*....
gi 2085927195 687 aavVYIEEKYLS-AYITGD 704
Cdd:cd05927 426 ---IYARSPFVAqIFVYGD 441
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
854-1012 |
2.81e-14 |
|
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: 76.19 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 854 YQASSAQKRMFALWETDKDSivYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDD--VVQIIHDTWELEFD 931
Cdd:cd19542 2 YPCTPMQEGMLLSQLRSPGL--YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEgtFLQVVLKSLDPPIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 932 YQKLPSDGIRPYVKQFIRPFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGhKLKQPPLQSK 1010
Cdd:cd19542 80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLeTSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-QLLPPAPPFS 158
|
..
gi 2085927195 1011 DY 1012
Cdd:cd19542 159 DY 160
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
283-663 |
3.04e-14 |
|
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: 76.48 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 283 KHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILK------TGSAFLPIDDespvsrINHILKDSK 356
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSqnipivTVYATLGEDA------LIHSLNETE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 357 ADILITDlcfladkniaaeclditdksiytsqntSNPDvqydleDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQI 436
Cdd:cd17639 78 CSAIFTD---------------------------GKPD------DLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 437 N--INSDSR--SLVTSKYSFDLCYTSIFpvLSGGGQVHfvdkevYLHSLSLIEYIHKNS---ITYLKmtPTLFS---TLM 506
Cdd:cd17639 125 PelLGPDDRylAYLPLAHIFELAAENVC--LYRGGTIG------YGSPRTLTDKSKRGCkgdLTEFK--PTLMVgvpAIW 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 507 EDV-----DMLASCPDL-KVIILGGESINIGNVKKLAEKCRW------------------------------MKFIN--- 547
Cdd:cd17639 195 DTIrkgvlAKLNPMGGLkRTLFWTAYQSKLKALKEGPGTPLLdelvfkkvraalggrlrymlsggaplsadtQEFLNivl 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 548 -----HYGPTEST-VGCIAHSIDLDhiqnceiYNKIGRPIHGINIYIVDRSDQLVPVGAP---GEICISGVGLASGYVNN 618
Cdd:cd17639 275 cpviqGYGLTETCaGGTVQDPGDLE-------TGRVGPPLPCCEIKLVDWEEGGYSTDKPpprGEILIRGPNVFKGYYKN 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2085927195 619 EELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIK 663
Cdd:cd17639 348 PEKTKEAFDGDGW------FHTGDIGEFHPDGTLKIIDRKKDLVK 386
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
860-1016 |
4.63e-14 |
|
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: 75.75 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 860 QKRMFALWETDKDSivYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIH-DTWELE-FDYQKLPS 937
Cdd:cd19534 8 QRWFFEQNLAGRHH--FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRgDVEELFrLEVVDLSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 938 DGIRPYVKQFI----RPFHLDKSPLIRAGLITYEDR-NLLLLDVHHIAADGVSVGIIRKEFNALY----AGHKLKQPPLQ 1008
Cdd:cd19534 86 LAQAAAIEALAaeaqSSLDLEEGPLLAAALFDGTDGgDRLLLVIHHLVVDGVSWRILLEDLEAAYeqalAGEPIPLPSKT 165
|
....*....
gi 2085927195 1009 S-KDYSEWQ 1016
Cdd:cd19534 166 SfQTWAELL 174
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
407-748 |
5.53e-14 |
|
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: 75.59 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 407 YTSGTSGKPKGVKVKNKS-LVNYSLWVCDQININSDSRSLVTSK--YSFDLCYTSIFPVLSGGGQVHFvDKEVYLHSLSL 483
Cdd:cd05958 104 FTSGTTGAPKATMHFHRDpLASADRYAVNVLRLREDDRFVGSPPlaFTFGLGGVLLFPFGVGASGVLL-EEATPDLLLSA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 484 IEyihKNSITYLKMTPTLFSTLMEDVDmlASCPDLKVIILggeSINIGNVKKLAEKCRW-----MKFINHYGPTESTvgC 558
Cdd:cd05958 183 IA---RYKPTVLFTAPTAYRAMLAHPD--AAGPDLSSLRK---CVSAGEALPAALHRAWkeatgIPIIDGIGSTEMF--H 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 559 IAHSIDLDHIQNceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGvglASGYVNNEELTNEKFIDNPFHpgakmy 638
Cdd:cd05958 253 IFISARPGDARP----GATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQGGWN------ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 639 KTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKY----LSAYI-----TGDIEMEG 709
Cdd:cd05958 320 ITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESrgvvVKAFVvlrpgVIPGPVLA 399
|
330 340 350
....*....|....*....|....*....|....*....
gi 2085927195 710 SFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:cd05958 400 RELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
274-745 |
8.96e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 75.56 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 274 DQTAAVYAG------KHITYKELNEKANQVATLLMEKGAGKNSITAM---MIRPSEYSM-----IG-----ILGilktgs 334
Cdd:PRK00174 82 DKVAIIWEGddpgdsRKITYRELHREVCRFANALKSLGVKKGDRVAIympMIPEAAVAMlacarIGavhsvVFG------ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 335 AFLPiddESPVSRINhilkDSKADILITdlcflAD-----------KNIAAECLDITDK--------------------- 382
Cdd:PRK00174 156 GFSA---EALADRII----DAGAKLVIT-----ADegvrggkpiplKANVDEALANCPSvekvivvrrtggdvdwvegrd 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 383 ----SIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVKvknKSLVNYSLWVcdqininsdsrsLVTSKYSFDLCYTS 458
Cdd:PRK00174 224 lwwhELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVL---HTTGGYLVYA------------AMTMKYVFDYKDGD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 459 IF------------------PVLSGGGQVHF---------------VDKevylhslslieyiHKNSITYlkmT-PTLFST 504
Cdd:PRK00174 289 VYwctadvgwvtghsyivygPLANGATTLMFegvpnypdpgrfwevIDK-------------HKVTIFY---TaPTAIRA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 505 LMEDVDMLASCPDLKVI-ILG--GESIN----------IGNvkklaEKCR-----WMkfinhygpTEsTVGC-IAH---S 562
Cdd:PRK00174 353 LMKEGDEHPKKYDLSSLrLLGsvGEPINpeawewyykvVGG-----ERCPivdtwWQ--------TE-TGGImITPlpgA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 563 IDLdhiqnceiynKIG---RPIHGINIYIVDRSDQLVPVGAPGEICI--SGVGLASGYVNNeeltNEKFIDNPFHPGAKM 637
Cdd:PRK00174 419 TPL----------KPGsatRPLPGIQPAVVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYGD----HERFVKTYFSTFKGM 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 638 YKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI------EEKYlsAYITgdiEMEGSF 711
Cdd:PRK00174 485 YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRpddikgQGIY--AFVT---LKGGEE 559
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2085927195 712 VQEKLAQALPKYM--------IPSFIIQLKELPLTANGKINR 745
Cdd:PRK00174 560 PSDELRKELRNWVrkeigpiaKPDVIQFAPGLPKTRSGKIMR 601
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
493-748 |
9.05e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.93 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 493 TYLKMTPTLFSTLMEDVDMLASCPDLKVIILGGESINIGnVKKLAEKCRwMKFINHYGPTESTVGCIahsidldhiqnce 572
Cdd:PRK07824 128 RYTSLVPMQLAKALDDPAATAALAELDAVLVGGGPAPAP-VLDAAAAAG-INVVRTYGMSETSGGCV------------- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 573 iYNkiGRPIHGINIYIVDrsdqlvpvgapGEICISGVGLASGYVNNEEltnekfiDNPF-HPGakMYKTGDLGRwMPDGN 651
Cdd:PRK07824 193 -YD--GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFaEPG--WFRTDDLGA-LDDGV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 652 IEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEMEGS------FVQEKLAQALPKYMI 725
Cdd:PRK07824 249 LTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGpaptleALRAHVARTLDRTAA 328
|
250 260
....*....|....*....|...
gi 2085927195 726 PSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK07824 329 PRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
269-748 |
1.15e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 74.66 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYA--GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVS 346
Cdd:PRK13390 7 AQIAPDRPAVIVAetGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 347 RINHILKDSKADILITDLCFlaDKNIAAECLDITDKSIYTSQNTSNPDVQYDLEDE----------VYVIYTSGTSGKPK 416
Cdd:PRK13390 87 EADYIVGDSGARVLVASAAL--DGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAgprlteqpcgAVMLYSSGTTGFPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 417 GVKvknKSLVNYSLwvcDQIN--INSDSRSLVTSKYSfDLCYTSIfPV-----LSGGGQVHFVDKEVYL----HSLSLIE 485
Cdd:PRK13390 165 GIQ---PDLPGRDV---DAPGdpIVAIARAFYDISES-DIYYSSA-PIyhaapLRWCSMVHALGGTVVLakrfDAQATLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 486 YIHKNSITYLKMTPTLFSTLME---DVDMLASCPDLKVIILGGESINIgNVKKlaEKCRWMKFI--NHYGPTEstvgciA 560
Cdd:PRK13390 237 HVERYRITVTQMVPTMFVRLLKldaDVRTRYDVSSLRAVIHAAAPCPV-DVKH--AMIDWLGPIvyEYYSSTE------A 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 561 HSID-LDHIQNCEIYNKIGRPIHGiNIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKfiDNPFHPgakMYK 639
Cdd:PRK13390 308 HGMTfIDSPDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAA--QHPAHP---FWT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 640 T-GDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEM-EGSFVQEKLA 717
Cdd:PRK13390 382 TvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLvEGIRGSDELA 461
|
490 500 510
....*....|....*....|....*....|....*....
gi 2085927195 718 QAL--------PKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK13390 462 RELidytrsriAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
578-690 |
1.59e-13 |
|
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: 73.10 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 578 GRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGR 657
Cdd:cd17636 166 GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHH-------TNDLGRREPDGSLSFVGP 238
|
90 100 110
....*....|....*....|....*....|...
gi 2085927195 658 IDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV 690
Cdd:cd17636 239 KTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
548-838 |
1.93e-13 |
|
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: 74.74 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 548 HYGPTESTVGCIAHSIDLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFI 627
Cdd:COG3319 291 AGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 628 DNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV----YIEEKYLSAYITG 703
Cdd:COG3319 371 PAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAaaaaAAAAAALAAAVVA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 704 DIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKELPLPDLQRLSVPRYEAPANETEEkLAEIWKEMLGHK 783
Cdd:COG3319 451 AAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELA-LALLLLLLLGLG 529
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 784 RISINEDFFELGGHSLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRLIQKRD 838
Cdd:COG3319 530 LVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAA 584
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
263-760 |
2.45e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 74.22 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 263 DLFEERAEKTPDQTAAVY--------AGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGS 334
Cdd:PRK07529 29 ELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 335 AFlPIDD--ESPvsRINHILKDSKADILITDLCF----LADKniAAECLD-----------------ITDKSIYTSQNTS 391
Cdd:PRK07529 109 AN-PINPllEPE--QIAELLRAAGAKVLVTLGPFpgtdIWQK--VAEVLAalpelrtvvevdlarylPGPKRLAVPLIRR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 392 NPDVQY-DLEDEV---------------------YViYTSGTSGKPKGVKVKNKSLVnYSLWVCDQININSDSRSLVTSK 449
Cdd:PRK07529 184 KAHARIlDFDAELarqpgdrlfsgrpigpddvaaYF-HTGGTTGMPKLAQHTHGNEV-ANAWLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 450 YSFDL--CYTSIFPVLSGGGQVHFV------DKEVYLHSLSLIEyihKNSITYLKMTPTLFSTLM----EDVDMlaSCpd 517
Cdd:PRK07529 262 PLFHVnaLLVTGLAPLARGAHVVLAtpqgyrGPGVIANFWKIVE---RYRINFLSGVPTVYAALLqvpvDGHDI--SS-- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 518 LKVIILGGESINIgNVKKLAEKCRWMKFINHYGPTESTvgCiAHSID-LDHIQnceiynKIGR-----PIHGINIYIVD- 590
Cdd:PRK07529 335 LRYALCGAAPLPV-EVFRRFEAATGVRIVEGYGLTEAT--C-VSSVNpPDGER------RIGSvglrlPYQRVRVVILDd 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 591 --RSDQLVPVGAPGEICISGVGLASGYVNNEelTNEK-FIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIkIR-G 666
Cdd:PRK07529 405 agRYLRDCAVDEVGVLCIAGPNVFSGYLEAA--HNKGlWLEDGW------LNTGDLGRIDADGYFWLTGRAKDLI-IRgG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 667 FRVEIGEIENQLLQLEGIKEAAVV-------------YIE--------EKYLSAYITGDIemegsfvQEKlaQALPKYMI 725
Cdd:PRK07529 476 HNIDPAAIEEALLRHPAVALAAAVgrpdahagelpvaYVQlkpgasatEAELLAFARDHI-------AER--AAVPKHVR 546
|
570 580 590
....*....|....*....|....*....|....*
gi 2085927195 726 PsfiiqLKELPLTANGKINRkelplPDLQRLSVPR 760
Cdd:PRK07529 547 I-----LDALPKTAVGKIFK-----PALRRDAIRR 571
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
393-767 |
4.44e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 73.18 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 393 PDVQYDLEDEVYVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDsrslvtskysfDLCYTS--IF---------- 460
Cdd:PRK07867 145 PFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPD-----------DVCYVSmpLFhsnavmagwa 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 461 PVLSGGGQVHFVDKevylHSLS-LIEYIHKNSITYL----KMTPTLFSTLMEDVDmlASCPdLKvIILGGESINiGNVKK 535
Cdd:PRK07867 214 VALAAGASIALRRK----FSASgFLPDVRRYGATYAnyvgKPLSYVLATPERPDD--ADNP-LR-IVYGNEGAP-GDIAR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 536 LAEK--CRwmkFINHYGPTEstvGCIAHSIDLDHIQNCeiynkIGRPIHGINIY-----------IVDRSDQLVPVGAPG 602
Cdd:PRK07867 285 FARRfgCV---VVDGFGSTE---GGVAITRTPDTPPGA-----LGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIG 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 603 EIC-ISGVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQL 681
Cdd:PRK07867 354 ELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRY 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 682 EGIKEAAVVYIEEKylsayITGDIEM-------EGSFVQEKLAQAL-------PKyMIPSFIIQLKELPLTANGKINRKE 747
Cdd:PRK07867 427 PDATEVAVYAVPDP-----VVGDQVMaalvlapGAKFDPDAFAEFLaaqpdlgPK-QWPSYVRVCAELPRTATFKVLKRQ 500
|
410 420
....*....|....*....|....*....
gi 2085927195 748 L---------PLPDLQRLSVPRYEAPANE 767
Cdd:PRK07867 501 LsaegvdcadPVWWIRRLTPSDYAALADE 529
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
258-748 |
5.03e-13 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 73.14 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 258 NKTIQDLFEERAEKT--PDQtAAVYAGKHITYKELNEKANQVATLLMEKG--AGKNSITAMMIRPSEYSMI------GIL 327
Cdd:PRK06060 3 NGNLAGLLAEQASEAgwYDR-PAFYAADVVTHGQIHDGAARLGEVLRNRGlsSGDRVLLCLPDSPDLVQLLlaclarGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 328 GILKTGSafLPIDDESPVSRinhilkDSKADILITD--LCflaDKNIAAECLDITDksIYTSQNTSNPdVQYDL---EDE 402
Cdd:PRK06060 82 AFLANPE--LHRDDHALAAR------NTEPALVVTSdaLR---DRFQPSRVAEAAE--LMSEAARVAP-GGYEPmggDAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 403 VYVIYTSGTSGKPKGVKVKNKSLVNY-SLWVCDQININSDSRSLVTSK--YSFDLCYTSIFPVLSGGGQVhFVDKEVYLH 479
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFvDAMCRKALRLTPEDTGLCSARmyFAYGLGNSVWFPLATGGSAV-INSAPVTPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 480 SLSLIEYIHKNSITYlkMTPTLFSTLMEdvdmlASCPD----LKVIILGGESINIGNVKKLAEKCRWMKFINHYGPTEST 555
Cdd:PRK06060 227 AAAILSARFGPSVLY--GVPNFFARVID-----SCSPDsfrsLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 556 VGCIAHSIDLDHIqnceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEE--LTNEKFIDnpfhp 633
Cdd:PRK06060 300 QTFVSNRVDEWRL------GTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD----- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 634 gakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEE----KYLSAYItgdIEMEG 709
Cdd:PRK06060 369 ------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVREstgaSTLQAFL---VATSG 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2085927195 710 SFVQE--------KLAQALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK06060 440 ATIDGsvmrdlhrGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
500-748 |
7.05e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 72.55 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 TLFSTLME-----DVDMLAscpdLKVIILGGESInignVKKLAEkcRWMKF-----INHYGPTE-STVGCIAHSIDLDHI 568
Cdd:PRK12492 316 TLFVALMDhpgfkDLDFSA----LKLTNSGGTAL----VKATAE--RWEQLtgctiVEGYGLTEtSPVASTNPYGELARL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 569 qnceiyNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFidnpfhPGAKMYKTGDLGRWMP 648
Cdd:PRK12492 386 ------GTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL------DAEGWFKTGDIAVIDP 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 649 DGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-EEKYLSAYITGDIEMEGSFVQEKL----AQALPKY 723
Cdd:PRK12492 454 DGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVpDERSGEAVKLFVVARDPGLSVEELkaycKENFTGY 533
|
250 260
....*....|....*....|....*
gi 2085927195 724 MIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK12492 534 KVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
250-748 |
1.28e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 71.80 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 250 KQSSNYTVNKTIqdLFEERAEKT-PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMmIRPSEYSMI-GIL 327
Cdd:PLN02479 12 KNAANYTALTPL--WFLERAAVVhPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAV-IAPNIPAMYeAHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 328 GILKTGSAFLPIDDESPVSRINHILKDSKADILITDLCFLAdknIAAECLDITDKS----------IYTSQNTSNPD-VQ 396
Cdd:PLN02479 89 GVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFT---LAEEALKILAEKkkssfkppllIVIGDPTCDPKsLQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 397 YDL-----------------------EDEVYVI---YTSGTSGKPKGVKVKNK-----SLVNYSLWvcdqiNINSDSRSL 445
Cdd:PLN02479 166 YALgkgaieyekfletgdpefawkppADEWQSIalgYTSGTTASPKGVVLHHRgaylmALSNALIW-----GMNEGAVYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 446 VTSK--YSFDLCYTSIFPVLSGGGQV--HFVDKEVYlhslsliEYIHKNSITYLKMTPTLFSTLME--DVDMLASCPDLK 519
Cdd:PLN02479 241 WTLPmfHCNGWCFTWTLAALCGTNIClrQVTAKAIY-------SAIANYGVTHFCAAPVVLNTIVNapKSETILPLPRVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 520 VIILGGESINIGNVKKLAEKCrwMKFINHYGPTE----STVGCIAHSID-LDHIQNCEIYNKIG-RPIHGINIYIVDRSD 593
Cdd:PLN02479 314 HVMTAGAAPPPSVLFAMSEKG--FRVTHTYGLSEtygpSTVCAWKPEWDsLPPEEQARLNARQGvRYIGLEGLDVVDTKT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 594 qLVPVGAPG----EICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRV 669
Cdd:PLN02479 392 -MKPVPADGktmgEIVMRGNMVMKGYLKNPKANEEAFANGWFH-------SGDLGVKHPDGYIEIKDRSKDIIISGGENI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 670 EIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYITGDIEMEGSfVQEKLAQ--------ALPKYMIPSFIIqLKELPL 737
Cdd:PLN02479 464 SSLEVENVVYTHPAVLEASVVARPDERWGespcAFVTLKPGVDKS-DEAALAEdimkfcreRLPAYWVPKSVV-FGPLPK 541
|
570
....*....|.
gi 2085927195 738 TANGKINRKEL 748
Cdd:PLN02479 542 TATGKIQKHVL 552
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
770-829 |
1.36e-12 |
|
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: 63.35 E-value: 1.36e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085927195 770 EKLAEIWKEMLG--HKRISINEDFFELGGHSLTAAFTISRIRKTFGTDIKVKELFEQPTIKQ 829
Cdd:pfam00550 1 ERLRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
269-695 |
1.43e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 71.06 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAGKHITYKELNEKANQVATLLMEKGA---------GKNSITAMMIrpseysmigILGILKTGSAFLPI 339
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVvegsgvalrGKNSPETLLA---------YLALLQCGARVLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 340 DDESPVSRINHILKDSKADILitdLCFLADKNIAaeCLDitdkSIYTSQNTSNPDVQYDLEDEVYVIYTSGTSGKPKGVk 419
Cdd:PRK09029 84 NPQLPQPLLEELLPSLTLDFA---LVLEGENTFS--ALT----SLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAA- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 420 VKNKS--LVNySLWVCDQININSDSRSLVtskySFDLcytsiFPV---------LSGGGQVHFVDKEVYLHSLSlieyih 488
Cdd:PRK09029 154 VHTAQahLAS-AEGVLSLMPFTAQDSWLL----SLPL-----FHVsgqgivwrwLYAGATLVVRDKQPLEQALA------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 489 knSITYLKMTPT-LFSTLMEDVDMLAscpdLKVIILGGESINIgnvkKLAEKCR------WMKfinhYGPTE--STVgCI 559
Cdd:PRK09029 218 --GCTHASLVPTqLWRLLDNRSEPLS----LKAVLLGGAAIPV----ELTEQAEqqgircWCG----YGLTEmaSTV-CA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 560 AHSidlDHIQNceiynkIGRPIHGINIYIVDrsdqlvpvgapGEICISGVGLASGYVNNEE---LTNEkfiDNPFHpgak 636
Cdd:PRK09029 283 KRA---DGLAG------VGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQlvpLVND---EGWFA---- 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 637 mykTGDLGRWMpDGNIEFLGRIDNQIkIRGfrveiGE------IENQLLQLEGIKEAAVVYIEEK 695
Cdd:PRK09029 336 ---TRDRGEWQ-NGELTILGRLDNLF-FSG-----GEgiqpeeIERVINQHPLVQQVFVVPVADA 390
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
35-173 |
2.99e-12 |
|
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: 69.77 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 35 LKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQGIEKMVGLFINAVPLRVKGDGDTVF-------- 106
Cdd:cd19544 227 LRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGGRSVReavrqtha 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 107 ------------IALAQK--------------LNsdfikantsYGYSSLADIQALTKMKEKlINHMLVYE--NYP----V 154
Cdd:cd19544 307 rlaellrhehasLALAQRcsgvpaptplfsalLN---------YRHSAAAAAAAALAAWEG-IELLGGEErtNYPltlsV 376
|
170 180
....*....|....*....|....*
gi 2085927195 155 DDYGKA------VDDTTDALRITDM 173
Cdd:cd19544 377 DDLGDGfsltaqVVAPIDAERVCAY 401
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
285-748 |
3.28e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 70.70 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 285 ITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSA----FLPIDDESPVSRInhilKDSKADIL 360
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSAESLAQRI----VDCKPKVV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 361 IT--------DLCFLADKNIAA------------ECLDITDKSIYTSQNT------------------SNPDVQY-DLED 401
Cdd:PLN02654 197 ITcnavkrgpKTINLKDIVDAAldesakngvsvgICLTYENQLAMKREDTkwqegrdvwwqdvvpnypTKCEVEWvDAED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 402 EVYVIYTSGTSGKPKGVKVKNKSLVNYslwvcdqininsdsrSLVTSKYSFDLCYTSIF------------------PVL 463
Cdd:PLN02654 277 PLFLLYTSGSTGKPKGVLHTTGGYMVY---------------TATTFKYAFDYKPTDVYwctadcgwitghsyvtygPML 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 464 SGGGQVHFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLA---SCPDLKVIILGGESINignvkklaeKC 540
Cdd:PLN02654 342 NGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVtrhSRKSLRVLGSVGEPIN---------PS 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 541 RWMKFINHYGPTE----------STVGCIAHSIDLDHIQnceiynKIGR---PIHGINIYIVDRSDQLVPVGAPGEICIS 607
Cdd:PLN02654 413 AWRWFFNVVGDSRcpisdtwwqtETGGFMITPLPGAWPQ------KPGSatfPFFGVQPVIVDEKGKEIEGECSGYLCVK 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 608 GVGlaSGYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEA 687
Cdd:PLN02654 487 KSW--PGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEA 564
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2085927195 688 AVVYIEEKY----LSAYITgdiEMEGSFVQEKLAQAL--------PKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PLN02654 565 AVVGIEHEVkgqgIYAFVT---LVEGVPYSEELRKSLiltvrnqiGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
349-772 |
5.35e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 69.77 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 349 NHILKDSKADIL-ITDLCFLADKNIAAECLDITDKSIYTSQNTSNPDVQY---DLEDEVYVIYTSGTSGKPKGVKVKNKS 424
Cdd:PTZ00237 199 SNVITLFRNDITsESDLKKIETIPTIPNTLSWYDEIKKIKENNQSPFYEYvpvESSHPLYILYTSGTTGNSKAVVRSNGP 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 425 -LV--NYSLWVCdqININSDSRSLVTSKYSFDLCYTSIFPVLSGG--------GQVHFVDKEVYLHSLslieyIHKNSIT 493
Cdd:PTZ00237 279 hLVglKYYWRSI--IEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGntfvmfegGIIKNKHIEDDLWNT-----IEKHKVT 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 494 YLKMTPTLFSTLME---DVDMLASCPD---LKVIILGGESI--NIGNV--KKLAEKCrwmkfINHYGPTESTvgcIAHSI 563
Cdd:PTZ00237 352 HTLTLPKTIRYLIKtdpEATIIRSKYDlsnLKEIWCGGEVIeeSIPEYieNKLKIKS-----SRGYGQTEIG---ITYLY 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 564 DLDHIQNceIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICIS---GVGLASGYVNNEELTNEKFidNPFhPGakMYKT 640
Cdd:PTZ00237 424 CYGHINI--PYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLF--SKF-PG--YYNS 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 641 GDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITG-------------DIEM 707
Cdd:PTZ00237 497 GDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGllvlkqdqsnqsiDLNK 576
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 708 EGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKELPlpdlQRLSVPRYEAPANETEEKL 772
Cdd:PTZ00237 577 LKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIIS----KFLNDSNYQLPDNVNDSEI 637
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
856-1016 |
5.56e-12 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 69.05 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 856 ASSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHD----------T 925
Cdd:cd19546 7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDadaarpelpvV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 926 WELEFDYQKLPSDGIRpyvkqfiRPFHLDKSPLIRAGLITYEDR-NLLLLDVHHIAADGVSVGIIRKEFNALY-AGHKLK 1003
Cdd:cd19546 87 PATEEELPALLADRAA-------HLFDLTRETPWRCTLFALSDTeHVLLLVVHRIAADDESLDVLVRDLAAAYgARREGR 159
|
170
....*....|....*...
gi 2085927195 1004 QP-----PLQSKDYSEWQ 1016
Cdd:cd19546 160 APeraplPLQFADYALWE 177
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
265-748 |
5.70e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.59 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 265 FEERAEKT-PDQTAAVYAGKHITYKELNEKANQVATLLMEKGAGKNSITAMMIrPSEYSMIGI-LGILKTGSAFLPIDDE 342
Cdd:PRK08162 23 FLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLL-PNIPAMVEAhFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 343 SPVSRINHILKDSKADILITDLCFLADKNIAAE--------CLDITDKSIYTSQ-----------NTSNPDVQYDL-EDE 402
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEFAEVAREALAllpgpkplVIDVDDPEYPGGRfigaldyeaflASGDPDFAWTLpADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 403 VYVI---YTSGTSGKPKGVKVKNKSlvNYslwvcdqinINSDSRSLVT-----SKYSFDL----CYTSIFP---VLSGGG 467
Cdd:PRK08162 182 WDAIalnYTSGTTGNPKGVVYHHRG--AY---------LNALSNILAWgmpkhPVYLWTLpmfhCNGWCFPwtvAARAGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 468 QV--HFVDKEvylhslSLIEYIHKNSITYLKMTPTLFSTLM-------EDVD-----MLASCPDLKVIILGGESINIGnv 533
Cdd:PRK08162 251 NVclRKVDPK------LIFDLIREHGVTHYCGAPIVLSALInapaewrAGIDhpvhaMVAGAAPPAAVIAKMEEIGFD-- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 534 kklaekcrwmkfINH-YGPTE----STVgCIAHS--IDLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAP----G 602
Cdd:PRK08162 323 ------------LTHvYGLTEtygpATV-CAWQPewDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADgetiG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 603 EICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLE 682
Cdd:PRK08162 390 EIMFRGNIVMKGYLKNPKATEEAFAGGWFH-------TGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHP 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2085927195 683 GIKEAAVV-------------YIEEKYlSAYITGDIEMEgsFVQEKLAqalpKYMIPSFIIqLKELPLTANGKINRKEL 748
Cdd:PRK08162 463 AVLVAAVVakpdpkwgevpcaFVELKD-GASATEEEIIA--HCREHLA----GFKVPKAVV-FGELPKTSTGKIQKFVL 533
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
857-1009 |
7.33e-12 |
|
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: 68.55 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 857 SSAQKRMfalWETDK---DSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEFDYQ 933
Cdd:cd19533 5 TSAQRGV---WFAEQldpEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 934 KL-----PSDGIRPYVK-QFIRPFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVSVGI----IRKEFNALYAGHKL 1002
Cdd:cd19533 82 DLsgdpdPEGAAQQWMQeDLRKPLPLDNDPLFRHALFTLgDNRHFWYQRVHHIVMDGFSFALfgqrVAEIYTALLKGRPA 161
|
....*..
gi 2085927195 1003 KQPPLQS 1009
Cdd:cd19533 162 PPAPFGS 168
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
261-746 |
7.34e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 69.15 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 261 IQDLFEERAEKTPDQTAAVYAGKHI--TYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLP 338
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 339 IDDESPVSRINHILKDSKADILITDLCFLADKNIAAECLDITDKSIYTSQNTSNPDVQYDLE-----------------D 401
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDaateptpatstpeglrpD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 402 EVYVIYTSGTSGKPKGVKvknkslvnyslWVcdQININSDSRSLVTSK--------------YSFDLCYTSIFPVLSGGG 467
Cdd:PRK05852 178 DAMIMFTGGTTGLPKMVP-----------WT--HANIASSVRAIITGYrlsprdatvavmplYHGHGLIAALLATLASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 468 QVhFVDKEVYLHSLSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLASC---PDLKVIILGGESINIGNVKKLAEKCRwMK 544
Cdd:PRK05852 245 AV-LLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGrkpAALRFIRSCSAPLTAETAQALQTEFA-AP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 545 FINHYGPTESTVGCIAHSID-LDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTN 623
Cdd:PRK05852 323 VVCAFGMTEATHQVTTTQIEgIGQTENPVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 624 EKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITG 703
Cdd:PRK05852 403 ANFTDGWLR-------TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAA 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2085927195 704 DIEMEGS----------FVQEKLAqalpKYMIPSFIIQLKELPLTANGKINRK 746
Cdd:PRK05852 476 VIVPRESapptaeelvqFCRERLA----AFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
286-748 |
9.18e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.01 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDLC 365
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 366 FL------ADKNIAAECLDI-TDKSiYTSQNT-------------SNPDVQYDLEDE---VYVIYTSGTSGKPKGVKVKN 422
Cdd:PRK06018 121 FVpilekiADKLPSVERYVVlTDAA-HMPQTTlknavayeewiaeADGDFAWKTFDEntaAGMCYTSGTTGDPKGVLYSH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 423 KSLVNYSLwvcdqININSDSRSLVTSKysfdlcytSIFPVL------------SGGGQ-VHFVDKEVYLHSLSLIEYIHK 489
Cdd:PRK06018 200 RSNVLHAL-----MANNGDALGTSAAD--------TMLPVVplfhanswgiafSAPSMgTKLVMPGAKLDGASVYELLDT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 490 NSITYLKMTPTLFSTLMEDVDML-ASCPDLKVIILGGESINIGNVKKLAEKCrwMKFINHYGPTE-STVGCIA----HSI 563
Cdd:PRK06018 267 EKVTFTAGVPTVWLMLLQYMEKEgLKLPHLKMVVCGGSAMPRSMIKAFEDMG--VEVRHAWGMTEmSPLGTLAalkpPFS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 564 DLDHIQNCEIYNKIGRPIHGINIYIVDRSDQLVPVG--APGEICISGVGLASGY--VNNEELTNEKFIDnpfhpgakmyk 639
Cdd:PRK06018 345 KLPGDARLDVLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYyrVDGEILDDDGFFD----------- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 640 TGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYI-----EEKYL-----SAYITGDIEMEG 709
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVyhpkwDERPLlivqlKPGETATREEIL 493
|
490 500 510
....*....|....*....|....*....|....*....
gi 2085927195 710 SFVQEKLAqalpKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK06018 494 KYMDGKIA----KWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
854-1016 |
9.27e-12 |
|
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: 68.50 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 854 YQASSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQIIHDTWELEF--- 930
Cdd:cd20484 2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFqee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 931 DYQKLPSDGIRPYVKQFIR-PFHLDKSPLIRAGLITY-EDRNLLLLDVHHIAADGVS-VGIIRKEFNALYAGHKLKQPPL 1007
Cdd:cd20484 82 DISSLKESEIIAYLREKAKePFVLENGPLMRVHLFSRsEQEHFVLITIHHIIFDGSSsLTLIHSLLDAYQALLQGKQPTL 161
|
170
....*....|....
gi 2085927195 1008 QS-----KDYSEWQ 1016
Cdd:cd20484 162 ASspasyYDFVAWE 175
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
500-748 |
2.74e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 67.39 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 500 TLFSTLM-----EDVDMLAscpdLKVIILGGESINignvKKLAEkcRWMK-----FINHYGPTESTVGCIAHSIDLDHiq 569
Cdd:PRK08974 308 TLFNALLnneefQELDFSS----LKLSVGGGMAVQ----QAVAE--RWVKltgqyLLEGYGLTECSPLVSVNPYDLDY-- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 570 nceiYN-KIGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMP 648
Cdd:PRK08974 376 ----YSgSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLA-------TGDIAVMDE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 649 DGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKylsayITGD------IEMEGSFVQEKLA----Q 718
Cdd:PRK08974 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSE-----VSGEavkifvVKKDPSLTEEELIthcrR 519
|
250 260 270
....*....|....*....|....*....|
gi 2085927195 719 ALPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK08974 520 HLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
24-227 |
1.05e-10 |
|
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: 65.07 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 24 TFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcRVQgIEKMVGLFINAVPLRVKGDGD 103
Cdd:cd19531 226 RFTLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRN-RAE-LEGLIGFFVNTLVLRTDLSGD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 104 TVFIA-LAQklnsdfIKANTsygyssladIQALT-------KMKEKL-----INH------MLVYENYPVDdygkavDDT 164
Cdd:cd19531 304 PTFRElLAR------VRETA---------LEAYAhqdlpfeKLVEALqperdLSRsplfqvMFVLQNAPAA------ALE 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 165 TDALRITDMEVFEQT-NYDFGLVIIPGSQ-IKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19531 363 LPGLTVEPLEVDSGTaKFDLTLSLTETDGgLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
577-748 |
1.10e-10 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 65.28 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 577 IGRPIHGINIYIVDRSD-QLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWMPDGNIEFL 655
Cdd:PRK07514 323 VGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYVHIV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 656 GRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITG------DIEMEGSFVQEKLAQALPKYMIPSFI 729
Cdd:PRK07514 397 GRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAvvvpkpGAALDEAAILAALKGRLARFKQPKRV 476
|
170
....*....|....*....
gi 2085927195 730 IQLKELPLTANGKINRKEL 748
Cdd:PRK07514 477 FFVDELPRNTMGKVQKNLL 495
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
267-748 |
1.71e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 64.62 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 267 ERAEKTPDQTAAVYA--GKHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESP 344
Cdd:PLN02246 31 ERLSEFSDRPCLIDGatGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 345 VSRINHILKDSKADILITDLCFlADK--NIAAE--------------CLDITDKSiyTSQNTSNPDVQYDLEDEVYVIYT 408
Cdd:PLN02246 111 PAEIAKQAKASGAKLIITQSCY-VDKlkGLAEDdgvtvvtiddppegCLHFSELT--QADENELPEVEISPDDVVALPYS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 409 SGTSGKPKGVKVKNKSLVNYslwVCDQI-----NINSDSRSLVtskysfdLCYTSIFPVLSgggqvhfvdkevyLHSL-- 481
Cdd:PLN02246 188 SGTTGLPKGVMLTHKGLVTS---VAQQVdgenpNLYFHSDDVI-------LCVLPMFHIYS-------------LNSVll 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 482 ------------------SLIEYIHKNSITYLKMTPTLF-----STLMEDVDmLAScpdLKVIILGGESINignvKKLAE 538
Cdd:PLN02246 245 cglrvgaailimpkfeigALLELIQRHKVTIAPFVPPIVlaiakSPVVEKYD-LSS---IRMVLSGAAPLG----KELED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 539 KCRwMKFINH-----YGPTES-----------------------TVgciahsidldhIQNCEIynKIGRPIHGINIyivd 590
Cdd:PLN02246 317 AFR-AKLPNAvlgqgYGMTEAgpvlamclafakepfpvksgscgTV-----------VRNAEL--KIVDPETGASL---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 591 rsdqlvPVGAPGEICISGVGLASGYVNNEELTnEKFIDNP--FHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKIRGFR 668
Cdd:PLN02246 379 ------PRNQPGEICIRGPQIMKGYLNDPEAT-ANTIDKDgwLH-------TGDIGYIDDDDELFIVDRLKELIKYKGFQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 669 VEIGEIENQLLQLEGIKEAAVVYIEEKYLS----AYI--TGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGK 742
Cdd:PLN02246 445 VAPAELEALLISHPSIADAAVVPMKDEVAGevpvAFVvrSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGK 524
|
....*.
gi 2085927195 743 INRKEL 748
Cdd:PLN02246 525 ILRKDL 530
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
877-1016 |
2.56e-10 |
|
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: 63.74 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 877 NLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQII------------HDTWElEFDyqklpsdgirpyv 944
Cdd:cd19537 25 NVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYssspprvqrvdtLDVWK-EIN------------- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085927195 945 kqfiRPFHLDKSPLIRAgLITyedRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQPPLQSKDYSEWQ 1016
Cdd:cd19537 91 ----RPFDLEREDPIRV-FIS---PDTLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWS 154
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
860-1013 |
3.20e-10 |
|
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: 63.47 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 860 QKRMFALweTDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSF-DVVSDDVVQIIHDTWELEFDYQKLPSD 938
Cdd:cd19545 8 QEGLMAL--TARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPISWTESTSLDE 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 939 GIRpyvKQFIRPFHLDKsPLIRAGLITYEDR-NLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQPPlQSKDYS 1013
Cdd:cd19545 86 YLE---EDRAAPMGLGG-PLVRLALVEDPDTeRYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPP-PFSRFV 156
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
884-1015 |
3.54e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 884 LNGKLDVKKAESVLQEIIGRHEALRTSFDV-VSDDVVQIIHDTWELEFDYQK---LPSDGIRPYVKQFIR---------- 949
Cdd:PRK05691 3288 INSALDPERFAQAWQAVVARHEALRASFSWnAGETMLQVIHKPGRTPIDYLDwrgLPEDGQEQRLQALHKqereagfdll 3367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085927195 950 ---PFHLDkspLIRAGlityEDRNLLLLDVHHIAADGVSVGIIRKEFNALYA----GHKLKQP-PLQSKDYSEW 1015
Cdd:PRK05691 3368 nqpPFHLR---LIRVD----EARYWFMMSNHHILIDAWCRSLLMNDFFEIYTalgeGREAQLPvPPRYRDYIGW 3434
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
599-759 |
3.93e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 63.47 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 599 GAPGEICISGVGLASGYVNNeeltnekFIDNPfhpgaKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQL 678
Cdd:PRK07445 299 NQTGNITIQAQSLALGYYPQ-------ILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 679 LQLEGIKEAAVVYIEEKY-----LSAYITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGKINRKELPLPDL 753
Cdd:PRK07445 367 LATGLVQDVCVLGLPDPHwgevvTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
....*.
gi 2085927195 754 QRLSVP 759
Cdd:PRK07445 447 QRLGLP 452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
405-760 |
5.34e-10 |
|
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: 62.50 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 405 VIYTSGTSGKPKGVKVKNKSLVnYSLWvCDQININSDSRSLVtskysfdLCYTSIFPV----------LSGGGQVHFV-- 472
Cdd:cd05944 7 YFHTGGTTGTPKLAQHTHSNEV-YNAW-MLALNSLFDPDDVL-------LCGLPLFHVngsvvtlltpLASGAHVVLAgp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 473 ----DKEVYLHSLSLIEyihKNSITYLKMTPTLFSTLMEdVDMLASCPDLKVIILGGESINIgNVKKLAEKCRWMKFINH 548
Cdd:cd05944 78 agyrNPGLFDNFWKLVE---RYRITSLSTVPTVYAALLQ-VPVNADISSLRFAMSGAAPLPV-ELRARFEDATGLPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 549 YGPTESTvgCiAHSIDLdhiQNCEIynKIGR-----PIHGINIYIVDRSDQLVPVGAP---GEICISGVGLASGYVNNEE 620
Cdd:cd05944 153 YGLTEAT--C-LVAVNP---PDGPK--RPGSvglrlPYARVRIKVLDGVGRLLRDCAPdevGEICVAGPGVFGGYLYTEG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 621 LTNEkFIDNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIkIR-GFRVEIGEIENQLLQLEGIKEAAVV--------- 690
Cdd:cd05944 225 NKNA-FVADGW------LNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVgqpdahage 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 691 ----YIEEKYLSAYITGDIEmegSFVQEKLAQ--ALPKYMIPsfiiqLKELPLTANGKINRkelplPDLQRLSVPR 760
Cdd:cd05944 297 lpvaYVQLKPGAVVEEEELL---AWARDHVPEraAVPKHIEV-----LEELPVTAVGKVFK-----PALRADAIHR 359
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
13-227 |
5.96e-10 |
|
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: 62.78 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 13 ADEGGFNNRKKTFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKMVGLFIN 92
Cdd:cd19539 214 PAGFPYPGADLRFELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRN--HPRFESTVGFFVN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 93 AVPLRVKGDGDTVFIALAQKLNSDFIKANtSYGYSSLADIQALTKMKEKLINHMLV-----YENYPvddygKAVDDTTDA 167
Cdd:cd19539 292 LLPLRVDVSDCATFRDLIARVRKALVDAQ-RHQELPFQQLVAELPVDRDAGRHPLVqivfqVTNAP-----AGELELAGG 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2085927195 168 LRITDMEVFEqTNYDFGLVIIP---GSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19539 366 LSYTEGSDIP-DGAKFDLNLTVteeGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
383-748 |
6.00e-10 |
|
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: 62.78 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 383 SIYTSQNTSNPDVQYD----------LEDEV---YVIYTSGTSGKPKGVK-------VKNKSLVNYSLwvcdQININSDS 442
Cdd:cd05929 95 GLFTGGGALDGLEDYEaaeggspetpIEDEAagwKMLYSGGTTGRPKGIKrglpggpPDNDTLMAAAL----GFGPGADS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 443 RSLVTSKYSFDLCYTSIFPVLSGGGQV----HFvDKEVYLhslSLIEyihKNSITYLKMTPTLFSTLM---------EDV 509
Cdd:cd05929 171 VYLSPAPLYHAAPFRWSMTALFMGGTLvlmeKF-DPEEFL---RLIE---RYRVTFAQFVPTMFVRLLklpeavrnaYDL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 510 DML-------ASCP-DLK--VIILGGESInignvkklaekcrwmkfINHYGPTESTVGCIAHSID-LDHiqnceiYNKIG 578
Cdd:cd05929 244 SSLkrvihaaAPCPpWVKeqWIDWGGPII-----------------WEYYGGTEGQGLTIINGEEwLTH------PGSVG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 579 RPIHGiNIYIVDRSDQLVPVGAPGEICISGvGLASGYVNNEELTNEKFIDNPFHpgakmyKTGDLGRWMPDGNIEFLGRI 658
Cdd:cd05929 301 RAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 659 DNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIE-MEGSFVQEKLA--------QALPKYMIPSFI 729
Cdd:cd05929 373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQpAPGADAGTALAeeliaflrDRLSRYKCPRSI 452
|
410
....*....|....*....
gi 2085927195 730 IQLKELPLTANGKINRKEL 748
Cdd:cd05929 453 EFVAELPRDDTGKLYRRLL 471
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
897-1000 |
6.93e-10 |
|
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: 62.45 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 897 LQEIIGRHEALRTSFdvVSDDV---VQIIHDTWELEFDYQKL-PSDGIRPYVKQFIRPFH----LDKSPLIRAgLITYED 968
Cdd:cd19544 45 LQQVIDRHDILRTAI--LWEGLsepVQVVWRQAELPVEELTLdPGDDALAQLRARFDPRRyrldLRQAPLLRA-HVAEDP 121
|
90 100 110
....*....|....*....|....*....|....*
gi 2085927195 969 RN---LLLLDVHHIAADGVSVGIIRKEFNALYAGH 1000
Cdd:cd19544 122 ANgrwLLLLLFHHLISDHTSLELLLEEIQAILAGR 156
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
400-742 |
1.27e-09 |
|
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: 61.24 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 EDEVYVIYTSGTSGKPKGVkvknkslvnysLWVCDQININS-DSRSLVTSKYSFDLCY---------TSIFPV------- 462
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGV-----------MWRQEDIFRMLmGGADFGTGEFTPSEDAhkaaaaaagTVMFPApplmhgt 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 463 --------LSGGGQVHFVDKEvyLHSLSLIEYIHKNSITYLKMTPTLFSTLMedVDMLAS-----CPDLKVIILGGESIN 529
Cdd:cd05924 72 gswtafggLLGGQTVVLPDDR--FDPEEVWRTIEKHKVTSMTIVGDAMARPL--IDALRDagpydLSSLFAISSGGALLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 530 IGNVKKLAEKCRWMKFINHYGPTESTVGCIAHSIDLDHIqnceiynkiGRPIHGIN--IYIVDRSDQLVPVG--APGEIC 605
Cdd:cd05924 148 PEVKQGLLELVPNITLVDAFGSSETGFTGSGHSAGSGPE---------TGPFTRANpdTVVLDDDGRVVPPGsgGVGWIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 606 ISGVgLASGYVNNEELTNEKF--IDnpfhpGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEG 683
Cdd:cd05924 219 RRGH-IPLGYYGDEAKTAETFpeVD-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPA 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 684 IKEAAVVYI-EEKYLS-----AYITGDIEMEGSFVQEKLAQALPKYMIPSFIIQLKELPLTANGK 742
Cdd:cd05924 293 VYDVLVVGRpDERWGQevvavVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
577-748 |
1.30e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 61.97 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 577 IGRPIHGINIYIVD--------RSDQ----LVPVGAPGEIC-ISGVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDL 643
Cdd:PRK13388 315 IGRGAPGVAIYNPEtltecavaRFDAhgalLNADEAIGELVnTAGAGFFEGYYNNPEATAERMRHG-------MYWSGDL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 644 GRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYlsayiTGDIEM------------EGSF 711
Cdd:PRK13388 388 AYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDER-----VGDQVMaalvlrdgatfdPDAF 462
|
170 180 190
....*....|....*....|....*....|....*...
gi 2085927195 712 VQEKLAQA-LPKYMIPSFIIQLKELPLTANGKINRKEL 748
Cdd:PRK13388 463 AAFLAAQPdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
405-709 |
2.95e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 60.98 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 405 VIYTSGTSGKPKGVKVKNKSLVNYSLWV---CDQINinsdsrslvtSKYSFDLCYTSIFPVlsgggqVHFVDK---EVYL 478
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQFE----------DKMTHDDVYLSFLPL------AHILDRmieEYFF 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 479 HSLSLIEYIHKN-----------SITYLKMTPTLFSTLMEDV-------------------------------------- 509
Cdd:PLN02430 289 RKGASVGYYHGDlnalrddlmelKPTLLAGVPRVFERIHEGIqkalqelnprrrlifnalykyklawmnrgyshkkaspm 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 510 -DMLASCP-------DLKVIILGGESINIgNVKKLAEKCRWMKFINHYGPTES----TVGCIAHSIDLDHIQNCEIYNKI 577
Cdd:PLN02430 369 aDFLAFRKvkaklggRLRLLISGGAPLST-EIEEFLRVTSCAFVVQGYGLTETlgptTLGFPDEMCMLGTVGAPAVYNEL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 578 GR---PIHGINiyivdrsdqlvPVGAP--GEICISGVGLASGYVNNEELTNEKFIDNPFHpgakmykTGDLGRWMPDGNI 652
Cdd:PLN02430 448 RLeevPEMGYD-----------PLGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEILPNGVL 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2085927195 653 EFLGRIDNQIKirgfrveigeienqLLQLEGIkeaAVVYIEEKYLSAYITGDIEMEG 709
Cdd:PLN02430 510 KIIDRKKNLIK--------------LSQGEYV---ALEYLENVYGQNPIVEDIWVYG 549
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
20-227 |
4.00e-09 |
|
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: 60.08 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 20 NRKKTFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVQgiEKMVGLFINAVPLRVK 99
Cdd:cd19533 216 FLRRTAELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAA--RQTPGMVANTLPLRLT 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 100 GDGDTVFIALAQKLNSDFIKA--NTSYGYSSLADIQALTKMKEKLINHMLvyeNYPVDDYGKAVDDT-----------TD 166
Cdd:cd19533 294 VDPQQTFAELVAQVSRELRSLlrHQRYRYEDLRRDLGLTGELHPLFGPTV---NYMPFDYGLDFGGVvglthnlssgpTN 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085927195 167 ALRITdmeVFEQtnydfglviIPGSQIKAEMTYNNNVYREDIINRIGVNFCHVLKQVATDP 227
Cdd:cd19533 371 DLSIF---VYDR---------DDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
673-742 |
5.17e-09 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 53.70 E-value: 5.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2085927195 673 EIENQLLQLEGIKEAAVVYIEEK----YLSAYIT---GDIEMEGSfVQEKLAQALPKYMIPSFIIQLKELPLTANGK 742
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDElkgeAPVAFVVlkpGVELLEEE-LVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
370-680 |
5.46e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 60.24 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 370 KNIAAECLDITDKSIYTSQNTSNPDVQYDleDEVYVIYTSGTSGKPKGVKVKNKSL------VNYSLWVCDQININSDSr 443
Cdd:PLN02861 192 EELGVSCFSWEEFSLMGSLDCELPPKQKT--DICTIMYTSGTTGEPKGVILTNRAIiaevlsTDHLLKVTDRVATEEDS- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 444 slvtskysfdlcYTSIFPVlsgggqVHFVDKEVYLHSLSLIEYIH--KNSITYL-----KMTPTLFSTLMEDVDMLASCP 516
Cdd:PLN02861 269 ------------YFSYLPL------AHVYDQVIETYCISKGASIGfwQGDIRYLmedvqALKPTIFCGVPRVYDRIYTGI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 517 DLKVIILGG---------ESINIGNVKK----------------------LAEKCRWM---------------------K 544
Cdd:PLN02861 331 MQKISSGGMlrkklfdfaYNYKLGNLRKglkqeeasprldrlvfdkikegLGGRVRLLlsgaaplprhveeflrvtscsV 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 545 FINHYGPTESTVGCiahsidLDHIQNC-EIYNKIGRPIHGINIYIVDRS----DQLVPVgAPGEICISGVGLASGYVNNE 619
Cdd:PLN02861 411 LSQGYGLTESCGGC------FTSIANVfSMVGTVGVPMTTIEARLESVPemgyDALSDV-PRGEICLRGNTLFSGYHKRQ 483
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085927195 620 ELTNEKFIDNPFHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKI-RGFRVEIGEIENQLLQ 680
Cdd:PLN02861 484 DLTEEVLIDGWFH-------TGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSR 538
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
854-1015 |
1.17e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.59 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 854 YQASSAQKRMF--ALWETDKDSIVYNLPIMIElngKLDVKKAESVLQEIIGRHEALRTSFDVVSD--DVVQIIHDTWEL- 928
Cdd:PRK12316 1557 YPLSPMQQGMLfhSLYEQEAGDYINQLRVDVQ---GLDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIHKQVELp 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 929 --EFDYQK---LPSDGIRPYVKQFIRPFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKL 1002
Cdd:PRK12316 1634 faELDWRGredLGQALDALAQAERQKGFDLTRAPLLRLVLVrTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPV 1713
|
170
....*....|...
gi 2085927195 1003 KQPPLQSKDYSEW 1015
Cdd:PRK12316 1714 AAPGGRYRDYIAW 1726
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
854-1015 |
2.72e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 58.25 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 854 YQASSAQKRMfaLWET--DKDSIVYNLPIMIELNGkLDVKKAESVLQEIIGRHEALRTSFdvVSDDV----VQIIHDTWE 927
Cdd:PRK12467 2647 YPLSPMQQGM--LFHTlyEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGF--LWDGEleepLQVVYKQAR 2721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 928 LEF---DYQKlpsdgiRPYVKQFI---------RPFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFN 994
Cdd:PRK12467 2722 LPFsrlDWRD------RADLEQALdalaaadrqQGFDLLSAPLLRLTLVrTGEDRHHLIYTNHHILMDGWSGSQLLGEVL 2795
|
170 180
....*....|....*....|.
gi 2085927195 995 ALYAGHKLKQPPLQSKDYSEW 1015
Cdd:PRK12467 2796 QRYFGQPPPAREGRYRDYIAW 2816
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
286-690 |
3.60e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 57.09 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILITDlc 365
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 366 FLADKNIAaeclditdksiytsqntsnpdvqydledevyVIYTSGTSGKPKGVKVKNKSLVNYSLWVCDQININSDSRSL 445
Cdd:cd05910 82 PKADEPAA-------------------------------ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 446 VT----SKYSFDLCYTSIFPVLSGGGQVHfVDKEvylhslSLIEYIHKNSITYLKMTPTLFSTLMEDVDMLA-SCPDLKV 520
Cdd:cd05910 131 ATfplfALFGPALGLTSVIPDMDPTRPAR-ADPQ------KLVGAIRQYGVSIVFGSPALLERVARYCAQHGiTLPSLRR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 521 IILGGESINIGnvkkLAEKCRWM-----KFINHYGPTESTVGCIAHSIDL---------DHIQNCeiynkIGRPIHGINI 586
Cdd:cd05910 204 VLSAGAPVPIA----LAARLRKMlsdeaEILTPYGATEALPVSSIGSRELlatttaatsGGAGTC-----VGRPIPGVRV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 587 YIVDRSDQ---------LVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFHpgAKMYKTGDLGRWMPDGNIEFLGR 657
Cdd:cd05910 275 RIIEIDDEpiaewddtlELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSE--GFWHRMGDLGYLDDEGRLWFCGR 352
|
410 420 430
....*....|....*....|....*....|...
gi 2085927195 658 IDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV 690
Cdd:cd05910 353 KAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
518-720 |
5.84e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 56.31 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 518 LKVIILGGESIniGNV--KKLAEkcRW-MKFINHYGPTESTVG----CIAHS---IDLDHIQnCEIYN-KIGRPihgini 586
Cdd:COG1541 205 LKKGIFGGEPW--SEEmrKEIEE--RWgIKAYDIYGLTEVGPGvayeCEAQDglhIWEDHFL-VEIIDpETGEP------ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 587 yivdrsdqlVPVGAPGEICISGvglasgyvnneeLTNEkfidnpfhpGAKM--YKTGDLGRWMPD-----------GNIe 653
Cdd:COG1541 274 ---------VPEGEEGELVVTT------------LTKE---------AMPLirYRTGDLTRLLPEpcpcgrthpriGRI- 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2085927195 654 fLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIEMEGSFVQEKLAQAL 720
Cdd:COG1541 323 -LGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEALAEAI 388
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
269-657 |
8.52e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 56.06 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAG----------KHITYKELNEKANQVATLLMEKGAGKNSITAMMIRPSE--YSMIgiLGILKTGSAF 336
Cdd:PRK09274 16 AQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLefFALT--FALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 337 LPIDDESPVSRINHILKDSKADILIT-------DLCFLADKNIAAECLDITDKSIY----------TSQNTSNPDVQYDL 399
Cdd:PRK09274 94 VLVDPGMGIKNLKQCLAEAQPDAFIGipkahlaRRLFGWGKPSVRRLVTVGGRLLWggttlatllrDGAAAPFPMADLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 EDEVYVIYTSGTSGKPKGVKVKNKSLvnyslwvCDQI-------NINSDSRSLVTskysfdlcytsiFPVLSgggqvhfv 472
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMF-------EAQIealredyGIEPGEIDLPT------------FPLFA-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 473 dkevyLHSLSL----------------------IEYIHKNSITYLKMTPTLFSTLMED-VDMLASCPDLKVIILGGESIN 529
Cdd:PRK09274 227 -----LFGPALgmtsvipdmdptrpatvdpaklFAAIERYGVTNLFGSPALLERLGRYgEANGIKLPSLRRVISAGAPVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 530 IgnvkKLAEKCRWM-----KFINHYGPTEST-VGCIAHSIDLDHIQN--------CeiynkIGRPIHGINIYIVDRSDQL 595
Cdd:PRK09274 302 I----AVIERFRAMlppdaEILTPYGATEALpISSIESREILFATRAatdngagiC-----VGRPVDGVEVRIIAISDAP 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 596 ---------VPVGAPGEICISGVGLASGYVNNEELTNEKFIDNP----FHpgakmyKTGDLGRWMPDGNIEFLGR 657
Cdd:PRK09274 373 ipewddalrLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWH------RMGDLGYLDAQGRLWFCGR 441
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
508-690 |
1.02e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.93 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 508 DVDMLAscpdLKVIILGGESINIGNVKKLAEKCRWMKF-----INHYGPTEST---------VGCIAHSIDLDHIQNCEI 573
Cdd:PRK05851 268 DVDLGA----LRVALNGGEPVDCDGFERFATAMAPFGFdagaaAPSYGLAESTcavtvpvpgIGLRVDEVTTDDGSGARR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 574 YNKIGRPIHGINIYIVDRsDQLVPVGAP--GEICISGVGLASGYVNneeltnekfiDNPFHPGaKMYKTGDLGrWMPDGN 651
Cdd:PRK05851 344 HAVLGNPIPGMEVRISPG-DGAAGVAGReiGEIEIRGASMMSGYLG----------QAPIDPD-DWFPTGDLG-YLVDGG 410
|
170 180 190
....*....|....*....|....*....|....*....
gi 2085927195 652 IEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV 690
Cdd:PRK05851 411 LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVV 449
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
386-664 |
1.03e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 55.88 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 386 TSQNTSNPDVQYDLEDEVYVI-YTSGTSGKPKGVKVKNKSLVNYSLWVCDqiniNSdsrslVTSKYSFD--LCY------ 456
Cdd:PTZ00342 289 TKNKTTNYKIQNEDPDFITSIvYTSGTSGKPKGVMLSNKNLYNTVVPLCK----HS-----IFKKYNPKthLSYlpishi 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 457 ---TSIFPVLSGGGQVHFVDKEVYLHSLSLieYIHKNSItyLKMTPTLFS----TLMEDVDMLASC-------------- 515
Cdd:PTZ00342 360 yerVIAYLSFMLGGTINIWSKDINYFSKDI--YNSKGNI--LAGVPKVFNriytNIMTEINNLPPLkrflvkkilslrks 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 516 -------------------------PDLKVIILGGESINignvKKLAEKCRWM---KFINHYGPTESTVGciahsIDLDH 567
Cdd:PTZ00342 436 nnnggfskflegithisskikdkvnPNLEVILNGGGKLS----PKIAEELSVLlnvNYYQGYGLTETTGP-----IFVQH 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 568 IQNCEiYNKIGRPIHGINIYIV------DRSDQLvpvgAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTG 641
Cdd:PTZ00342 507 ADDNN-TESIGGPISPNTKYKVrtwetyKATDTL----PKGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTG 575
|
330 340
....*....|....*....|...
gi 2085927195 642 DLGRWMPDGNIEFLGRIDNQIKI 664
Cdd:PTZ00342 576 DIVQINKNGSLTFLDRSKGLVKL 598
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
854-1015 |
3.06e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.96 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 854 YQASSAQKRMFALWETDKDSIVYNLPIMIELNGkLDVKKAESVLQEIIGRHEALRTSFDVVSDD--VVQIIHDTWELEFD 931
Cdd:PRK12316 4103 YPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGELgrPLQVVHKQVSLPFA 4181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 932 YQ------KLPSDGIRPYVKQFIRPFHLDKSPLIRAGLI-TYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQ 1004
Cdd:PRK12316 4182 ELdwrgraDLQAALDALAAAERERGFDLQRAPLLRLVLVrTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRPPAQ 4261
|
170
....*....|.
gi 2085927195 1005 PPLQSKDYSEW 1015
Cdd:PRK12316 4262 PGGRYRDYIAW 4272
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
286-690 |
3.74e-07 |
|
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: 54.01 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 286 TYKELNEKANQVATLLMEKGAGKNSITAMMIRPSEYSMIGILGILKTGSAFLPIDDESPVSRINHILKDSKADILItdLC 365
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF--VG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 366 FLAD-KNIAAECLDITDKSIYTSQNTSNPDVQYD--------LEDE--------VYVIYTSGTSGKPKGVKvknKSLVNY 428
Cdd:cd05932 86 KLDDwKAMAPGVPEGLISISLPPPSAANCQYQWDdliaqhppLEERptrfpeqlATLIYTSGTTGQPKGVM---LTFGSF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 429 SlWVCDQ----ININSDSRSLvtsKYsFDLCY----TSIF-PVLSGGGQVHFVDkevylhSL-SLIEYIHKNSITYLKMT 498
Cdd:cd05932 163 A-WAAQAgiehIGTEENDRML---SY-LPLAHvterVFVEgGSLYGGVLVAFAE------SLdTFVEDVQRARPTLFFSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 499 PTLFSTLMEDV---------DMLASCPDL---------------KVIILGGESINIGNVKKLAEKCRWMKFINHYGPTES 554
Cdd:cd05932 232 PRLWTKFQQGVqdkipqqklNLLLKIPVVnslvkrkvlkglgldQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTEN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 555 tvgcIAHSidldHIqNCEIYNKIG---RPIHGINIYIVDRsdqlvpvgapGEICISGVGLASGYVNNEELTNEKFIDNPF 631
Cdd:cd05932 312 ----FAYS----HL-NYPGRDKIGtvgNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 632 hpgakmYKTGDLGRWMPDGNIEFLGRIDNQIKI-RGFRVEIGEIENQLLQLEGIKEAAVV 690
Cdd:cd05932 373 ------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
762-837 |
4.35e-07 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 48.79 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 762 EAPANETEEKL----AEIWKEMLGH---KRISINEDFFELGGHSLTAAFTISRIRKTFGTDIKVKELFEQPTIKQLSRLI 834
Cdd:smart00823 3 ALPPAERRRLLldlvREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
|
...
gi 2085927195 835 QKR 837
Cdd:smart00823 83 AAE 85
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
641-766 |
5.42e-07 |
|
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: 53.43 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 641 GDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYlsayitGDIEM-------EGSFVQ 713
Cdd:cd05943 489 GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKD------GDERVilfvklrEGVELD 562
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2085927195 714 EKLAQAL---------PKYmIPSFIIQLKELPLTANGKinRKELPLPD-LQRLSVPRYEAPAN 766
Cdd:cd05943 563 DELRKRIrstirsalsPRH-VPAKIIAVPDIPRTLSGK--KVEVAVKKiIAGRPVKNAGALAN 622
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
602-678 |
1.22e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 52.43 E-value: 1.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2085927195 602 GEICISGVGLASGYVNNEELTNEKFIDNpfHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIR-GFRVEIGEIENQL 678
Cdd:PLN02387 503 GEIVIGGPSVTLGYFKNQEKTDEVYKVD--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
260-666 |
1.57e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.87 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 260 TIQDLFEERAEKTPDQTAAVY-------AG--KHITYKELNEKANQVATLLMEKGAGKNSitAMMIRPS--EYsMIGILG 328
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFidyeqdpAGvaETLTWSQLYRRTLNVAEELRRHGSTGDR--AVILAPQglEY-IVAFLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 329 ILKTGSAFLP-------IDDEspvsRINHILKDSKADILITDLCFLAD--KNIAAECLDITDKSI------YTSQNTSNP 393
Cdd:PRK05850 79 ALQAGLIAVPlsvpqggAHDE----RVSAVLRDTSPSVVLTTSAVVDDvtEYVAPQPGQSAPPVIevdlldLDSPRGSDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 394 DVQyDLEDEVYVIYTSGTSGKPKGVKVKNKSL-VNyslwvCDQI---------NINSDSRSLVtSKYSF--D--LCYTSI 459
Cdd:PRK05850 155 RPR-DLPSTAYLQYTSGSTRTPAGVMVSHRNViAN-----FEQLmsdyfgdtgGVPPPDTTVV-SWLPFyhDmgLVLGVC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 460 FPVLSGGGQVhfvdkevylhSLSLIEYIHKNS--ITYLKMTPTLFS-------------TLMEDVDMLascpDL---KVI 521
Cdd:PRK05850 228 APILGGCPAV----------LTSPVAFLQRPArwMQLLASNPHAFSaapnfafelavrkTSDDDMAGL----DLggvLGI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 522 ILGGESINIGNVKKLAEkcRWMKFINH-------YGPTESTV-------GCIAHSIDLD-------HIQNCEiyNKIGRP 580
Cdd:PRK05850 294 ISGSERVHPATLKRFAD--RFAPFNLRetairpsYGLAEATVyvatrepGQPPESVRFDyeklsagHAKRCE--TGGGTP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 581 IHGiniYIVDRSdQLV-----------PVGAPGEICISGVGLASGYVNNEELTNEKF---IDNPFH--PGAKMYKTGDLG 644
Cdd:PRK05850 370 LVS---YGSPRS-PTVrivdpdtciecPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPgtPEGPWLRTGDLG 445
|
490 500
....*....|....*....|..
gi 2085927195 645 rWMPDGNIEFLGRIDNQIKIRG 666
Cdd:PRK05850 446 -FISEGELFIVGRIKDLLIVDG 466
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
283-702 |
2.57e-06 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 51.20 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 283 KHITYKELNEKANQVATLLMEKGAGK-NSITAMMIRPSE--YSMIG-------ILGILKTGSAflpiddESpvsrINHIL 352
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERfHGVGILGFNSPEwfIAAVGaifaggiAVGIYTTNSP------EA----CQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 353 KDSKADILITDlcflaDKNIAAECLDITDK-------------------SIYT-----SQNTSNPDVQYDLEDEVY---- 404
Cdd:cd05933 77 ETSEANILVVE-----NQKQLQKILQIQDKlphlkaiiqykeplkekepNLYSwdefmELGRSIPDEQLDAIISSQkpnq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 405 ---VIYTSGTSGKPKGVKVKNKSLVnyslWVCDQININSDSRSLVTSKYSF----DLCYTS-----IFPVLSGGGQVHFV 472
Cdd:cd05933 152 cctLIYTSGTTGMPKGVMLSHDNIT----WTAKAASQHMDLRPATVGQESVvsylPLSHIAaqildIWLPIKVGGQVYFA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 473 DKEvylhSL--SLIEYIHKNSITYLKMTPTLFSTLMED-VDMLASCPDLKVIIL---------------GGESINIGNvK 534
Cdd:cd05933 228 QPD----ALkgTLVKTLREVRPTAFMGVPRVWEKIQEKmKAVGAKSGTLKRKIAswakgvgletnlklmGGESPSPLF-Y 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 535 KLAEK--------------CRwmKFINH----------------------YGPTESTvGCiaHSIDLDhiQNCEIYNkIG 578
Cdd:cd05933 303 RLAKKlvfkkvrkalgldrCQ--KFFTGaapisretlefflslnipimelYGMSETS-GP--HTISNP--QAYRLLS-CG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 579 RPIHGINIYIVDRSDQlvpvgAPGEICISGVGLASGYVNNEELTNEKfIDNP--FHpgakmykTGDLGRWMPDGNIEFLG 656
Cdd:cd05933 375 KALPGCKTKIHNPDAD-----GIGEICFWGRHVFMGYLNMEDKTEEA-IDEDgwLH-------SGDLGKLDEDGFLYITG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2085927195 657 RIDNQIKIRGfrveiGE------IENQL-LQLEGIKEAAVVYIEEKYLSAYIT 702
Cdd:cd05933 442 RIKELIITAG-----GEnvppvpIEDAVkKELPIISNAMLIGDKRKFLSMLLT 489
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
29-113 |
3.62e-06 |
|
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: 50.78 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 29 ETCTSML--------KAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKMVGLFINAVPLRVKG 100
Cdd:cd20484 219 QTYTRRLpselsnqiKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRP--EERFDSLIGYFINMLPIRSRI 296
|
90
....*....|...
gi 2085927195 101 DGDTVFIALAQKL 113
Cdd:cd20484 297 LGEETFSDFIRKL 309
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
400-745 |
5.99e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 50.00 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 400 EDEVYVIYTSGTSGKPKGVKVKNKSLV-NYSLWVCDQININSDSR------------------SLVTSKYSFDLCYTSIF 460
Cdd:PRK09192 176 DDIAYLQYSSGSTRFPRGVIITHRALMaNLRAISHDGLKVRPGDRcvswlpfyhdmglvgfllTPVATQLSVDYLPTRDF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 461 PVlsgggqvhfvdkevylHSLSLIEYIHKN--SITYlkmTPTlF----------STLMEDVDMlaSCpdLKVIILGGESI 528
Cdd:PRK09192 256 AR----------------RPLQWLDLISRNrgTISY---SPP-FgyelcarrvnSKDLAELDL--SC--WRVAGIGADMI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 529 NIGNVKKLAEKCRWM-----KFINHYGPTESTV---------GCIAHSIDLDHIQNCEI----------YNKI---GRPI 581
Cdd:PRK09192 312 RPDVLHQFAEAFAPAgfddkAFMPSYGLAEATLavsfsplgsGIVVEEVDRDRLEYQGKavapgaetrrVRTFvncGKAL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 582 HGINIYIVDRSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNpfhpgakMYKTGDLGrWMPDGNIEFLGRIDNQ 661
Cdd:PRK09192 392 PGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADG-------WLDTGDLG-YLLDGYLYITGRAKDL 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 662 IKIRGFRVEIGEIENQLLQLEGIK--EAAVVYIEEKYLSAYI------TGDIEMEGSFVQEklAQALPKYMIP-SFIIQL 732
Cdd:PRK09192 464 IIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIVllvqcrISDEERRGQLIHA--LAALVRSEFGvEAAVEL 541
|
410
....*....|....*.
gi 2085927195 733 ---KELPLTANGKINR 745
Cdd:PRK09192 542 vppHSLPRTSSGKLSR 557
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
882-1012 |
2.15e-05 |
|
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: 48.25 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 882 IELNGK-LDVKKAESVLQEIIGRHEALRTsfdVVSDDVVQIIHDT---WELE-FDYQKLPSDGIRPYVKQfIRP------ 950
Cdd:cd19535 30 LEFDGEdLDPDRLERAWNKLIARHPMLRA---VFLDDGTQQILPEvpwYGITvHDLRGLSEEEAEAALEE-LRErlshrv 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2085927195 951 FHLDKSPL--IRAGLItYEDRNLLLLDVHHIAADGVSVGIIRKEFNALYAGHKLKQPPLQS--KDY 1012
Cdd:cd19535 106 LDVERGPLfdIRLSLL-PEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPLPPLELsfRDY 170
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
549-746 |
2.73e-05 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 48.19 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 549 YGPTESTVGCIAHSI-DLDHiqnceiyNKIGRPIHGINIYIVDRsdqlvpvgapGEICISGVGLASGYVNNEELTNEKFI 627
Cdd:cd17641 355 YGQTELAGAYTVHRDgDVDP-------DTVGVPFPGTEVRIDEV----------GEILVRSPGVFVGYYKNPEATAEDFD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 628 DNPFhpgakmYKTGDLGRWMPDGNIEFLGRIDNQIKI-RGFRVEIGEIENQLLQLEGIKEAAVVYIEEKYLSAYITGDIE 706
Cdd:cd17641 418 EDGW------LHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFICIDYA 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085927195 707 MEGSFVQ--------------------------EKLAQALP-KYMIPSFIIQLKEL-----PLTANGKINRK 746
Cdd:cd17641 492 IVGKWAEqrgiafttytdlasrpevyelirkevEKVNASLPeAQRIRRFLLLYKELdaddgELTRTRKVRRG 563
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
545-658 |
3.57e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 47.66 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 545 FINHYGPTEST-VGCIAHSIDLDhiqnceiYNKIGRPIHGINIYIVD-----RSDQLVPvgaPGEICISGVGLASGYVNN 618
Cdd:PTZ00216 455 VIQGWGLTETVcCGGIQRTGDLE-------PNAVGQLLKGVEMKLLDteeykHTDTPEP---RGEILLRGPFLFKGYYKQ 524
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2085927195 619 EELTNEKFI-DNPFHpgakmykTGDLGRWMPDGNIEFLGRI 658
Cdd:PTZ00216 525 EELTREVLDeDGWFH-------TGDVGSIAANGTLRIIGRV 558
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
577-690 |
6.39e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.91 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 577 IGRPIHGINIYIVDRSDQLVPVGAPGEICISGVGLASGYvnneeLTNEKFIdnPFHPGAKMYKTGDLGRWMPDGNIEFLG 656
Cdd:PRK07768 362 LGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCG 434
|
90 100 110
....*....|....*....|....*....|....
gi 2085927195 657 RIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAVV 690
Cdd:PRK07768 435 RVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
259-674 |
1.06e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 46.19 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 259 KTIQDLFEERAEKTPD-----QTAAVYAGKH-ITYKELNEKANQVATLLMEKGAGK---------NSI-------TAMMI 316
Cdd:PRK12582 49 RSIPHLLAKWAAEAPDrpwlaQREPGHGQWRkVTYGEAKRAVDALAQALLDLGLDPgrpvmilsgNSIehalmtlAAMQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 317 R-------PSeYSMIG--------ILGILKTGSAFlpIDDESPVSRINHILKDSKADILITDLCFLADKNIAAECLDIT- 380
Cdd:PRK12582 129 GvpaapvsPA-YSLMShdhaklkhLFDLVKPRVVF--AQSGAPFARALAALDLLDVTVVHVTGPGEGIASIAFADLAATp 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 381 -DKSIYTSQNTSNPDVQYDLedevyvIYTSGTSGKPKGVkvknkslVNYSLWVCD----QININSDSRSLVTSKYSFDLC 455
Cdd:PRK12582 206 pTAAVAAAIAAITPDTVAKY------LFTSGSTGMPKAV-------INTQRMMCAniamQEQLRPREPDPPPPVSLDWMP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 456 YTSIF-------PVLSGGGQVHFVD-KEVYLHSLSLIEYIHKNSITYLKMTPTLFSTL---ME-DVDMLASC-PDLKVII 522
Cdd:PRK12582 273 WNHTMggnanfnGLLWGGGTLYIDDgKPLPGMFEETIRNLREISPTVYGNVPAGYAMLaeaMEkDDALRRSFfKNLRLMA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 523 LGGESINIGNVKKL-----AEKCRWMKFINHYGPTE-STVGCIAHSIdldhiqnCEIYNKIGRPIHGINIyivdrsdQLV 596
Cdd:PRK12582 353 YGGATLSDDLYERMqalavRTTGHRIPFYTGYGATEtAPTTTGTHWD-------TERVGLIGLPLPGVEL-------KLA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 597 PVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWM----PDGNIEFLGRIDNQIKI-RGFRVEI 671
Cdd:PRK12582 419 PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGRVAEDFKLsTGTWVSV 492
|
...
gi 2085927195 672 GEI 674
Cdd:PRK12582 493 GTL 495
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
549-704 |
1.09e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 46.25 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 549 YGPTESTvgCIAHSIDLDHiqncEIYNKIGRPIHGINIYIVD-------RSDQLVPvgaPGEICISGVGLASGYVNNEEL 621
Cdd:PLN02736 408 YGMTETS--CVISGMDEGD----NLSGHVGSPNPACEVKLVDvpemnytSEDQPYP---RGEICVRGPIIFKGYYKDEVQ 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 622 TNEkFIDNP--FHpgakmykTGDLGRWMPDGNIEFLGRIDNQIKI-RGFRVEIGEIENqllqlegikeaavVYIEEKYLS 698
Cdd:PLN02736 479 TRE-VIDEDgwLH-------TGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIEN-------------VYAKCKFVA 537
|
....*..
gi 2085927195 699 -AYITGD 704
Cdd:PLN02736 538 qCFVYGD 544
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
843-1016 |
1.16e-04 |
|
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: 46.39 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 843 PVISKARKQSYYQASSAQKRMFALWETDKDSIVYNLPIMIELNGKLDVKKAESVLQEIIGRHEALRTSFDVVSDDVVQII 922
Cdd:COG1020 7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 923 HDTWELEFDYQKLPSDGIRPYVKQ--------FIRPFHLDKSPLIRAGLI-----TYEDRNLLLLDVHHIAADGVSVGII 989
Cdd:COG1020 87 QPVVAAPLPVVVLLVDLEALAEAAaeaaaaaeALAPFDLLRGPLLRLLLLlllllLLLLLLALHHIISDGLSDGLLLAEL 166
|
170 180
....*....|....*....|....*....
gi 2085927195 990 RKEFNALYAGHKLKQPPL--QSKDYSEWQ 1016
Cdd:COG1020 167 LRLYLAAYAGAPLPLPPLpiQYADYALWQ 195
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
588-666 |
1.32e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 45.88 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 588 IVD-RSDQLVPVGAPGEICISGVGLASGYVNNEELTNEKFID------NPFH-----PGAKMYKTGDLGRWMpDGNIEFL 655
Cdd:PRK07769 404 IVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNilksrlSESHaegapDDALWVRTGDYGVYF-DGELYIT 482
|
90
....*....|.
gi 2085927195 656 GRIDNQIKIRG 666
Cdd:PRK07769 483 GRVKDLVIIDG 493
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
11-109 |
1.68e-04 |
|
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: 45.33 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 11 SSADEGGfnnrKKTFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKMVGLF 90
Cdd:cd19538 217 ESSYEGG----TLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRN--DDSLEDLVGFF 290
|
90
....*....|....*....
gi 2085927195 91 INAVPLRVKGDGDTVFIAL 109
Cdd:cd19538 291 VNTLVLRTDTSGNPSFREL 309
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
18-111 |
1.70e-04 |
|
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: 45.14 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 18 FNNRKKTFIIDETCTSMLKAAADQYHIT-----LSALiQtawgVLLQKYNNVNDVVFGAVISGRqcRVQGIEKMVGLFIN 92
Cdd:cd19532 213 YDTHTAERRLDAALAARIKEASRKLRVTpfhfyLAAL-Q----VLLARLLDVDDICIGIADANR--TDEDFMETIGFFLN 285
|
90
....*....|....*....
gi 2085927195 93 AVPLRVKGDGDTVFIALAQ 111
Cdd:cd19532 286 LLPLRFRRDPSQTFADVLK 304
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
269-418 |
3.95e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 44.17 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 269 AEKTPDQTAAVYAG------KHITYKELNEKANQVATLLMEKGAGKNS---ITAMMIRPSEYSM-----IG-----ILGI 329
Cdd:PRK10524 63 LAKRPEQLALIAVStetdeeRTYTFRQLHDEVNRMAAMLRSLGVQRGDrvlIYMPMIAEAAFAMlacarIGaihsvVFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 330 LKTGSAFLPIDDESPV--------SRINHILkDSKAdiLITDLCFLADKNIAAecLDITDKSIYTSQNTSNPDVQYD--- 398
Cdd:PRK10524 143 FASHSLAARIDDAKPVlivsadagSRGGKVV-PYKP--LLDEAIALAQHKPRH--VLLVDRGLAPMARVAGRDVDYAtlr 217
|
170 180 190
....*....|....*....|....*....|....
gi 2085927195 399 ---LEDEV-----------YVIYTSGTSGKPKGV 418
Cdd:PRK10524 218 aqhLGARVpvewlesnepsYILYTSGTTGKPKGV 251
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
577-658 |
5.18e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 44.10 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 577 IGRPIHGINIyivdrsdQLVPVGAPGEICISGVGLASGYVNNEELTNEKFIDNPFhpgakmYKTGDLGRWM----PDGNI 652
Cdd:PRK08180 394 IGLPAPGCEV-------KLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRFVdpadPERGL 460
|
....*.
gi 2085927195 653 EFLGRI 658
Cdd:PRK08180 461 MFDGRI 466
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
24-109 |
9.81e-04 |
|
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: 42.80 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 24 TFIIDETCTSMLKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQcrVQGIEKMVGLFINAVPLRVKGDGD 103
Cdd:cd19540 226 EFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRG--DEALDDLVGMFVNTLVLRTDVSGD 303
|
....*.
gi 2085927195 104 TVFIAL 109
Cdd:cd19540 304 PTFAEL 309
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
35-109 |
1.18e-03 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 42.47 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085927195 35 LKAAADQYHITLSALIQTAWGVLLQKYNNVNDVVFGAVISGRQCRVqGIEKMVGLFINAVPLRVKGDGDTVFIAL 109
Cdd:cd19546 240 LMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEG-DLEGMVGPFARPLALRTDLSGDPTFREL 313
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
614-731 |
1.63e-03 |
|
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: 42.28 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085927195 614 GYVNNEELTNEKFIDNPFHPGAKMYKTGDLGRWMPDGNIEFLGRIDNQIKIRGFRVEIGEIENQLLQLEGIKEAAV--VY 691
Cdd:cd05938 364 GYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVT 443
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2085927195 692 I---EEKYLSAYIT--GDIEMEGSFVQEKLAQALPKYMIPSFI-IQ 731
Cdd:cd05938 444 VpghEGRIGMAAVKlkPGHEFDGKKLYQHVREYLPAYARPRFLrIQ 489
|
|
| |
