|
Name |
Accession |
Description |
Interval |
E-value |
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3-1033 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 602.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEqpeigFVASQLPVP 82
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQ-----WVDPALTFP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 igVLPIVELLPAPmtDEEQTIRQWARDEISLPLDLLNGLPCRFALL--CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQI 160
Cdd:PRK10252 84 --LPEIIDLRTQP--DPHAAAQALMQADLQQDLRVDSGKPLVFHQLiqLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 161 YTALTAGQSAPVAEFGPFSAVLEEERQRDASGQTAQARDFWLETLNAMPEPASFSEKKAPI---AARFLRQSCDMPADLW 237
Cdd:PRK10252 160 YCAWLRGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGrsaSADILRLKLEFTDGAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 238 QPLSALCEGnkISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFVALAQQVA 317
Cdd:PRK10252 240 RQLAAQASG--VQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 318 RTKRTLRRHQHYRYEHLRRDLNRVGGEQRLFGPLINIMPFDHPLNYGSLSSSTLNLSAGPVEDLTIEIHFKPDGTPVLDF 397
Cdd:PRK10252 318 AQLKKMRRHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLELALFPDEHGGLSIEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 398 DANPACYSAEALASLQETLFTLLQRWLAQPQQTSGELLGRWLREERELALIT-SREPEPfvEPVLTA-IAKQARKNPSHI 475
Cdd:PRK10252 398 LANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNaTAVEIP--ETTLSAlVAQQAAKTPDAP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 476 ALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAG 555
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDAR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 556 LRTIVTQADYQHRLASVFSGAIVLAGHLLssnAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQ 635
Cdd:PRK10252 556 PSLLITTADQLPRFADVPDLTSLCYNAPL---APQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQN 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 636 RYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESiPTFVEQV-DAQAITLLDLPTAFWNEWVVGLKTGT 714
Cdd:PRK10252 633 HYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRD-PLAMQQFfAEYGVTTTHFVPSMLAAFVASLTPEG 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 715 LTMPSA-LRAIIIGGEAVYPEQLVQWQR--HAPdtlrLINTYGPTETTVvatscDLQTQPA---DVAQ-----LPIGLPL 783
Cdd:PRK10252 712 ARQSCAsLRQVFCSGEALPADLCREWQQltGAP----LHNLYGPTEAAV-----DVSWYPAfgeELAAvrgssVPIGYPV 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 784 AGVNALVLAAGDRP---AAEGELVLLGPTLAAGYIGT-EHTAFTLLAvgDRHLPA---YRTGDRVR-LEKGHLLYLGRMD 855
Cdd:PRK10252 783 WNTGLRILDARMRPvppGVAGDLYLTGIQLAQGYLGRpDLTASRFIA--DPFAPGermYRTGDVARwLDDGAVEYLGRSD 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 856 NEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVY------PNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPAMIPT 928
Cdd:PRK10252 861 DQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVInqaaatGGDARQLVGYLVSQSGLpLDTSALQAQLRERLPPHMVPV 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 929 DYRAFHQLPKTGSNKVDRKRL-LAEYHDDAPTQALASETENRVSAIWQQILGVSGIQSRDNFFELGGQSLQTIQIVNRLA 1007
Cdd:PRK10252 941 VLLQLDQLPLSANGKLDRKALpLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLS 1020
|
1050 1060
....*....|....*....|....*.
gi 499404633 1008 AEFSVSIKVSDVFDHPQLSDFCRYLD 1033
Cdd:PRK10252 1021 RQFARQVTPGQVMVASTVAKLATLLD 1046
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3-1023 |
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: 565.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMEceclycqfVEVAGEHAEQPEIGFVASQLPVP 82
Cdd:COG1020 19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARR--------RRALRTRLRTRAGRPVQVIQPVV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPIVELLPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:COG1020 91 AAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLlLLLLLLLLLLALHHIISDGLSDGLLLAELLRLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAE-FGPFSAVLEEERQRDASGQTAQARDFWLETLNAMPEPASFSEKKAPIAA---RFLRQSCDMPADLW 237
Cdd:COG1020 171 LAAYAGAPLPLPPlPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVqsyRGARVSFRLPAELT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 238 QPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFVALAQQVA 317
Cdd:COG1020 251 AALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 318 RTKRTLRRHQHYRYEHLRRDLNRVGGEQRlfGPLINIM------PFDHPLNYGSLSSSTLNLSAGPVEDLTIEIHFKPDG 391
Cdd:COG1020 331 ETLLAAYAHQDLPFERLVEELQPERDLSR--NPLFQVMfvlqnaPADELELPGLTLEPLELDSGTAKFDLTLTVVETGDG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 392 tPVLDFDANPACYSAEALASLQETLFTLLQRWLAQPQQTSGELlgRWL-REERELALIT---SREPEPFVEPVLTAIAKQ 467
Cdd:COG1020 409 -LRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDL--PLLtAAERQQLLAEwnaTAAPYPADATLHELFEAQ 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQ 547
Cdd:COG1020 486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 548 QHIIQIAGLRTIVTQADYQHRLASvfSGAIVLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIGASALD 627
Cdd:COG1020 566 AYMLEDAGARLVLTQSALAARLPE--LGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 628 HFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNEWV 707
Cdd:COG1020 644 NLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALL 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 708 VGLKTGtltmPSALRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATSCDLQTQPADVAQLPIGLPLAGVN 787
Cdd:COG1020 724 DAAPEA----LPSLRLVLVGGEALPPELVRRWRARLPGA-RLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTR 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 788 ALVLAAGDRPA---AEGELVLLGPTLAAGYIG-TEHTA--F---TLLAVGDRhlpAYRTGDRVR-LEKGHLLYLGRMDNE 857
Cdd:COG1020 799 VYVLDAHLQPVpvgVPGELYIGGAGLARGYLNrPELTAerFvadPFGFPGAR---LYRTGDLARwLPDGNLEFLGRADDQ 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 858 FKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTDYRAFHQL 936
Cdd:COG1020 876 VKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGaAAAAALLRLALALLLPPYMVPAAVVLLLPL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 937 PKTGSNKVDRKRLLAEYHDDAPTQALASETENRV-SAIWQQILGVSGIQSRDNFFELGGQSLQTIQIVNRLAAEFSVSIK 1015
Cdd:COG1020 956 PLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEeAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLL 1035
|
....*...
gi 499404633 1016 VSDVFDHP 1023
Cdd:COG1020 1036 LLLLFLAA 1043
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
472-949 |
6.03e-144 |
|
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: 438.11 E-value: 6.03e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADyqhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVEIGASALDHFTA 631
Cdd:cd05930 81 EDSGAKLVLTDPD-------------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 AARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNEWvvgLK 711
Cdd:cd05930 124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLL---LQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 712 TGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATSCDLQTQPADVAQLPIGLPLAGVNALVL 791
Cdd:cd05930 201 ELELAALPSLRLVLVGGEALPPDLVRRWRELLPGA-RLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 792 AAGDRPA---AEGELVLLGPTLAAGYIGTEH-TAFTLLAV----GDRhlpAYRTGDRVR-LEKGHLLYLGRMDNEFKISG 862
Cdd:cd05930 280 DENLRPVppgVPGELYIGGAGLARGYLNRPElTAERFVPNpfgpGER---MYRTGDLVRwLPDGNLEFLGRIDDQVKIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 863 YRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGS 941
Cdd:cd05930 357 YRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGgELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPN 436
|
....*...
gi 499404633 942 NKVDRKRL 949
Cdd:cd05930 437 GKVDRKAL 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-1033 |
7.14e-137 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 457.32 E-value: 7.14e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpeigfVASQLPVP 82
Cdd:PRK12467 51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQV-----IDASLSLT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPIVELLPapmTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:PRK12467 126 IPLDDLANEQG---RARESQIEAYINEEVARPFDLANGPLLRVRLLrLADDEHVLVVTLHHIISDGWSMRVLVEELVQLY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAEFgPFSAVLEEERQRD--ASGQTAQARDFWLETLNA----------MPEPASFSEKKApiaarflRQS 229
Cdd:PRK12467 203 SAYSQGREPSLPAL-PIQYADYAIWQRSwlEAGERERQLAYWQEQLGGehtvlelptdRPRPAVPSYRGA-------RLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 230 CDMPADLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANF 309
Cdd:PRK12467 275 VDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 310 VALAQQVARTKRTLRRHQHYRYEHLRRDLNrvggEQRLFG--PLINIMpFDH-PLNYGSLSSSTLNLSAGPVE------- 379
Cdd:PRK12467 355 LELLQQVKRTALGAQAHQDLPFEQLVEALQ----PERSLShsPLFQVM-FNHqNTATGGRDREGAQLPGLTVEelswarh 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 380 ----DLTIEIHFKPDG-----TPVLDFdanpacYSAEALASLQETLFTLLQRWLAQPQQTSGELlGRWLREERELALITS 450
Cdd:PRK12467 430 taqfDLALDTYESAQGlwaafTYATDL------FEATTIERLATHWRNLLEAIVAEPRRRLGEL-PLLDAEERARELVRW 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 451 REPEPFVEP--VLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAV 528
Cdd:PRK12467 503 NAPATEYAPdcVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAV 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 529 MQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRL---ASVFSGAIVLAGHLLSSNAQAVALPTAESRegQIAY 605
Cdd:PRK12467 583 LKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLpvpAGLRSLCLDEPADLLCGYSGHNPEVALDPD--NLAY 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 606 VMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFV 685
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFA 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 686 EQVDAQAITLLDLPTAFWNEWvvgLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATSC 765
Cdd:PRK12467 741 ALMADQGVTVLKIVPSHLQAL---LQASRVALPRPQRALVCGGEALQVDLLARVRALGPGA-RLINHYGPTETTVGVSTY 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 766 DLQTQPADVAQLPIGLPLAGVNALVLAAGDRPA---AEGELVLLGPTLAAGYIGteHTAFTllavGDRHLPA-------- 834
Cdd:PRK12467 817 ELSDEERDFGNVPIGQPLANLGLYILDHYLNPVpvgVVGELYIGGAGLARGYHR--RPALT----AERFVPDpfgadggr 890
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 835 -YRTGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGvRRLVAFVATKEGEIDAR- 911
Cdd:PRK12467 891 lYRTGDLARYRAdGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAG-LQLVAYLVPAAVADGAEh 969
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 912 -----ALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEyhDDAPTQ----ALASETENRVSAIWQQILGVSG 982
Cdd:PRK12467 970 qatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKP--DASAVQatfvAPQTELEKRLAAIWADVLKVER 1047
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 499404633 983 IQSRDNFFELGGQSLQTIQIVNRLAAEFSVSIKVSDVFDHPQLSDFCRYLD 1033
Cdd:PRK12467 1048 VGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVA 1098
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
485-885 |
1.30e-124 |
|
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: 386.24 E-value: 1.30e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQAAAALHER-GVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQA 563
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 DYQHRLASVFSGAIVLAGHLLSSNAQAVALPTAESREG--QIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRA 641
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGpdDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 642 EDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQ-AITLLDLPTAFWNEWVVGLktgtLTMPSA 720
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEhPVTVLNLTPSLLALLAAAL----PPALAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 721 LRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATSCDLQTQPADVAQ-LPIGLPLAGVNALVLAAGDRPA- 798
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRARGPGA-RLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTRLYVLDDDLRPVp 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 799 --AEGELVLLGPTLAAGYIGT-EHTA---FTLLAVGDRHLPAYRTGDRVR-LEKGHLLYLGRMDNEFKISGYRIQPGEVE 871
Cdd:TIGR01733 316 vgVVGELYIGGPGVARGYLNRpELTAerfVPDPFAGGDGARLYRTGDLVRyLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395
|
410
....*....|....
gi 499404633 872 AHLLAQPEVDEACV 885
Cdd:TIGR01733 396 AALLRHPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
464-949 |
1.02e-123 |
|
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: 387.08 E-value: 1.02e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQHIIQIAGLRTIVTQADYQHRLASVFsgAIVLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIGA 623
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVEL--VAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 624 SALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFW 703
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 704 nEWVVGLKTGTLTMPSALRAIIIGGEA-VYPEQLVQWQRHAPdTLRLINTYGPTETTVVaTSCDLQTQPAD-VAQLPIGL 781
Cdd:cd17651 239 -RALAEHGRPLGVRLAALRYLLTGGEQlVLTEDLREFCAGLP-GLRLHNHYGPTETHVV-TALSLPGDPAAwPAPPPIGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 782 PLAGVNALVLAAGDRPAA---EGELVLLGPTLAAGYIGT-EHTAFTLLA---VGDRHLpaYRTGDRVR-LEKGHLLYLGR 853
Cdd:cd17651 316 PIDNTRVYVLDAALRPVPpgvPGELYIGGAGLARGYLNRpELTAERFVPdpfVPGARM--YRTGDLARwLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 854 MDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFV-ATKEGEIDARALKQRLSSVLPPAMIPTDYRA 932
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVvGDPEAPVDAAELRAALATHLPEYMVPSAFVL 473
|
490
....*....|....*..
gi 499404633 933 FHQLPKTGSNKVDRKRL 949
Cdd:cd17651 474 LDALPLTPNGKLDRRAL 490
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-1022 |
4.13e-121 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 411.09 E-value: 4.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEvageHAEQPEigfvasQLPVP 82
Cdd:PRK12467 1118 PLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ----EDGRTR------QVIHP 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPIVELLPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:PRK12467 1188 VGSLTLEEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLrLAADEHVLVLTLHHIVSDGWSMQVLVDELVALY 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAEFgPFS----AVLEeeRQRDASGQTAQARDFW----------LETLNAMPEPASFSEKKAPIAARFlr 227
Cdd:PRK12467 1268 AAYSQGQSLQLPAL-PIQyadyAVWQ--RQWMDAGERARQLAYWkaqlggeqpvLELPTDRPRPAVQSHRGARLAFEL-- 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 228 qscdmPADLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQA 307
Cdd:PRK12467 1343 -----PPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQA 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 308 NFVALAQQVARTKRTLRRHQHYRYEHLRRDLNRvggEQRL-FGPLINIMpFDHPLNYGSLSSSTLNLSAGPVE------- 379
Cdd:PRK12467 1418 SFQQLLQQVKQAALEAQAHQDLPFEQLVEALQP---ERSLsHSPLFQVM-FNHQRDDHQAQAQLPGLSVESLSwesqtaq 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 380 -DLTIEIHFKPDG-----TPVLD-FDANpacySAEALAslqETLFTLLQRWLAQPQQTSGELlgRWLRE-ERELALITSR 451
Cdd:PRK12467 1494 fDLTLDTYESSEGlqaslTYATDlFEAS----TIERLA---GHWLNLLQGLVADPERRLGEL--DLLDEaERRQILEGWN 1564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 452 EPE---PFVEPVLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAV 528
Cdd:PRK12467 1565 ATHtgyPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAI 1644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 529 MQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLAS--------VFSGAIVLAGHLLSSNAQAVAlptaesrE 600
Cdd:PRK12467 1645 LKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLpdglrslvLDQEDDWLEGYSDSNPAVNLA-------P 1717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 601 GQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLES 680
Cdd:PRK12467 1718 QNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRD 1797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 681 IPTFVEQVDAQAITLLDLPTAFWNEWVVglKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTV 760
Cdd:PRK12467 1798 PEQLIQLIERQQVTTLHFVPSMLQQLLQ--MDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDT-GLFNLYGPTETAV 1874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 761 VAT--SCDLQtQPADVAQLPIGLPLAGVNALVLAAGDRPAA---EGELVLLGPTLAAGYI---GTEHTAFTLLAVGDRHL 832
Cdd:PRK12467 1875 DVThwTCRRK-DLEGRDSVPIGQPIANLSTYILDASLNPVPigvAGELYLGGVGLARGYLnrpALTAERFVADPFGTVGS 1953
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 833 PAYRTGDRVRLE-KGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGvRRLVAFVATKEGEIDA- 910
Cdd:PRK12467 1954 RLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVPTDPGLVDd 2032
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 911 --------RALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEyhDDAPTQ----ALASETENRVSAIWQQIL 978
Cdd:PRK12467 2033 deaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP--DASELQqayvAPQSELEQRLAAIWQDVL 2110
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 499404633 979 GVSGIQSRDNFFELGGQSLQTIQIVNRlAAEFSVSIKVSDVFDH 1022
Cdd:PRK12467 2111 GLEQVGLHDNFFELGGDSIISIQVVSR-ARQAGIRFTPKDLFQH 2153
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-1034 |
2.17e-120 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 408.78 E-value: 2.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLwLGHALNDDKA-TFNTAECIAFDGkVDIDAMLSAIRQAVMECECLYCQFVEVAGehAEQPeIGFVASQLPV 81
Cdd:PRK12467 2648 PLSPMQQGM-LFHTLYEGGAgDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGE--LEEP-LQVVYKQARL 2722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 82 PIgvlpiVELLPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQI 160
Cdd:PRK12467 2723 PF-----SRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVrTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQR 2797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 161 YTALTAGqsAPVAEFGPFSAVLEeeRQrDASGQTAqardFWLETLNAMPEPASFSEKKAPIAARFLRQSCD----MPADL 236
Cdd:PRK12467 2798 YFGQPPP--AREGRYRDYIAWLQ--AQ-DAEASEA----FWKEQLAALEEPTRLARALYPAPAEAVAGHGAhylhLDATQ 2868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 237 WQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRigSASLMVPSMQM----NIVPLCIQVDEQANFVAL 312
Cdd:PRK12467 2869 TRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGR--PAQLRGAEQQLglfiNTLPVIASPRAEQTVSDW 2946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 313 AQQVARTKRTLRRHQHYRYEHLRRDLNRVGgeQRLFGpliNIMPFD-HPLNYGSLSSSTLNLSAGPVED-------LTIE 384
Cdd:PRK12467 2947 LQQVQAQNLALREFEHTPLADIQRWAGQGG--EALFD---SILVFEnYPISEALKQGAPSGLRFGAVSSreqtnypLTLA 3021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 385 IHFkpDGTPVLDFDANPACYSAEALASLQETLFTLLQRWLAQPQQTSGEL--LGRWLREERELALITSREPEPFVEPVLT 462
Cdd:PRK12467 3022 VGL--GDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELptLAAHERRQVLHAWNATAAAYPSERLVHQ 3099
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQ 542
Cdd:PRK12467 3100 LIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY 3179
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQQHIIQIAGLRTIVTQADYQHRLASVfSGAIVLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIG 622
Cdd:PRK12467 3180 PRERLAYMIEDSGVKLLLTQAHLLEQLPAP-AGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVR 3258
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 623 ASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESiPTFVEQVDAQAITLLDLPTAF 702
Cdd:PRK12467 3259 HGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDP-EELWQAIHAHRISIACFPPAY 3337
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 703 WNEWVVGLKTGTLTmpsALRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVAT--SCDLQTQPADVAqLPIG 780
Cdd:PRK12467 3338 LQQFAEDAGGADCA---SLDIYVFGGEAVPPAAFEQVKRKLKPR-GLTNGYGPTEAVVTVTlwKCGGDAVCEAPY-APIG 3412
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 781 LPLAGVNALVLAAGDRPAAE---GELVLLGPTLAAGYigteHTAFTLLAvgDRHLPA---------YRTGDRVRLEK-GH 847
Cdd:PRK12467 3413 RPVAGRSIYVLDGQLNPVPVgvaGELYIGGVGLARGY----HQRPSLTA--ERFVADpfsgsggrlYRTGDLARYRAdGV 3486
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 848 LLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGvRRLVAF-VATKEGEIDARALKQRLSSVLPPAMI 926
Cdd:PRK12467 3487 IEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYvVPADPQGDWRETLRDHLAASLPDYMV 3565
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 927 PTDYRAFHQLPKTGSNKVDRKRL-LAEYHDDAPTQALASETENRVSAIWQQILGVSGIQSRDNFFELGGQSLQTIQIVNR 1005
Cdd:PRK12467 3566 PAQLLVLAAMPLGPNGKVDRKALpDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSR 3645
|
1050 1060
....*....|....*....|....*....
gi 499404633 1006 LAAEFSVSIKVSDVFDHPQLSDFCRYLDD 1034
Cdd:PRK12467 3646 IRQSLGLKLSLRDLMSAPTIAELAGYSPL 3674
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1030 |
1.39e-118 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 403.57 E-value: 1.39e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVaGEHAEQpEIGFVASQLPVP 82
Cdd:PRK12316 2604 PLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEV-GEQTRQ-VILPNMSLRIVL 2681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPIVEllpapmtdeeQTIRQWARDEISLPLDLLNGLPCRFALLCGEKRD-FLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:PRK12316 2682 EDCAGVAD----------AAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEhVLVITQHHIVSDGWSMQVMVDELVQAY 2751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAEFgPFSAVLEEERQRD--ASGQTAQARDFWLETLNA---MPEPASFSEKKAPIAARFLRQSCDMPADL 236
Cdd:PRK12316 2752 AGARRGEQPTLPPL-PLQYADYAAWQRAwmDSGEGARQLDYWRERLGGeqpVLELPLDRPRPALQSHRGARLDVALDVAL 2830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 237 WQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFVALAQQV 316
Cdd:PRK12316 2831 SRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQV 2910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 317 ARTKRTLRRHQHYRYEHLRRDLN--RVGGEQRLFGPLINIM--PFDHPLNYGSLSSSTLNLSAGPVEDLTIEIHFKPDGT 392
Cdd:PRK12316 2911 KEQALGAQAHQDLPFEQLVEALQpeRSLSHSPLFQVMYNHQsgERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGL 2990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 393 PV-LDFDANpaCYSAEALASLQETLFTLLQRWLAQPQQTSGELlGRWLREERELALITSREPE---PFVEPVLTAIAKQA 468
Cdd:PRK12316 2991 GAsLTYATD--LFDARTVERLARHWQNLLRGMVENPQRSVDEL-AMLDAEERGQLLEAWNATAaeyPLERGVHRLFEEQV 3067
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 469 RKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQ 548
Cdd:PRK12316 3068 ERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLA 3147
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 549 HIIQIAGLRTIVTQADYQHRLASVFSGAIVLAGHLLSSNAQAVALPTAESregqIAYVMFTSGSTGLPKGVEIGASALDH 628
Cdd:PRK12316 3148 YMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPEN----LAYVIYTSGSTGKPKGVGIRHSALSN 3223
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 629 FTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAItllDLPTAFWNEWVV 708
Cdd:PRK12316 3224 HLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGV---DVLHAYPSMLQA 3300
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 709 GLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPdtlrLINTYGPTETTVVATSCDLQTQpaDVAQLPIGLPLAGVNA 788
Cdd:PRK12316 3301 FLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP----LYNLYGPTEATITVTHWQCVEE--GKDAVPIGRPIANRAC 3374
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 789 LVLAAGDRP---AAEGELVLLGPTLAAGY-----IGTEHTAFTLLAVGDRhlpAYRTGDRVRL-EKGHLLYLGRMDNEFK 859
Cdd:PRK12316 3375 YILDGSLEPvpvGALGELYLGGEGLARGYhnrpgLTAERFVPDPFVPGER---LYRTGDLARYrADGVIEYIGRVDHQVK 3451
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 860 ISGYRIQPGEVEAHLLAQPEVDEACVQGIvypnGVRRLVAFVATKEGEIDAR-ALKQRLSSVLPPAMIPTDYRAFHQLPK 938
Cdd:PRK12316 3452 IRGFRIELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPEDEAGDLReALKAHLKASLPEYMVPAHLLFLERMPL 3527
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 939 TGSNKVDRKRLLAEYHDDAPTQALA--SETENRVSAIWQQILGVSGIQSRDNFFELGGQSLQTIQIVNRlAAEFSVSIKV 1016
Cdd:PRK12316 3528 TPNGKLDRKALPRPDAALLQQDYVApvNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSR-ARQAGIRFTP 3606
|
1050
....*....|....
gi 499404633 1017 SDVFDHPQLSDFCR 1030
Cdd:PRK12316 3607 KDLFQHQTIQGLAR 3620
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
472-949 |
1.10e-116 |
|
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: 367.08 E-value: 1.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQadyqhrlasvfsgaivlaghllssnaqavalptaesREGQIAYVMFTSGSTGLPKGVEIGASALDHFTA 631
Cdd:cd17649 81 EDSGAGLLLTH------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 AARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNEWVVGLK 711
Cdd:cd17649 125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEAD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 712 TGTLTMPSALRAIIIGGEAVYPEQLVQWQrhaPDTLRLINTYGPTETTVVATSCDLQTQPADV-AQLPIGLPLAGVNALV 790
Cdd:cd17649 205 RTGDGRPPSLRLYIFGGEALSPELLRRWL---KAPVRLFNAYGPTEATVTPLVWKCEAGAARAgASMPIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 791 LAAGDRP---AAEGELVLLGPTLAAGYIG-TEHTAFTLL-----AVGDRhlpAYRTGDRVR-LEKGHLLYLGRMDNEFKI 860
Cdd:cd17649 282 LDADLNPvpvGVTGELYIGGEGLARGYLGrPELTAERFVpdpfgAPGSR---LYRTGDLARwRDDGVIEYLGRVDHQVKI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 861 SGYRIQPGEVEAHLLAQPEVDEACVqgIVYP-NGVRRLVAFVATKEGEI---DARALKQRLSSVLPPAMIPTDYRAFHQL 936
Cdd:cd17649 359 RGFRIELGEIEAALLEHPGVREAAV--VALDgAGGKQLVAYVVLRAAAAqpeLRAQLRTALRASLPDYMVPAHLVFLARL 436
|
490
....*....|...
gi 499404633 937 PKTGSNKVDRKRL 949
Cdd:cd17649 437 PLTPNGKLDRKAL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1033 |
6.50e-116 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 395.48 E-value: 6.50e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLwLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAgeHAEQPeIGFVASQLPvp 82
Cdd:PRK12316 4104 PLSPMQQGM-LFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALDRHDVLRSGFVWQG--ELGRP-LQVVHKQVS-- 4177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 igvLPIVELLPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:PRK12316 4178 ---LPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVrTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQsaPVAEFGPFSAVLEeeRQRDASgqtaqARDFWLETLNAMPEPA----SFSEKKAPIAARFLRQSCDMPADLW 237
Cdd:PRK12316 4255 SGRPPAQ--PGGRYRDYIAWLQ--RQDAAA-----SEAFWREQLAALDEPTrlaqAIARADLRSANGYGEHVRELDATAT 4325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 238 QPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRigSASLMVPSMQM----NIVPLCIQVDEQANFVALA 313
Cdd:PRK12316 4326 ARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGR--PAELPGIEGQIglfiNTLPVIATPRAQQSVVEWL 4403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 314 QQVARTKRTLRRHQHYRYEHLRRDLNRvGGEQrLFGPLINI--MPFDHPLNYGSLSSSTLNLSAGPVED---LTIEIHFK 388
Cdd:PRK12316 4404 QQVQRQNLALREHEHTPLYEIQRWAGQ-GGEA-LFDSLLVFenYPVSEALQQGAPGGLRFGEVTNHEQTnypLTLAVGLG 4481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 389 PdgTPVLDFDANPACYSAEALASLQETLFTLLQRWLAQPQQTSGELlgRWLREE---RELALITSREPE-PFVEPVLTAI 464
Cdd:PRK12316 4482 E--TLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGEL--QLLEKAeqqRIVALWNRTDAGyPATRCVHQLV 4557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 465 AKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPR 544
Cdd:PRK12316 4558 AERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPR 4637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 545 ERQQHIIQIAGLRTIVTQADYQHRL---ASVFSGAIVLAGHLLSSNAQAVALPTAESregQIAYVMFTSGSTGLPKGVEI 621
Cdd:PRK12316 4638 ERLAYMMEDSGAALLLTQSHLLQRLpipDGLASLALDRDEDWEGFPAHDPAVRLHPD---NLAYVIYTSGSTGRPKGVAV 4714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 622 GASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFvEQVDAQAITLLDLPTA 701
Cdd:PRK12316 4715 SHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLY-AEIHEHRVTVLVFPPV 4793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 702 FWNEWVVGLKTGtlTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATSCD-LQTQPADVAQLPIG 780
Cdd:PRK12316 4794 YLQQLAEHAERD--GEPPSLRVYCFGGEAVAQASYDLAWRALKPV-YLFNGYGPTETTVTVLLWKaRDGDACGAAYMPIG 4870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 781 LPLAGVNALVL--AAGDRPA-AEGELVLLGPTLAAGYIgtEHTAFTllavGDRHLPA---------YRTGDRVRLEK-GH 847
Cdd:PRK12316 4871 TPLGNRSGYVLdgQLNPLPVgVAGELYLGGEGVARGYL--ERPALT----AERFVPDpfgapggrlYRTGDLARYRAdGV 4944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 848 LLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGvRRLVAFVA--------TKEGEIDARA-LKQRLS 918
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVpqdpaladADEAQAELRDeLKAALR 5023
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 919 SVLPPAMIPTDYRAFHQLPKTGSNKVDRKRlLAEYHDDAPTQALA---SETENRVSAIWQQILGVSGIQSRDNFFELGGQ 995
Cdd:PRK12316 5024 ERLPEYMVPAHLVFLARMPLTPNGKLDRKA-LPQPDASLLQQAYVaprSELEQQVAAIWAEVLQLERVGLDDNFFELGGH 5102
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 499404633 996 SLQTIQIVNRLAAEFSVSIKVSDVFDHPQLSDFCRYLD 1033
Cdd:PRK12316 5103 SLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAA 5140
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
465-949 |
1.24e-115 |
|
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: 365.37 E-value: 1.24e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 465 AKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPR 544
Cdd:cd12117 4 EEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 545 ERQQHIIQIAGLRTIVTQADYQHRLAsVFSGAIVLAGHLLSSNAQAVALPtaeSREGQIAYVMFTSGSTGLPKGVEIGAS 624
Cdd:cd12117 84 ERLAFMLADAGAKVLLTDRSLAGRAG-GLEVAVVIDEALDAGPAGNPAVP---VSPDDLAYVMYTSGSTGRPKGVAVTHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 625 ALDHFtaAARQRYG-LRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFW 703
Cdd:cd12117 160 GVVRL--VKNTNYVtLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 704 NEwVVGLKTGTLtmpSALRAIIIGGEAVYPEQLVQWQRHAPDtLRLINTYGPTETTVVATSCDLQTQPADVAQLPIGLPL 783
Cdd:cd12117 238 NQ-LADEDPECF---AGLRELLTGGEVVSPPHVRRVLAACPG-LRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 784 AGVNALVLAAGDRPA---AEGELVLLGPTLAAGYIG-TEHTA--FTLL--AVGDRhlpAYRTGDRVR-LEKGHLLYLGRM 854
Cdd:cd12117 313 ANTRVYVLDEDGRPVppgVPGELYVGGDGLALGYLNrPALTAerFVADpfGPGER---LYRTGDLARwLPDGRLEFLGRI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 855 DNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVaTKEGEIDARALKQRLSSVLPPAMIPTDYRAFH 934
Cdd:cd12117 390 DDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV-VAEGALDAAELRAFLRERLPAYMVPAAFVVLD 468
|
490
....*....|....*
gi 499404633 935 QLPKTGSNKVDRKRL 949
Cdd:cd12117 469 ELPLTANGKVDRRAL 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1028 |
2.93e-113 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 387.78 E-value: 2.93e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLwLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGehAEQPeIGFVASQLPvp 82
Cdd:PRK12316 1558 PLSPMQQGM-LFHSLYEQEAGDYINQLRVDVQGLDPDRFRAAWQATVDRHEILRSGFLWQDG--LEQP-LQVIHKQVE-- 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 igvLPIVELLPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:PRK12316 1632 ---LPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVrTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRY 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 taltAGQ--SAPVAEFGPFSAVLEeeRQRDASGQTaqardFWLETLNAMPEP-----ASFSEKKAPIAARFLRQscdMPA 234
Cdd:PRK12316 1709 ----AGQpvAAPGGRYRDYIAWLQ--RQDAAASEA-----FWKEQLAALEEPtrlaqAARTEDGQVGYGDHQQL---LDP 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 235 DLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRigSASLMVPSMQM----NIVPLCIQVDEQANFV 310
Cdd:PRK12316 1775 AQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGR--PAELPGIEQQIglfiNTLPVIAAPRPDQSVA 1852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 311 ALAQQVARTKRTLRRHQHYRYEHLRRDLNRvGGEQrLFGpliNIMPFD-HPLNYGSLSSSTLNLSAGPVED-------LT 382
Cdd:PRK12316 1853 DWLQEVQALNLALREHEHTPLYDIQRWAGQ-GGEA-LFD---SLLVFEnYPVAEALKQGAPAGLVFGRVSNheqtnypLT 1927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 383 IEIHFKPdgTPVLDFDANPACYSAEALASLQETLFTLLQRWLAQPQQTSGELlgRWL-REERELAL-ITSREPEPF-VEP 459
Cdd:PRK12316 1928 LAVTLGE--TLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGEL--ALLdAGERQRILaDWDRTPEAYpRGP 2003
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 -VLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL 538
Cdd:PRK12316 2004 gVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL 2083
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 DPEQPRERQQHIIQIAGLRTIVTQADYQHRL---ASVFSGAIVLAGHLLSSNAQAvalPTAESREGQIAYVMFTSGSTGL 615
Cdd:PRK12316 2084 DPNYPAERLAYMLEDSGAALLLTQRHLLERLplpAGVARLPLDRDAEWADYPDTA---PAVQLAGENLAYVIYTSGSTGL 2160
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 616 PKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFvEQVDAQAITL 695
Cdd:PRK12316 2161 PKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLY-DEMERHGVTI 2239
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 696 LDLPTAFWNEWVVGLKTGtlTMPSALRAIIIGGEAVYPEQLVQWQRhAPDTLRLINTYGPTETTVVATSCDLQTQ-PADV 774
Cdd:PRK12316 2240 LDFPPVYLQQLAEHAERD--GRPPAVRVYCFGGEAVPAASLRLAWE-ALRPVYLFNGYGPTEAVVTPLLWKCRPQdPCGA 2316
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 775 AQLPIGLPLAGVNALVLAAGDRPAAE---GELVLLGPTLAAGYIGTEH-TAFTLL-----AVGDRhlpAYRTGDRVRL-E 844
Cdd:PRK12316 2317 AYVPIGRALGNRRAYILDADLNLLAPgmaGELYLGGEGLARGYLNRPGlTAERFVpdpfsASGER---LYRTGDLARYrA 2393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 845 KGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGvRRLVAFVATKEG-EIDARALKQRLSSVLPP 923
Cdd:PRK12316 2394 DGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASG-KQLVAYVVPDDAaEDLLAELRAWLAARLPA 2472
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 924 AMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDAPTQALA--SETENRVSAIWQQILGVSGIQSRDNFFELGGQSLQTIQ 1001
Cdd:PRK12316 2473 YMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVApqEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQ 2552
|
1050 1060
....*....|....*....|....*..
gi 499404633 1002 IVNRLAAEFSVSIKVSDVFDHPQLSDF 1028
Cdd:PRK12316 2553 VVSRVRQDLGLEVPLRILFERPTLAAF 2579
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1022 |
4.54e-113 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 387.01 E-value: 4.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpeigfVASQLPVp 82
Cdd:PRK12316 51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQ-----VPLDRPL- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 igVLPIVELLPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:PRK12316 125 --EVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLrLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAEFgP--FSAVLEEERQRDASGQTAQARDFW----------LETLNAMPEPASFSEKKApiaarflRQS 229
Cdd:PRK12316 203 SAYATGAEPGLPAL-PiqYADYALWQRSWLEAGEQERQLEYWraqlgeehpvLELPTDHPRPAVPSYRGS-------RYE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 230 CDMPADLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANF 309
Cdd:PRK12316 275 FSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 310 VALAQQVARTKRTLRRHQHYRYEHLRRDLNRvggEQRL-FGPLINIMPFDHPLNYGSLSSSTLN-LSAGPVE-------- 379
Cdd:PRK12316 355 ATLLAGVKDTVLGAQAHQDLPFERLVEALKV---ERSLsHSPLFQVMYNHQPLVADIEALDTVAgLEFGQLEwksrttqf 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 380 DLTIEIHFKPDGTPVLDFDANpACYSAEALASLQETLFTLLQRWLAQPQQTSGELlgRWLREERELALITSREPEPFVEP 459
Cdd:PRK12316 432 DLTLDTYEKGGRLHAALTYAT-DLFEARTVERMARHWQNLLRGMVENPQARVDEL--PMLDAEERGQLVEGWNATAAEYP 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 ----VLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVY 535
Cdd:PRK12316 509 lqrgVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 536 VPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLaSVFSGAIVLAGHLLSS--NAQAVALPTAESREGQIAYVMFTSGST 613
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-PLAAGVQVLDLDRPAAwlEGYSEENPGTELNPENLAYVIYTSGST 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 614 GLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAI 693
Cdd:PRK12316 668 GKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGV 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 694 TLLDLPTAFWNEWvvgLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATSCDLQTQPAD 773
Cdd:PRK12316 748 DTLHFVPSMLQAF---LQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQA-GLYNLYGPTEAAIDVTHWTCVEEGGD 823
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 774 vaQLPIGLPLAGVNALVLAAGDRP---AAEGELVLLGPTLAAGYIGteHTAFTllavGDRHLPA--------YRTGDRVR 842
Cdd:PRK12316 824 --SVPIGRPIANLACYILDANLEPvpvGVLGELYLAGRGLARGYHG--RPGLT----AERFVPSpfvagermYRTGDLAR 895
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 843 LEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIvypnGVRRLVAF-VATKEGEIDARALKQRLSSV 920
Cdd:PRK12316 896 YRAdGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYvVLESEGGDWREALKAHLAAS 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 921 LPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDAPTQALASET--ENRVSAIWQQILGVSGIQSRDNFFELGGQSLQ 998
Cdd:PRK12316 972 LPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNalERTLAAIWQDVLGVERVGLDDNFFELGGDSIV 1051
|
1050 1060
....*....|....*....|....
gi 499404633 999 TIQIVNRlAAEFSVSIKVSDVFDH 1022
Cdd:PRK12316 1052 SIQVVSR-ARQAGIQLSPRDLFQH 1074
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
467-949 |
3.15e-112 |
|
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: 355.59 E-value: 3.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 467 QARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRER 546
Cdd:cd17644 9 QVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 547 QQHIIQIAGLRTIVTQadyQHRLAsvfsgaivlaghllssnaqavalptaesregqiaYVMFTSGSTGLPKGVEIGASAL 626
Cdd:cd17644 89 LTYILEDAQISVLLTQ---PENLA----------------------------------YVIYTSGSTGKPKGVMIEHQSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 627 DHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNEW 706
Cdd:cd17644 132 VNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 707 VVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTLRLINTYGPTETTVVATSCDL-QTQPADVAQLPIGLPLAG 785
Cdd:cd17644 212 VLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLtQLTERNITSVPIGRPIAN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 786 VNALVLAAGDRP---AAEGELVLLGPTLAAGYIG-TEHTAFTLLAVGDRHLPA---YRTGDRVR-LEKGHLLYLGRMDNE 857
Cdd:cd17644 292 TQVYILDENLQPvpvGVPGELHIGGVGLARGYLNrPELTAEKFISHPFNSSESerlYKTGDLARyLPDGNIEYLGRIDNQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 858 FKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAF-VATKEGEIDARALKQRLSSVLPPAMIPTDYRAFHQL 936
Cdd:cd17644 372 VKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYiVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEEL 451
|
490
....*....|...
gi 499404633 937 PKTGSNKVDRKRL 949
Cdd:cd17644 452 PLTPNGKIDRRAL 464
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
3-427 |
3.88e-110 |
|
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: 348.59 E-value: 3.88e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEqpeigFVASQLPVP 82
Cdd:cd19533 3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQ-----WIDPYTPVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IgvlPIVELLPAPmtDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:cd19533 78 I---RHIDLSGDP--DPEGAAQQWMQEDLRKPLPLDNDPLFRHALFtLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAEFGPFSAVLEEERQRDASGQTAQARDFWLETLNAMPEPASFSEKKAPIAARFLRQSCDMPADLWQPLS 241
Cdd:cd19533 153 TALLKGRPAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELTRTLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 242 ALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFVALAQQVARTKR 321
Cdd:cd19533 233 EAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 322 TLRRHQHYRYEHLRRDLNRVGGEQRLFGPLINIMPFDHPLNYGSLSSSTLNLSAGPVEDLTIEIH-FKPDGTPVLDFDAN 400
Cdd:cd19533 313 SLLRHQRYRYEDLRRDLGLTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSIFVYdRDDESGLRIDFDAN 392
|
410 420
....*....|....*....|....*..
gi 499404633 401 PACYSAEALASLQETLFTLLQRWLAQP 427
Cdd:cd19533 393 PALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
464-949 |
1.32e-109 |
|
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: 349.70 E-value: 1.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQHIIQIAGLRTIVTQADYQHRLAsvFSGAIVLAGHLLSSNAQAVALPtAESREGQIAYVMFTSGSTGLPKGVEIGA 623
Cdd:cd17655 83 EERIQYILEDSGADILLTQSHLQPPIA--FIGLIDLLDEDTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 624 SALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFW 703
Cdd:cd17655 160 RGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 704 NEwvvgLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTLRLINTYGPTETTVVATSCDLQTQPADVAQLPIGLPL 783
Cdd:cd17655 240 KL----LDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 784 AGVNALVLAAGDRPAAE---GELVLLGPTLAAGYIG-TEHTAFTLL----AVGDRhlpAYRTGDRVR-LEKGHLLYLGRM 854
Cdd:cd17655 316 GNTRIYILDQYGRPQPVgvaGELYIGGEGVARGYLNrPELTAEKFVddpfVPGER---MYRTGDLARwLPDGNIEFLGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 855 DNEFKISGYRIQPGEVEAHLLAQPEVDEACVqgIVYP--NGVRRLVAFVATKEgEIDARALKQRLSSVLPPAMIPTDYRA 932
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVV--IARKdeQGQNYLCAYIVSEK-ELPVAQLREFLARELPDYMIPSYFIK 469
|
490
....*....|....*..
gi 499404633 933 FHQLPKTGSNKVDRKRL 949
Cdd:cd17655 470 LDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
472-949 |
3.91e-109 |
|
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: 347.74 E-value: 3.91e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADYQHRLAsvfsGAIVLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTA 631
Cdd:cd12116 81 EDAEPALVLTDDALPDRLP----AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 AARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNewvvGLK 711
Cdd:cd12116 157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWR----MLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 712 TGTLTMPSALRAiIIGGEAVYPEQLVQWQRHAPdtlRLINTYGPTETTVVATSCDLQtqpADVAQLPIGLPLAGVNALVL 791
Cdd:cd12116 233 DAGWQGRAGLTA-LCGGEALPPDLAARLLSRVG---SLWNLYGPTETTIWSTAARVT---AAAGPIPIGRPLANTQVYVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 792 AAGDRPAAE---GELVLLGPTLAAGYIGTEHTAFTLLaVGDRHLPA----YRTGDRVRLEK-GHLLYLGRMDNEFKISGY 863
Cdd:cd12116 306 DAALRPVPPgvpGELYIGGDGVAQGYLGRPALTAERF-VPDPFAGPgsrlYRTGDLVRRRAdGRLEYLGRADGQVKIRGH 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 864 RIQPGEVEAHLLAQPEVDEACVQgIVYPNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSN 942
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANG 463
|
....*..
gi 499404633 943 KVDRKRL 949
Cdd:cd12116 464 KLDRKAL 470
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-1029 |
3.18e-106 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 366.80 E-value: 3.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpeigfVASQLPVP 82
Cdd:PRK05691 677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQR-----IDAQGEFA 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPIVELLPAPMTDEEQTIRQwarDEISLPLDLLNGLPCRFALLC-GEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:PRK05691 752 LQRIDLSDLPEAEREARAAQIRE---EEARQPFDLEKGPLLRVTLVRlDDEEHQLLVTLHHIVADGWSLNILLDEFSRLY 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAEFG-PFSAVLEEERQRDASGQTAQARDFWLETLN------AMPEPASFSEKKAPIAARFlrqSCDMPA 234
Cdd:PRK05691 829 AAACQGQTAELAPLPlGYADYGAWQRQWLAQGEAARQLAYWKAQLGdeqpvlELATDHPRSARQAHSAARY---SLRVDA 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 235 DLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFVALAQ 314
Cdd:PRK05691 906 SLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLA 985
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 315 QVARTKRTLRRHQHYRYEHLRRDLNRvGGEQRLFgpliNIMpFDHPLNYGSLSSSTLNLSAgpvEDL---------TIEI 385
Cdd:PRK05691 986 QVRQATLGAQAHQDLPFEQLVEALPQ-AREQGLF----QVM-FNHQQRDLSALRRLPGLLA---EELpwhsreakfDLQL 1056
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 386 HFKPD--GTPVLDFDANPACYSAEALASLQETLFTLLQRWLAQPQQTSGELLGRWLREERELALITSREPEPFVEPVLTA 463
Cdd:PRK05691 1057 HSEEDrnGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPEL 1136
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYP 1216
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQHIIQIAGLRTIVTQADYQHRLASVfSGAIVLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIGA 623
Cdd:PRK05691 1217 AERLAYMLADSGVELLLTQSHLLERLPQA-EGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTH 1295
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 624 SALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLD----LP 699
Cdd:PRK05691 1296 AALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHfvppLL 1375
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 700 TAFWNEWVVGLKTgtltmpsALRAIIIGGEAVYPE-------QLVQWQRHapdtlrliNTYGPTETTVVATScdLQTQPA 772
Cdd:PRK05691 1376 QLFIDEPLAAACT-------SLRRLFSGGEALPAElrnrvlqRLPQVQLH--------NRYGPTETAINVTH--WQCQAE 1438
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 773 DVAQLPIGLPLAGVNALVLAAGDRPAAEG---ELVLLGPTLAAGYIGTEH-TA--FTLLAVGDRHLPAYRTGDRVRLE-K 845
Cdd:PRK05691 1439 DGERSPIGRPLGNVLCRVLDAELNLLPPGvagELCIGGAGLARGYLGRPAlTAerFVPDPLGEDGARLYRTGDRARWNaD 1518
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 846 GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSVLPPAM 925
Cdd:PRK05691 1519 GALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYM 1598
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 926 IPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDAPTQALASETENRVSAIWQQILGVSGIQSRDNFFELGGQSLQTIQIVNR 1005
Cdd:PRK05691 1599 VPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSR 1678
|
1050 1060
....*....|....*....|....
gi 499404633 1006 LAAEFSVSIKVSDVFDHPQLSDFC 1029
Cdd:PRK05691 1679 TRQACDVELPLRALFEASELGAFA 1702
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
468-949 |
7.86e-105 |
|
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: 335.37 E-value: 7.86e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQ 547
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 548 QHIIQIAGlrtivtqadyqhrlasvfSGAIVLAGHLLssnaqavalptaesregqiAYVMFTSGSTGLPKGVEIGASALD 627
Cdd:cd05945 81 REILDAAK------------------PALLIADGDDN-------------------AYIIFTSGSTGRPKGVQISHDNLV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 628 HFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITL-LDLPTAfwneW 706
Cdd:cd05945 124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVwVSTPSF----A 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 707 VVGLKTGTLT---MPSaLRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATSCDL-QTQPADVAQLPIGLP 782
Cdd:cd05945 200 AMCLLSPTFTpesLPS-LRHFLFCGEVLPHKTARALQQRFPDA-RIYNTYGPTEATVAVTYIEVtPEVLDGYDRLPIGYA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 783 LAGVNALVLAAGDRP---AAEGELVLLGPTLAAGYIGT-EHTAFTLlaVGDRHLPAYRTGDRVRLE-KGHLLYLGRMDNE 857
Cdd:cd05945 278 KPGAKLVILDEDGRPvppGEKGELVISGPSVSKGYLNNpEKTAAAF--FPDEGQRAYRTGDLVRLEaDGLLFYRGRLDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 858 FKISGYRIQPGEVEAHLLAQPEVDEACVqgIVYPNG--VRRLVAFVATKEGE--IDARALKQRLSSVLPPAMIPTDYRAF 933
Cdd:cd05945 356 VKLNGYRIELEEIEAALRQVPGVKEAVV--VPKYKGekVTELIAFVVPKPGAeaGLTKAIKAELAERLPPYMIPRRFVYL 433
|
490
....*....|....*.
gi 499404633 934 HQLPKTGSNKVDRKRL 949
Cdd:cd05945 434 DELPLNANGKIDRKAL 449
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
464-949 |
4.15e-104 |
|
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: 335.01 E-value: 4.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQHIIQIAGLRTIVTQADYQHRLASvfSGAIVLAGHLLSSNAQAvALPTAESREGQIAYVMFTSGSTGLPKGVEIGA 623
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTADLAARLPA--GGDVALLGDEALAAPPA-TPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 624 SALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDL-PTAF 702
Cdd:cd17646 161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFvPSML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 703 wnewVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRhAPDTlRLINTYGPTETTVVATSCDLqTQPADVAQLPIGLP 782
Cdd:cd17646 241 ----RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLA-LPGA-ELHNLYGPTEAAIDVTHWPV-RGPAETPSVPIGRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 783 LAGVNALVLAAGDRPA---AEGELVLLGPTLAAGYIG-TEHTAFTLLA----VGDRhlpAYRTGDRVR-LEKGHLLYLGR 853
Cdd:cd17646 314 VPNTRLYVLDDALRPVpvgVPGELYLGGVQLARGYLGrPALTAERFVPdpfgPGSR---MYRTGDLARwRPDGALEFLGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 854 MDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFV--ATKEGEIDARALKQRLSSVLPPAMIPTDYR 931
Cdd:cd17646 391 SDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVvpAAGAAGPDTAALRAHLAERLPEYMVPAAFV 470
|
490
....*....|....*...
gi 499404633 932 AFHQLPKTGSNKVDRKRL 949
Cdd:cd17646 471 VLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
460-955 |
7.23e-104 |
|
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: 334.13 E-value: 7.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 VLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLD 539
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 540 PEQPRERQQHIIQIAGLRTIVTqadyqhrlasvfsgaivlaghllssnaqavalptaeSREGQIAYVMFTSGSTGLPKGV 619
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLT------------------------------------SSPSDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 620 EIG----ASALDHFTAAarqrYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATL-VLRTDEMLESIPTFVEQVDaqaIT 694
Cdd:cd05918 125 VIEhralSTSALAHGRA----LGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLcIPSEEDRLNDLAGFINRLR---VT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 695 LLDLPTAFwnewvvglktGTLTMPSA---LRAIIIGGEAVYPEQLVQWQRHApdtlRLINTYGPTETTVVATSCDlQTQP 771
Cdd:cd05918 198 WAFLTPSV----------ARLLDPEDvpsLRTLVLGGEALTQSDVDTWADRV----RLINAYGPAECTIAATVSP-VVPS 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 772 ADVAqlPIGLPLaGVNALVLAAGD--RPA---AEGELVLLGPTLAAGYIG-TEHTA--------FTLLAVGDRHLPAYRT 837
Cdd:cd05918 263 TDPR--NIGRPL-GATCWVVDPDNhdRLVpigAVGELLIEGPILARGYLNdPEKTAaafiedpaWLKQEGSGRGRRLYRT 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 838 GDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYP---NGVRRLVAFVATKEGE------ 907
Cdd:cd05918 340 GDLVRYNPdGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPkdgSSSPQLVAFVVLDGSSsgsgdg 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 908 ------------IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHD 955
Cdd:cd05918 420 dslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
472-949 |
7.42e-104 |
|
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: 332.30 E-value: 7.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADyqhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVEIGASALDHFTA 631
Cdd:cd17652 81 ADARPALLLTTPD-------------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 AARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFwnewVVGLK 711
Cdd:cd17652 124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAA----LAALP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 712 TGTLtmpSALRAIIIGGEAVYPEQLVQWQRHApdtlRLINTYGPTETTVVATSCDLQTqpaDVAQLPIGLPLAGVNALVL 791
Cdd:cd17652 200 PDDL---PDLRTLVVAGEACPAELVDRWAPGR----RMINAYGPTETTVCATMAGPLP---GGGVPPIGRPVPGTRVYVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 792 AAGDRPA---AEGELVLLGPTLAAGYIG-TEHTAFTLLA-----VGDRhlpAYRTGDRVRLEK-GHLLYLGRMDNEFKIS 861
Cdd:cd17652 270 DARLRPVppgVPGELYIAGAGLARGYLNrPGLTAERFVAdpfgaPGSR---MYRTGDLARWRAdGQLEFLGRADDQVKIR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 862 GYRIQPGEVEAHLLAQPEVDEACVqgIVY--PNGVRRLVAFVATKEGEI-DARALKQRLSSVLPPAMIPTDYRAFHQLPK 938
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEAVV--VVRddRPGDKRLVAYVVPAPGAApTAAELRAHLAERLPGYMVPAAFVVLDALPL 424
|
490
....*....|.
gi 499404633 939 TGSNKVDRKRL 949
Cdd:cd17652 425 TPNGKLDRRAL 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-1022 |
3.28e-98 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 342.92 E-value: 3.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpeigfVASQLPVP 82
Cdd:PRK05691 1730 PLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQ-----VAEDSGLR 1804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPIVELLPApmtDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:PRK05691 1805 MDWQDFSALPAD---ARQQRLQQLADSEAHQPFDLERGPLLRACLVkAAEREHYFVLTLHHIVTEGWAMDIFARELGALY 1881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVA----EFGPFSAVleeERQRDASGQTAQARDFW----------LETLNAMPEPASFSEKKApiAARFlr 227
Cdd:PRK05691 1882 EAFLDDRESPLEplpvQYLDYSVW---QRQWLESGERQRQLDYWkaqlgnehplLELPADRPRPPVQSHRGE--LYRF-- 1954
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 228 qscDMPADLWQPLSALCEGNKISwpdLFLAMLATHLKLV---SGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVD 304
Cdd:PRK05691 1955 ---DLSPELAARVRAFNAQRGLT---LFMTMTATLAALLyrySGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLD 2028
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 305 EQANFVALAQQVARTKRTLRRHQHYRYEHLRRDLN--RVGGEQRLFGPLINI-------------MPFDHPLNYGSLSSS 369
Cdd:PRK05691 2029 GQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQppRSAAYNPLFQVMCNVqrwefqqsrqlagMTVEYLVNDARATKF 2108
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 370 tlnlsagpveDLTIEihfkpdgtpVLDFDANPAC---YSAE-----ALASLQETLFTLLQRWLAQPQQTSGELlgRWLRE 441
Cdd:PRK05691 2109 ----------DLNLE---------VTDLDGRLGCcltYSRDlfdepRIARMAEHWQNLLEALLGDPQQRLAEL--PLLAA 2167
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 442 ERELALITSREPEPfVEPVLTA-----IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLN 516
Cdd:PRK05691 2168 AEQQQLLDSLAGEA-GEARLDQtlhglFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALE 2246
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 517 RSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLASVFSGaivLAGHLLSSNAQAVA-LPT 595
Cdd:PRK05691 2247 RSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAG---VARWCLEDDAAALAaYSD 2323
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 596 AE----SREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLV 671
Cdd:PRK05691 2324 APlpflSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVV 2403
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 672 LRTDEM--LESIPTFVEQvdaQAITLLDLPTAFWNEWVVGLKTGTLTMPsaLRAIIIGGEAVYPEQLvQWQRHAPDTLRL 749
Cdd:PRK05691 2404 LRAQGQwgAEEICQLIRE---QQVSILGFTPSYGSQLAQWLAGQGEQLP--VRMCITGGEALTGEHL-QRIRQAFAPQLF 2477
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 750 INTYGPTETTVVATSCDL-QTQPADVAQLPIGLPLAGVNALVLAAGDRP---AAEGELVLLGPTLAAGYigteHTAFTLL 825
Cdd:PRK05691 2478 FNAYGPTETVVMPLACLApEQLEEGAASVPIGRVVGARVAYILDADLALvpqGATGELYVGGAGLAQGY----HDRPGLT 2553
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 826 A---VGDRHLPA----YRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGvRRL 897
Cdd:PRK05691 2554 AerfVADPFAADggrlYRTGDLVRLrADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSG-KQL 2632
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 898 VAFVATKEGEIDA-------RALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL------LAEYHDDAPtqalAS 964
Cdd:PRK05691 2633 AGYLVSAVAGQDDeaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALpapdpeLNRQAYQAP----RS 2708
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404633 965 ETENRVSAIWQQILGVSGIQSRDNFFELGGQSLQTIQIVNRlAAEFSVSIKVSDVFDH 1022
Cdd:PRK05691 2709 ELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQH 2765
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
472-949 |
3.16e-96 |
|
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: 312.32 E-value: 3.16e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADyqhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVEIGASALDHFTA 631
Cdd:cd17643 81 ADSGPSLLLTDPD-------------------------------------DLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 AARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLD-LPTAFWN--EWVV 708
Cdd:cd17643 124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNqTPSAFYQlvEAAD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 709 GLKTGTLtmpsALRAIIIGGEAVYPEQLVQW-QRHAPDTLRLINTYGPTETTVVATSCDLQTQPAD-VAQLPIGLPLAGV 786
Cdd:cd17643 204 RDGRDPL----ALRYVIFGGEALEAAMLRPWaGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPaAAASPIGRPLPGL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 787 NALVLAAGDRPAA---EGELVLLGPTLAAGYIG-TEHTA--FTLLAVGDRHLPAYRTGDRVR-LEKGHLLYLGRMDNEFK 859
Cdd:cd17643 280 RVYVLDADGRPVPpgvVGELYVSGAGVARGYLGrPELTAerFVANPFGGPGSRMYRTGDLARrLPDGELEYLGRADEQVK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 860 ISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTDYRAFHQLPK 938
Cdd:cd17643 360 IRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGaAADIAELRALLKELLPDYMVPARYVPLDALPL 439
|
490
....*....|.
gi 499404633 939 TGSNKVDRKRL 949
Cdd:cd17643 440 TVNGKLDRAAL 450
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
472-949 |
2.31e-95 |
|
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: 311.13 E-value: 2.31e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADYQHRLASVFSGAIVLAGHLLSSNAQAVALPTAesreGQIAYVMFTSGSTGLPKGVEIGASALDHFTA 631
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAP----DDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 AARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLldlptafWN------E 705
Cdd:cd12114 157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTL-------WNsvpallE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 706 WVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDtLRLINTYGPTETTVVATSCDLQTQPADVAQLPIGLPLAG 785
Cdd:cd12114 230 MLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPD-ARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLAN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 786 VNALVLAAGDRPA---AEGELVLLGPTLAAGYIG-TEHTAFTLLAVGDRHLpAYRTGDRVR-LEKGHLLYLGRMDNEFKI 860
Cdd:cd12114 309 QRYRVLDPRGRDCpdwVPGELWIGGRGVALGYLGdPELTAARFVTHPDGER-LYRTGDLGRyRPDGTLEFLGRRDGQVKV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 861 SGYRIQPGEVEAHLLAQPEVDEACVqgIVYPN-GVRRLVAFVATKEG--EIDARALKQRLSSVLPPAMIPTDYRAFHQLP 937
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARAVV--VVLGDpGGKRLAAFVVPDNDgtPIAPDALRAFLAQTLPAYMIPSRVIALEALP 465
|
490
....*....|..
gi 499404633 938 KTGSNKVDRKRL 949
Cdd:cd12114 466 LTANGKVDRAAL 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
464-949 |
1.13e-91 |
|
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: 300.00 E-value: 1.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQHIIQIAGLRTIVTQADyqhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVEIGA 623
Cdd:cd12115 85 PERLRFILEDAQARLVLTDPD-------------------------------------DLAYVIYTSGSTGRPKGVAIEH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 624 SALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEM-LESIPTfveqvdAQAITLLD-LPTA 701
Cdd:cd12115 128 RNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLaLPDLPA------AAEVTLINtVPSA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 702 FwNEWvvgLKTGTLtmPSALRAIIIGGEAVYPEqLVQWQRHAPDTLRLINTYGPTETTVVATSCDLQtqPADVAQLPIGL 781
Cdd:cd12115 202 A-AEL---LRHDAL--PASVRVVNLAGEPLPRD-LVQRLYARLQVERVVNLYGPSEDTTYSTVAPVP--PGASGEVSIGR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 782 PLAGVNALVLAAGDRP---AAEGELVLLGPTLAAGYIG-TEHTAFTLLAvgDRHLPA---YRTGDRVR-LEKGHLLYLGR 853
Cdd:cd12115 273 PLANTQAYVLDRALQPvplGVPGELYIGGAGVARGYLGrPGLTAERFLP--DPFGPGarlYRTGDLVRwRPDGLLEFLGR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 854 MDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPAMIPTDYRA 932
Cdd:cd12115 351 ADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAaGLVEDLRRHLGTRLPAYMVPSRFVR 430
|
490
....*....|....*..
gi 499404633 933 FHQLPKTGSNKVDRKRL 949
Cdd:cd12115 431 LDALPLTPNGKIDRSAL 447
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
460-957 |
8.95e-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: 297.88 E-value: 8.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 VLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLD 539
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 540 PEQPRERQQHIIQIAGLRTIVTqadyqhrlasvfsgaivlaghllssnaqavalptaesregqiAYVMFTSGSTGLPKGV 619
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 620 EIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDAS-IEEVFATLTSGATLVLRTDemlESIPTFVEQVDAQAITLLDL 698
Cdd:COG0318 119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 699 PTAFWNEWVVGLKTGTLTMPSaLRAIIIGGEAVYPEQLVQWQRHApdTLRLINTYGPTETTVVATSCDLQTQPADVAqlP 778
Cdd:COG0318 196 VPTMLARLLRHPEFARYDLSS-LRLVVSGGAPLPPELLERFEERF--GVRIVEGYGLTETSPVVTVNPEDPGERRPG--S 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 779 IGLPLAGVNALVLAAGDRPAA---EGELVLLGPTLAAGYIG-TEHTAFTlLAVGdrhlpAYRTGDRVRL-EKGHLLYLGR 853
Cdd:COG0318 271 VGRPLPGVEVRIVDEDGRELPpgeVGEIVVRGPNVMKGYWNdPEATAEA-FRDG-----WLRTGDLGRLdEDGYLYIVGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 854 MDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTDYRA 932
Cdd:COG0318 345 KKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGaELDAEELRAFLRERLARYKVPRRVEF 424
|
490 500
....*....|....*....|....*
gi 499404633 933 FHQLPKTGSNKVDRKRLLAEYHDDA 957
Cdd:COG0318 425 VDELPRTASGKIDRRALRERYAAGA 449
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
463-949 |
8.00e-84 |
|
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: 278.42 E-value: 8.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQ 542
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQQHIIQIAGLRTIVTqADYQHRLAsvfsgaivlaghllssnaqavalptaesregqiaYVMFTSGSTGLPKGVEIG 622
Cdd:cd17653 82 PSARIQAILRTSGATLLLT-TDSPDDLA----------------------------------YIIFTSGSTGIPKGVMVP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 623 ASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEmlESIPTFVEQVDAQAITlldlPTAf 702
Cdd:cd17653 127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPS--DPFAHVARTVDALMST----PSI- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 703 wnewvvgLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHApdtlRLINTYGPTETTVVATScdLQTQPADvaQLPIGLP 782
Cdd:cd17653 200 -------LSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGR----RLYNAYGPTECTISSTM--TELLPGQ--PVTIGKP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 783 LAGVNALVLAAGDRPAAE---GELVLLGPTLAAGYIGT-EHTAFTLLAV----GDRHlpaYRTGDRVRL-EKGHLLYLGR 853
Cdd:cd17653 265 IPNSTCYILDADLQPVPEgvvGEICISGVQVARGYLGNpALTASKFVPDpfwpGSRM---YRTGDYGRWtEDGGLEFLGR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 854 MDNEFKISGYRIQPGEVEAHLLA-QPEVDEACVQGIvypNGvrRLVAFVATKegEIDARALKQRLSSVLPPAMIPTDYRA 932
Cdd:cd17653 342 EDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIVV---NG--RLVAFVTPE--TVDVDGLRSELAKHLPSYAVPDRIIA 414
|
490
....*....|....*..
gi 499404633 933 FHQLPKTGSNKVDRKRL 949
Cdd:cd17653 415 LDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
466-949 |
2.69e-81 |
|
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: 271.74 E-value: 2.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 466 KQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRE 545
Cdd:cd17645 6 EQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 546 RQQHIIQIAGLRTIVTQADyqhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVEIGASA 625
Cdd:cd17645 86 RIAYMLADSSAKILLTNPD-------------------------------------DLAYVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 626 LDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNE 705
Cdd:cd17645 129 LVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 706 WvvglktgTLTMPSALRAIIIGGEAVypeqlvqwQRHAPDTLRLINTYGPTETTVVATSCDLQTQPADvaqLPIGLPLAG 785
Cdd:cd17645 209 F-------MQLDNQSLRVLLTGGDKL--------KKIERKGYKLVNNYGPTENTVVATSFEIDKPYAN---IPIGKPIDN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 786 VNALVLAAGDR---PAAEGELVLLGPTLAAGYIG-TEHTAFTLlaVGDRHLPA---YRTGDRVR-LEKGHLLYLGRMDNE 857
Cdd:cd17645 271 TRVYILDEALQlqpIGVAGELCIAGEGLARGYLNrPELTAEKF--IVHPFVPGermYRTGDLAKfLPDGNIEFLGRLDQQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 858 FKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEgEIDARALKQRLSSVLPPAMIPTDYRAFHQLP 937
Cdd:cd17645 349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPE-EIPHEELREWLKNDLPDYMIPTYFVHLKALP 427
|
490
....*....|..
gi 499404633 938 KTGSNKVDRKRL 949
Cdd:cd17645 428 LTANGKVDRKAL 439
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
472-949 |
2.75e-76 |
|
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: 259.33 E-value: 2.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADYQHRLAsvFSGAIVLAGHLLSSNAQAVALpTAESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTA 631
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLS--FNKSTILLEDPSISQEDTSNI-DYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 AARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWnEWVVGLK 711
Cdd:cd17656 159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFL-KFIFSER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 712 TGTLTMPSALRAIIIGGEAVYPEQLVQ--WQRHapdTLRLINTYGPTETTVVaTSCDLQTQPADVAQLPIGLPLAGVNAL 789
Cdd:cd17656 238 EFINRFPTCVKHIITAGEQLVITNEFKemLHEH---NVHLHNHYGPSETHVV-TTYTINPEAEIPELPPIGKPISNTWIY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 790 VLAAGDRP---AAEGELVLLGPTLAAGYIGTE---HTAFtllaVGDRHLP---AYRTGDRVR-LEKGHLLYLGRMDNEFK 859
Cdd:cd17656 314 ILDQEQQLqpqGIVGELYISGASVARGYLNRQeltAEKF----FPDPFDPnerMYRTGDLARyLPDGNIEFLGRADHQVK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 860 ISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATkEGEIDARALKQRLSSVLPPAMIPTDYRAFHQLPKT 939
Cdd:cd17656 390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-EQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLT 468
|
490
....*....|
gi 499404633 940 GSNKVDRKRL 949
Cdd:cd17656 469 PNGKVDRKAL 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
472-949 |
3.15e-76 |
|
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: 258.17 E-value: 3.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADyqhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVEIGASALDHFTA 631
Cdd:cd17650 81 EDSGAKLLLTQPE-------------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 AARQRYGLRAED-RVLQFAPFNFDASIEEVFATLTSGATLVLRTDE-----------MLESIPTFVEQVDAQAITLLDLp 699
Cdd:cd17650 124 AWRREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEvkldpaalydlILKSRITLMESTPALIRPVMAY- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 700 tAFWNewvvGLKtgtltmPSALRAIIIGGEAVYPEQLVQWQRHAPDTLRLINTYGPTETTVVATSCDLQTQPA-DVAQLP 778
Cdd:cd17650 203 -VYRN----GLD------LSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLgDSANVP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 779 IGLPLAGVNALVLAAGDRP---AAEGELVLLGPTLAAGYIGT-EHTA--FT--LLAVGDRhlpAYRTGDRVR-LEKGHLL 849
Cdd:cd17650 272 IGRPLPNTAMYVLDERLQPqpvGVAGELYIGGAGVARGYLNRpELTAerFVenPFAPGER---MYRTGDLARwRADGNVE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 850 YLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEgEIDARALKQRLSSVLPPAMIPTD 929
Cdd:cd17650 349 LLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA-TLNTAELRAFLAKELPSYMIPSY 427
|
490 500
....*....|....*....|
gi 499404633 930 YRAFHQLPKTGSNKVDRKRL 949
Cdd:cd17650 428 YVQLDALPLTPNGKVDRRAL 447
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
464-861 |
4.60e-72 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 245.68 E-value: 4.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALA-QRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQ 542
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQQHIIQIAGLRTIVTQADYQ-HRLASVFSGAIVLAGHLLS---------------SNAQAVALPTAESREGQIAYV 606
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKlEELLEALGKLEVVKLVLVLdrdpvlkeeplpeeaKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 607 MFTSGSTGLPKGVEIGASALDHFTAAARQRY----GLRAEDRVLQFAPFNFDASIE-EVFATLTSGATLVLRTDEMLESI 681
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 682 PTFVEQVDAQAITLLDLPTAFWNeWVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTlrLINTYGPTETTVV 761
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLN-MLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA--LVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 762 ATsCDLQTQPADVAQLPIGLPLAGVNALVL-AAGDRPAA---EGELVLLGPTLAAGYIG-TEHTAFTLLAVGdrhlpAYR 836
Cdd:pfam00501 318 VT-TPLPLDEDLRSLGSVGRPLPGTEVKIVdDETGEPVPpgePGELCVRGPGVMKGYLNdPELTAEAFDEDG-----WYR 391
|
410 420
....*....|....*....|....*.
gi 499404633 837 TGDRVR-LEKGHLLYLGRMDNEFKIS 861
Cdd:pfam00501 392 TGDLGRrDEDGYLEIVGRKKDQIKLG 417
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
460-952 |
1.45e-70 |
|
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: 243.90 E-value: 1.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 VLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLD 539
Cdd:TIGR01734 2 LIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 540 PEQPRERQQHIIQIAGLRTIVTQADYQhrLASVFSGAIVLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGV 619
Cdd:TIGR01734 82 TSIPSERIEMIIEAAGPELVIHTAELS--IDAVGTQIITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 620 EIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAItlldlp 699
Cdd:TIGR01734 160 QISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGL------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 700 tafwNEWV-------VGLKTGTLT---MPSALRAIIIGGEavYPEQLVQWQRHAPDTLRLINTYGPTETTVVATSCDLqT 769
Cdd:TIGR01734 234 ----NVWVstpsfvdMCLLDPNFNqenYPHLTHFLFCGEE--LPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKI-T 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 770 QP--ADVAQLPIGLPLAGVNALV-------LAAGDrpaaEGELVLLGPTLAAGYIGT-EHTAFTLLAVGDrhLPAYRTGD 839
Cdd:TIGR01734 307 QEilDQYPRLPIGFAKPDMNLFImdeegepLPEGE----KGEIVIVGPSVSKGYLNNpEKTAEAFFSHEG--QPAYRTGD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 840 RVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNG-VRRLVAFVATKEGEIDA-----RAL 913
Cdd:TIGR01734 381 AGTITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHkVEYLIAAIVPETEDFEKefqltKAI 460
|
490 500 510
....*....|....*....|....*....|....*....
gi 499404633 914 KQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAE 952
Cdd:TIGR01734 461 KKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAEE 499
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
472-949 |
1.49e-69 |
|
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: 239.61 E-value: 1.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERG-VKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHI 550
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 551 IQIAGLRTIVTqadyqhrlasvfsgaivlaghllssnaqavalptaESRegQIAYVMFTSGSTGLPKGVEIGASALDHFT 630
Cdd:cd17648 81 LEDTGARVVIT-----------------------------------NST--DLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 631 AAARQRYGLRAED--RVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLD-LPTAfwnewv 707
Cdd:cd17648 124 TSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSgTPSV------ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 708 vgLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDtlRLINTYGPTETTVVATSCDLQTQPAdvAQLPIGLPLAGVN 787
Cdd:cd17648 198 --LQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNHKRFFPGDQR--FDKSLGRPVRNTK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 788 ALVLAAGDRP---AAEGELVLLGPTLAAGYIGTEhtAFTllavGDRHLP----------------AYRTGDRVR-LEKGH 847
Cdd:cd17648 272 CYVLNDAMKRvpvGAVGELYLGGDGVARGYLNRP--ELT----AERFLPnpfqteqerargrnarLYKTGDLVRwLPSGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 848 LLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACV-----QGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSVLP 922
Cdd:cd17648 346 LEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVvakedASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLP 425
|
490 500
....*....|....*....|....*..
gi 499404633 923 PAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd17648 426 RYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
460-952 |
1.55e-66 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 232.86 E-value: 1.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 VLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERgvKPGERIGIML--NRSPETIISLLAVMQCGAVYVP 537
Cdd:PRK04813 4 IIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 538 LDPEQPRERQQHIIQIAGLRTIVTQADYQHRLASVfsgAIVLAGHLLSSNAQAVALPTAESREG-QIAYVMFTSGSTGLP 616
Cdd:PRK04813 82 VDVSSPAERIEMIIEVAKPSLIIATEELPLEILGI---PVITLDELKDIFATGNPYDFDHAVKGdDNYYIIFTSGTTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 617 KGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLE----------------- 679
Cdd:PRK04813 159 KGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTAnfkqlfetlpqlpinvw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 680 -SIPTFVEqvdaqaITLLDlPTaFWNEwvvglktgtlTMPSaLRAIIIGGEAVyP----EQLVQwqRHaPDTlRLINTYG 754
Cdd:PRK04813 239 vSTPSFAD------MCLLD-PS-FNEE----------HLPN-LTHFLFCGEEL-PhktaKKLLE--RF-PSA-TIYNTYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 755 PTETTVVATScdLQTQPADVAQ---LPIGLPLAGVNALVL-AAGDRPAA--EGELVLLGPTLAAGYIG----TEHTAFTl 824
Cdd:PRK04813 295 PTEATVAVTS--IEITDEMLDQykrLPIGYAKPDSPLLIIdEEGTKLPDgeQGEIVISGPSVSKGYLNnpekTAEAFFT- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 825 lavgDRHLPAYRTGDRVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIvYPNG-VRRLVAFVAT 903
Cdd:PRK04813 372 ----FDGQPAYHTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPY-NKDHkVQYLIAYVVP 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 499404633 904 KEGEIDA-----RALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAE 952
Cdd:PRK04813 447 KEEDFERefeltKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEE 500
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
602-945 |
5.36e-62 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 214.46 E-value: 5.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 602 QIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDemlESI 681
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 682 PTFVEQVDAQAITLLDLPTAFWNEWVVGLKTGTLTMPSaLRAIIIGGEAVYPEQLVQWQRHAPdtLRLINTYGPTETTVV 761
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSS-LRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 762 ATSCDlqtqPADVAQLP--IGLPLAGVNALVLAAGDRPAA---EGELVLLGPTLAAGYIGTEHTAFTLLAVGdrhlpAYR 836
Cdd:cd04433 155 VATGP----PDDDARKPgsVGRPVPGVEVRIVDPDGGELPpgeIGELVVRGPSVMKGYWNNPEATAAVDEDG-----WYR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 837 TGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALK 914
Cdd:cd04433 226 TGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEELR 305
|
330 340 350
....*....|....*....|....*....|.
gi 499404633 915 QRLSSVLPPAMIPTDYRAFHQLPKTGSNKVD 945
Cdd:cd04433 306 AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
95-1005 |
3.70e-60 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 226.59 E-value: 3.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 95 PMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIYTALTAGQSA--P 171
Cdd:PRK05691 3344 PEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIrVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAqlP 3423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 172 VAEfgpfsavleeeRQRDASG-----QTAQARDFWLETLNAMpepasfsEKKAPIAAR--FLRQ----SCDMP-ADLWQP 239
Cdd:PRK05691 3424 VPP-----------RYRDYIGwlqrqDLAQARQWWQDNLRGF-------ERPTPIPSDrpFLREhagdSGGMVvGDCYTR 3485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 240 LSA--------LCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRigsaSLMVPSMQ------MNIVPLCIQVDE 305
Cdd:PRK05691 3486 LDAadgarlreLAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGR----PVSMPQMQrtvglfINSIALRVQLPA 3561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 306 QANFVALAQQVartKRTLRRHQHYR-YEHLrrdlnrvggeqrlfgPLINI-----MPFDHPLnygslSSSTLNLSAGPVE 379
Cdd:PRK05691 3562 AGQRCSVRQWL---QGLLDSNMELReYEYL---------------PLVAIqecseLPKGQPL-----FDSLFVFENAPVE 3618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 380 ----DLTIEIHFKPD-GTPVLDFDANPACYSAEALA---SLQETLF--TLLQRWLAQPQQTSGELLGRWLREERELALIT 449
Cdd:PRK05691 3619 vsvlDRAQSLNASSDsGRTHTNFPLTAVCYPGDDLGlhlSYDQRYFdaPTVERLLGEFKRLLLALVQGFHGDLSELPLLG 3698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 450 SREPE-------------PFVEPVLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLN 516
Cdd:PRK05691 3699 EQERDflldgcnrserdyPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAE 3778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 517 RSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIV---TQADYQHRLASVFSGAI---VLAGHLLSSNAQA 590
Cdd:PRK05691 3779 RGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVcsaACREQARALLDELGCANrprLLVWEEVQAGEVA 3858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 591 VALPTAESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATL 670
Cdd:PRK05691 3859 SHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARV 3938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 671 VLRTDEMLESIPTFVEQVDAQAITLLdlptafwnEWVVGLKTGTLTMP----SALRAIIIGGEAVYPEQLVQWQRHAPDt 746
Cdd:PRK05691 3939 EIVPNAIAHDPQGLLAHVQAQGITVL--------ESVPSLIQGMLAEDrqalDGLRWMLPTGEAMPPELARQWLQRYPQ- 4009
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 747 LRLINTYGPTETtvvatSCDLQTQPADVAQ-----LPIGLPLAGvNALVLAAGDRP----AAEGELVLLGPTLAAGYIGT 817
Cdd:PRK05691 4010 IGLVNAYGPAEC-----SDDVAFFRVDLAStrgsyLPIGSPTDN-NRLYLLDEALElvplGAVGELCVAGTGVGRGYVGD 4083
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 818 -EHTAFTLL-----AVGDRhlpAYRTGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVY 890
Cdd:PRK05691 4084 pLRTALAFVphpfgAPGER---LYRTGDLARRRSdGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEG 4160
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 891 PNGvRRLVAFVATKEGEIDARAL----KQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLA----EYHDDApTQAL 962
Cdd:PRK05691 4161 VNG-KHLVGYLVPHQTVLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPAldigQLQSQA-YLAP 4238
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 499404633 963 ASETENRVSAIWQQILGVSGIQSRDNFFELGGQSLQTIQIVNR 1005
Cdd:PRK05691 4239 RNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASR 4281
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
463-963 |
1.65e-53 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 196.87 E-value: 1.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIAL-----AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVP 537
Cdd:COG0365 14 CLDRHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 538 ----LDPEQPRERqqhiIQIAGLRTIVTQADYQHR-----LASVFSGAIVLAGHL-----LSSNAQAVALPT----AESR 599
Cdd:COG0365 94 vfpgFGAEALADR----IEDAEAKVLITADGGLRGgkvidLKEKVDEALEELPSLehvivVGRTGADVPMEGdldwDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 600 EGQ-------------IAYVMFTSGSTGLPKGVEIGASA-LDHFTAAARQRYGLRAEDRVLQFAPFNF---DASIeeVFA 662
Cdd:COG0365 170 AAAsaefepeptdaddPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWatgHSYI--VYG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 663 TLTSGATLVlrtdeMLESIPTFV------EQVDAQAITLLDL-PTAFW---NEWVVGLKTGTLtmpSALRAIIIGGEAVY 732
Cdd:COG0365 248 PLLNGATVV-----LYEGRPDFPdpgrlwELIEKYGVTVFFTaPTAIRalmKAGDEPLKKYDL---SSLRLLGSAGEPLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 733 PEQLVQWQRH--APdtlrLINTYGPTETTVVATSCdlqtqPADVAQLP--IGLPLAGVNALVL-AAGD--RPAAEGELVL 805
Cdd:COG0365 320 PEVWEWWYEAvgVP----IVDGWGQTETGGIFISN-----LPGLPVKPgsMGKPVPGYDVAVVdEDGNpvPPGEEGELVI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 806 LG--PTLAAGYIG-TEHTAFTLLavgDRHLPAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVD 881
Cdd:COG0365 391 KGpwPGMFRGYWNdPERYRETYF---GRFPGWYRTGDGARRdEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 882 EACVqgIVYPNGVR--RLVAFVATKEGEID----ARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHD 955
Cdd:COG0365 468 EAAV--VGVPDEIRgqVVKAFVVLKPGVEPsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
570
....*....|
gi 499404633 956 DAP--TQALA 963
Cdd:COG0365 546 RPLgdTSTLE 555
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
491-950 |
3.40e-52 |
|
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: 190.34 E-value: 3.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 491 GLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVM----QCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQ 566
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAyaggRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 567 HRLASVFS-----GAIVLAGHLLSSNAQAVALPTAESregQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRA 641
Cdd:cd05922 81 DRLRDALPaspdpGTVLDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 642 EDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESipTFVEQVDAQAITLLD-LPTAFwnEWVVGLKTGTLTMPSa 720
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDD--AFWEDLREHGATGLAgVPSTY--AMLTRLGFDPAKLPS- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 721 LRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATscdlqTQPAD-VAQLP--IGLPLAGVNALVLAAGDRP 797
Cdd:cd05922 233 LRYLTQAGGRLPQETIARLRELLPGA-QVYVMYGQTEATRRMT-----YLPPErILEKPgsIGLAIPGGEFEILDDDGTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 798 AAEGELVLL---GPTLAAGYIGTEhtafTLLAVGDRHLPAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAH 873
Cdd:cd05922 307 TPPGEPGEIvhrGPNVMKGYWNDP----PYRRKEGRGGGVLHTGDLARRdEDGFLFIVGRRDRMIKLFGNRISPTEIEAA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404633 874 LLAQPEVDEACVQGIVYPNGvRRLVAFVATKEgEIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLL 950
Cdd:cd05922 383 ARSIGLIIEAAAVGLPDPLG-EKLALFVTAPD-KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
465-949 |
4.66e-51 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 187.39 E-value: 4.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 465 AKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPR 544
Cdd:cd05936 6 EEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 545 ERQQHIIQIAGLRTIVTQADYQHRLAsvfsgaivlaghllssnAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIGAS 624
Cdd:cd05936 86 RELEHILNDSGAKALIVAVSFTDLLA-----------------AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 625 ALDHFTAAARQRYG--LRAEDRVLQFAP----FNFDASieeVFATLTSGATLVLrtdemlesIPTF-----VEQVDAQAI 693
Cdd:cd05936 149 NLVANALQIKAWLEdlLEGDDVVLAALPlfhvFGLTVA---LLLPLALGATIVL--------IPRFrpigvLKEIRKHRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 694 TLL-DLPTAFWNewVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDtlRLINTYGPTETTVVATSCdlqtqPA 772
Cdd:cd05936 218 TIFpGVPTMYIA--LLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGV--PIVEGYGLTETSPVVAVN-----PL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 773 DVAQLP--IGLPLAGVNALVLAAGDRPAA---EGELVLLGPTLAAGYIGT-EHTAFTLlaVGDRhlpaYRTGDRVRL-EK 845
Cdd:cd05936 289 DGPRKPgsIGIPLPGTEVKIVDDDGEELPpgeVGELWVRGPQVMKGYWNRpEETAEAF--VDGW----LRTGDIGYMdED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 846 GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPA 924
Cdd:cd05936 363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGAsLTEEEIIAFCREQLAGY 442
|
490 500
....*....|....*....|....*
gi 499404633 925 MIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd05936 443 KVPRQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
484-949 |
5.63e-51 |
|
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: 186.52 E-value: 5.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVtQA 563
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL-QN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 DYQHRLASVFSgaivlaghllsSNAQAVALPTAESregqIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAED 643
Cdd:cd17654 96 KELDNAPLSFT-----------PEHRHFNIRTDEC----LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 644 rVLQFAPFN-FDASIEEVFATLTSGATLVLRTDEMlESIPTFVEQVDAQA--ITLLDL-PTAFWNEWVVGLKTGTLTMPS 719
Cdd:cd17654 161 -ILFLTSPLtFDPSVVEIFLSLSSGATLLIVPTSV-KVLPSKLADILFKRhrITVLQAtPTLFRRFGSQSIKSTVLSATS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 720 ALRAIIIGGEAVYPEQLVQWQRHAPDTLRLINTYGPTETTVVATscdLQTQPADVAQLPIGLPLAGvnaLVLAAGDRPAA 799
Cdd:cd17654 239 SLRVLALGGEPFPSLVILSSWRGKGNRTRIFNIYGITEVSCWAL---AYKVPEEDSPVQLGSPLLG---TVIEVRDQNGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 800 EGELVLLGPTLAAGYI--GTEHTAFTLLavgdrhlpaYRTGDRVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQ 877
Cdd:cd17654 313 EGTGQVFLGGLNRVCIldDEVTVPKGTM---------RATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404633 878 PEVDEACVqgiVYPNGvRRLVAFVATKegEIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd17654 384 LGVESCAV---TLSDQ-QRLIAFIVGE--SSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
3-449 |
2.01e-46 |
|
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: 173.29 E-value: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpeigFVASQLPVP 82
Cdd:pfam00668 6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQ----VILEERPFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPIVELlpaPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:pfam00668 82 LEIIDISDL---SESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFrIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAEFGPFSAVLEEERQRDASGQTAQARDFWLETLNAMPEPASFSEKKAPIAARFL---RQSCDMPADLWQ 238
Cdd:pfam00668 159 QQLLKGEPLPLPPKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFkgdRLSFTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 239 PLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFVALAQQVAR 318
Cdd:pfam00668 239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 319 TKRTLRRHQHYRYEHLRRDLNRVGGEQR--LFGPLINIMPFD--------HPLNYGSLSSSTLNLSAGPVeDLTIEIhFK 388
Cdd:pfam00668 319 DLLSAEPHQGYPFGDLVNDLRLPRDLSRhpLFDPMFSFQNYLgqdsqeeeFQLSELDLSVSSVIEEEAKY-DLSLTA-SE 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404633 389 PDGTPVLDFDANPACYSAEALASLQETLFTLLQRWLAQPQQTSGELlgrWLREERELALIT 449
Cdd:pfam00668 397 RGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSEL---DLLSDAEKQKLL 454
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
484-949 |
4.85e-44 |
|
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: 165.59 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVP----LDPEQPRERqqhiIQIAGLRTI 559
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPlttlLGPKDIEYR----LEAAGAKAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 560 VTQADyqhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGL 639
Cdd:cd05972 77 VTDAE-------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 640 RAEDRVLQFA-PFNFDASIEEVFATLTSGATLVLrtDEMLESIPT-FVEQVDAQAITLLDLPTAFWNEWV-VGLKTGTlt 716
Cdd:cd05972 120 RPDDIHWNIAdPGWAKGAWSSFFGPWLLGATVFV--YEGPRFDAErILELLERYGVTSFCGPPTAYRMLIkQDLSSYK-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 717 mPSALRAIIIGGEAVYPEQLVQWQRHAPDTLRliNTYGPTETT-VVATSCDLQTQPADvaqlpIGLPLAGVNALVL-AAG 794
Cdd:cd05972 196 -FSHLRLVVSAGEPLNPEVIEWWRAATGLPIR--DGYGQTETGlTVGNFPDMPVKPGS-----MGRPTPGYDVAIIdDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 795 D--RPAAEGELVLLGPT--LAAGYIGT-EHTAFTLlaVGDrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPG 868
Cdd:cd05972 268 RelPPGEEGDIAIKLPPpgLFLGYVGDpEKTEASI--RGD----YYLTGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 869 EVEAHLLAQPEVDEACVQGIvyPNGVRRLV--AFVATKEGEIDARALKQRL----SSVLPPAMIPTDYRAFHQLPKTGSN 942
Cdd:cd05972 342 EVESALLEHPAVAEAAVVGS--PDPVRGEVvkAFVVLTSGYEPSEELAEELqghvKKVLAPYKYPREIEFVEELPKTISG 419
|
....*..
gi 499404633 943 KVDRKRL 949
Cdd:cd05972 420 KIRRVEL 426
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
481-949 |
5.80e-44 |
|
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: 165.54 E-value: 5.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIV 560
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 561 TQadyqhrlasvfsgaivlaghllssnaqavalptaesregqIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLR 640
Cdd:cd05934 81 VD----------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 641 AEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRtdemlesiPTFVeqvdaqaitlldlPTAFWNEwvvGLKTG-TLT-- 716
Cdd:cd05934 121 EDDVYLTVLPlFHINAQAVSVLAALSVGATLVLL--------PRFS-------------ASRFWSD---VRRYGaTVTny 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 717 ---MPSALRA-----------IIIGGEAVYPEQLvqwqrHAPDT----LRLINTYGPTETTVVATScdlqTQPADVAQLP 778
Cdd:cd05934 177 lgaMLSYLLAqppspddrahrLRAAYGAPNPPEL-----HEEFEerfgVRLLEGYGMTETIVGVIG----PRDEPRRPGS 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 779 IGLPLAGVNALVLAAGDRPAAE---GELVL---LGPTLAAGYIG-TEHTAFTLlavgdRHLpAYRTGDRV-RLEKGHLLY 850
Cdd:cd05934 248 IGRPAPGYEVRIVDDDGQELPAgepGELVIrglRGWGFFKGYYNmPEATAEAM-----RNG-WFHTGDLGyRDADGFFYF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 851 LGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPAMIPTD 929
Cdd:cd05934 322 VDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGEtLDPEELFAFCEGQLAYFKVPRY 401
|
490 500
....*....|....*....|
gi 499404633 930 YRAFHQLPKTGSNKVDRKRL 949
Cdd:cd05934 402 IRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
467-957 |
9.77e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 167.29 E-value: 9.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 467 QARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVP----LDPEQ 542
Cdd:PRK06187 15 GARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPinirLKPEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 ---------------PRERQQHIIQIAG----LRTIVTQADYQHRLASVFSGAIVlagHLLSsnAQAVALPTAESREGQI 603
Cdd:PRK06187 95 iayilndaedrvvlvDSEFVPLLAAILPqlptVRTVIVEGDGPAAPLAPEVGEYE---ELLA--AASDTFDFPDIDENDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 604 AYVMFTSGSTGLPKGVEIG-ASALDHfTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVlrtdeMLESIP 682
Cdd:PRK06187 170 AAMLYTSGTTGHPKGVVLShRNLFLH-SLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQV-----IPRRFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 683 --TFVEQVDAQAITLLDL-PTAfWNewvvglktGTLTMP-------SALRAIIIGGEAVyPEQLVqwqRHAPDTL--RLI 750
Cdd:PRK06187 244 peNLLDLIETERVTFFFAvPTI-WQ--------MLLKAPrayfvdfSSLRLVIYGGAAL-PPALL---REFKEKFgiDLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 751 NTYGPTETTVVATScdLQTQPADVAQLPI----GLPLAGVNA-LVLAAGDR-PAAE---GELVLLGPTLAAGYIGT-EHT 820
Cdd:PRK06187 311 QGYGMTETSPVVSV--LPPEDQLPGQWTKrrsaGRPLPGVEArIVDDDGDElPPDGgevGEIIVRGPWLMQGYWNRpEAT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 821 AFTLlaVGDrhlpAYRTGDRVRLEKGHLLYL-GRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVA 899
Cdd:PRK06187 389 AETI--DGG----WLHTGDVGYIDEDGYLYItDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVA 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499404633 900 FVATKEGE-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDA 957
Cdd:PRK06187 463 VVVLKPGAtLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
468-946 |
2.28e-43 |
|
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: 163.94 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQ 547
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 548 QHIIQiaglrtivtqaDyqhrlasvfSGAIVLAGhllssnaqavalptaesregQIAYVMFTSGSTGLPKGV-----EIG 622
Cdd:cd17631 85 AYILA-----------D---------SGAKVLFD--------------------DLALLMYTSGTTGRPKGAmlthrNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 623 ASALDHFTAaarqrYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVL----RTDEMLESI----PTFVEQVDAQAI 693
Cdd:cd17631 125 WNAVNALAA-----LDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVIlrkfDPETVLDLIerhrVTSFFLVPTMIQ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 694 TLLDLPTAfwnewvvglktgTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPdtlRLINTYGPTETTVVATSCDlqtqPAD 773
Cdd:cd17631 200 ALLQHPRF------------ATTDLSSLRAVIYGGAPMPERLLRALQARGV---KFVQGYGMTETSPGVTFLS----PED 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 774 VAQLP--IGLPLAGVNALVLAAGDRPAAE---GELVLLGPTLAAGYIGTEHTAFTLLAVGdrhlpAYRTGDRVRL-EKGH 847
Cdd:cd17631 261 HRRKLgsAGRPVFFVEVRIVDPDGREVPPgevGEIVVRGPHVMAGYWNRPEATAAAFRDG-----WFHTGDLGRLdEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 848 LLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMI 926
Cdd:cd17631 336 LYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGaELDEDELIAHCRERLARYKI 415
|
490 500
....*....|....*....|
gi 499404633 927 PTDYRAFHQLPKTGSNKVDR 946
Cdd:cd17631 416 PKSVEFVDALPRNATGKILK 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
475-950 |
5.14e-42 |
|
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: 161.77 E-value: 5.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 475 IALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIA 554
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 555 GLRTIVTQADYQHRLASVFSGAIVLAGHLLSSN----------------AQAVALPTAESREGQIAYVMFTSGSTGLPKG 618
Cdd:cd05959 101 RARVVVVSGELAPVLAAALTKSEHTLVVLIVSGgagpeagalllaelvaAEAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 619 -VEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASI-EEVFATLTSGATLVL-----RTDEMLESI----PTFVEQ 687
Cdd:cd05959 181 vVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLgNSLTFPLSVGATTVLmperpTPAAVFKRIrryrPTVFFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 688 VDAQAITLLDLPTAfwnewvvglktgTLTMPSALRAIIIGGEAVyPEQLVQ-WQRHApdTLRLINTYGPTEttvvATSCD 766
Cdd:cd05959 261 VPTLYAAMLAAPNL------------PSRDLSSLRLCVSAGEAL-PAEVGErWKARF--GLDILDGIGSTE----MLHIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 767 LQTQPADVAQLPIGLPLAGVN-ALVLAAG-DRPAAE-GELVLLGPTLAAGYIGT-EHTAFTLLAvgdrhlPAYRTGDR-V 841
Cdd:cd05959 322 LSNRPGRVRYGTTGKPVPGYEvELRDEDGgDVADGEpGELYVRGPSSATMYWNNrDKTRDTFQG------EWTRTGDKyV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 842 RLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG----EIDARALKQRL 917
Cdd:cd05959 396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedsEALEEELKEFV 475
|
490 500 510
....*....|....*....|....*....|...
gi 499404633 918 SSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLL 950
Cdd:cd05959 476 KDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
463-949 |
1.74e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 157.37 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQ 542
Cdd:PRK07656 10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQQHIIQIAGLRTIVTQADY-------QHRLASV------FSGAIVLAGHLLSSNAQAVALPTAESREGQ-----IA 604
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLFlgvdysaTTRLPALehvvicETEEDDPHTEKMKTFTDFLAAGDPAERAPEvdpddVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 605 YVMFTSGSTGLPKGVEIG-ASALDHFTAAARqRYGLRAEDRVLQFAPF--NF--DASIeevFATLTSGATLVLrtdemle 679
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLThRQLLSNAADWAE-YLGLTEGDRYLAANPFfhVFgyKAGV---NAPLMRGATILP------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 680 sIPTF-----VEQVDAQAITLLDLPTAFWNEW--VVGLKTGTLtmpSALRAIIIGGeAVYPEQLVQWQRHAPDTLRLINT 752
Cdd:PRK07656 239 -LPVFdpdevFRLIETERITVLPGPPTMYNSLlqHPDRSAEDL---SSLRLAVTGA-ASMPVALLERFESELGVDIVLTG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 753 YGPTETTVVATSCDLQTQPADVAQlPIGLPLAGV-NALVLAAGDR-PAAE-GELVLLGPTLAAGYIG-TEHTAFTLLAVG 828
Cdd:PRK07656 314 YGLSEASGVTTFNRLDDDRKTVAG-TIGTAIAGVeNKIVNELGEEvPVGEvGELLVRGPNVMKGYYDdPEATAAAIDADG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 829 DRHlpayrTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG- 906
Cdd:PRK07656 393 WLH-----TGDLGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGa 467
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 499404633 907 EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK07656 468 ELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
478-944 |
4.32e-40 |
|
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: 155.45 E-value: 4.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 478 AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLR 557
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 558 TIVTQADYQHRLASVFSGA------IVLAGH----------LLSSNAQAVALPTAESREG--QIAYVMFTSGSTGLPKGV 619
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELgpkdkiIVLDDKpdgvlsiedlLSPTLGEEDEDLPPPLKDGkdDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 620 EIGASAL--DHFTAAARQRYGLRAEDRVLQFAPFNFdasIEEVFATLTS---GATLVL----RTDEMLESIP----TFVE 686
Cdd:cd05911 165 CLSHRNLiaNLSQVQTFLYGNDGSNDVILGFLPLYH---IYGLFTTLASllnGATVIImpkfDSELFLDLIEkykiTFLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 687 QVDAQAITLLDLPTafwnewvvgLKTGTLtmpSALRAIIIGGEAVYPEQLVQWQRHAPDTlRLINTYGPTETTVVATscd 766
Cdd:cd05911 242 LVPPIAAALAKSPL---------LDKYDL---SSLRVILSGGAPLSKELQELLAKRFPNA-TIKQGYGMTETGGILT--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 767 lQTQPADVAQLPIGLPLAGVNALVLAAGDRPAA----EGELVLLGPTLAAGYIG-TEHTAFTLLAVGdrhlpAYRTGDRV 841
Cdd:cd05911 306 -VNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLgpnePGEICVRGPQVMKGYYNnPEATKETFDEDG-----WLHTGDIG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 842 RLEKGHLLYL-GRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSS 919
Cdd:cd05911 380 YFDEDGYLYIvDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEkLTEKEVKDYVAK 459
|
490 500 510
....*....|....*....|....*....|..
gi 499404633 920 VLPpamiptDYRAFH-------QLPKTGSNKV 944
Cdd:cd05911 460 KVA------SYKQLRggvvfvdEIPKSASGKI 485
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
484-946 |
9.87e-40 |
|
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: 153.44 E-value: 9.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQA 563
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 DYQHRLASvfsGAIVLaghllssnaqavalptaesregqiayvMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAED 643
Cdd:cd05973 81 ANRHKLDS---DPFVM---------------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 644 RVLQFAPFNFDASI-EEVFATLTSG-ATLVLrtdEMLESIPTFVEQVDAQAIT-LLDLPTAFwnewvVGLKTGTLTMPSA 720
Cdd:cd05973 131 SFWNAADPGWAYGLyYAITGPLALGhPTILL---EGGFSVESTWRVIERLGVTnLAGSPTAY-----RLLMAAGAEVPAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 721 ----LRAIIIGGEAVYPEqLVQWQRHAPDTLrLINTYGPTETTVVATSCDLQTQPadVAQLPIGLPLAGVNALVLAAGDR 796
Cdd:cd05973 203 pkgrLRRVSSAGEPLTPE-VIRWFDAALGVP-IHDHYGQTELGMVLANHHALEHP--VHAGSAGRAMPGWRVAVLDDDGD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 797 PAAEGELVLLGPTLAA-------GYIGTEHTAFtllaVGDRhlpaYRTGDRVRLE-KGHLLYLGRMDNEFKISGYRIQPG 868
Cdd:cd05973 279 ELGPGEPGRLAIDIANsplmwfrGYQLPDTPAI----DGGY----YLTGDTVEFDpDGSFSFIGRADDVITMSGYRIGPF 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 869 EVEAHLLAQPEVDEACVQGIvyPNGVRRLV--AFVATKEGEIDARAL--------KQRLSSVLPPamiptdyRAFH---Q 935
Cdd:cd05973 351 DVESALIEHPAVAEAAVIGV--PDPERTEVvkAFVVLRGGHEGTPALadelqlhvKKRLSAHAYP-------RTIHfvdE 421
|
490
....*....|.
gi 499404633 936 LPKTGSNKVDR 946
Cdd:cd05973 422 LPKTPSGKIQR 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
484-951 |
7.87e-39 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 150.73 E-value: 7.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL----DPEQPRERQQHiiqiaglrti 559
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDRLEN---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 560 vtqadyqhrlasvfSGAIVLaghllssnaqaVALPT-AESREGQ-IAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRY 637
Cdd:cd05969 71 --------------SEAKVL-----------ITTEElYERTDPEdPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 638 GLRAEDRVLQFA-PFNFDASIEEVFATLTSGATLVLRTDEMleSIPTFVEQVDAQAITLL-DLPTAFWNEWVVGLKTGTL 715
Cdd:cd05969 126 DLHPDDIYWCTAdPGWVTGTVYGIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWyTAPTAIRMLMKEGDELARK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 716 TMPSALRAIIIGGEAVYPEqLVQWQRHAPDtLRLINTYGPTETTVVATsCDLQTQPADVAQLpiGLPLAGVNALVL---A 792
Cdd:cd05969 204 YDLSSLRFIHSVGEPLNPE-AIRWGMEVFG-VPIHDTWWQTETGSIMI-ANYPCMPIKPGSM--GKPLPGVKAAVVdenG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 793 AGDRPAAEGELVLLG--PTLAAGYIGTEHTAFTLLAVGdrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGE 869
Cdd:cd05969 279 NELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDG-----WYLTGDLAYRdEDGYFWFVGRADDIIKTSGHRVGPFE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 870 VEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSV----LPPAMIPTDYRAFHQLPKTGSNKVD 945
Cdd:cd05969 354 VESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFvrqkLGAHVAPREIEFVDNLPKTRSGKIM 433
|
....*.
gi 499404633 946 RKRLLA 951
Cdd:cd05969 434 RRVLKA 439
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1-427 |
1.63e-38 |
|
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: 149.48 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 1 MKPLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEhAEQPEIGFVASQLP 80
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGR-YEQVVLDKTVRFRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 81 VPIGVlpivellpAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQ 159
Cdd:cd19066 80 EIIDL--------RNLADPEARLLELIDQIQQTIYDLERGPLVRVALFrLADERDVLVVAIHHIIVDGGSFQILFEDISS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 160 IYTALTAGQSAPVAEFGPFSAVLEEERQRDASGQTAQARDFWLETLNAMPEPASFS---EKKAPIAARFLRQSCDMPADL 236
Cdd:cd19066 152 VYDAAERQKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPkakRPSQVASYEVLTLEFFLRSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 237 WQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFVALAQQV 316
Cdd:cd19066 232 TKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 317 ARTKRTLRRHQHYRYEHLRRDLNRVGGEQR--LFGPLINIMPFDHPLNY---GSLSSSTLNLSAGPVEDLTIEIHFKPDG 391
Cdd:cd19066 312 KEQSREAIEHQRVPFIELVRHLGVVPEAPKhpLFEPVFTFKNNQQQLGKtggFIFTTPVYTSSEGTVFDLDLEASEDPDG 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 499404633 392 TPVLDFDANPACYSAEALASLQETLFTLLQRWLAQP 427
Cdd:cd19066 392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
475-951 |
1.05e-36 |
|
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: 144.35 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 475 IALAQRDRQYSYQQLLGLSGQAAAALHERG-VKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIqi 553
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 554 aglrtivTQADyqhrlasvfsGAIVLAGhllssnaqavalptaesregqiAYVMFTSGSTGLPKGVEIGASALDHFTAAA 633
Cdd:cd05941 81 -------TDSE----------PSLVLDP----------------------ALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 634 RQRYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRTdemlESIPTFVEQVDAQ-AITLL-DLPT------AFWN 704
Cdd:cd05941 122 VDAWRWTEDDVLLHVLPlHHVHGLVNALLCPLFAGASVEFLP----KFDPKEVAISRLMpSITVFmGVPTiytrllQYYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 705 EWVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQR---HapdtlRLINTYGPTETtVVATSCdlqtqPADVAQLP--I 779
Cdd:cd05941 198 AHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAitgH-----TLLERYGMTEI-GMALSN-----PLDGERRPgtV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 780 GLPLAGVNALVLAAGDRPAA----EGELVLLGPTLAAGYIGT-EHT--AFTllavGDRHlpaYRTGDRVRLEK-GHLLYL 851
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLprgeVGEIQVRGPSVFKEYWNKpEATkeEFT----DDGW---FKTGDLGVVDEdGYYWIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 852 GRM-DNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE--IDARALKQRLSSVLPPAMIPT 928
Cdd:cd05941 340 GRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaaLSLEELKEWAKQRLAPYKRPR 419
|
490 500
....*....|....*....|...
gi 499404633 929 DYRAFHQLPKTGSNKVDRKRLLA 951
Cdd:cd05941 420 RLILVDELPRNAMGKVNKKELRK 442
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
484-949 |
6.66e-36 |
|
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: 142.13 E-value: 6.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQA 563
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 DY-QHRLAsvfsgaivlaghllssnaqavALPtaesreGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAE 642
Cdd:cd05903 82 RFrQFDPA---------------------AMP------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 643 DRVLQFAPF-NFDASIEEVFATLTSGATLVLRT----DEMLESIPTfveqvdaQAITLLDLPTAFWNEWVVGLKTGTlTM 717
Cdd:cd05903 135 DVFLVASPMaHQTGFVYGFTLPLLLGAPVVLQDiwdpDKALALMRE-------HGVTFMMGATPFLTDLLNAVEEAG-EP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 718 PSALRAIIIGGEAVyPEQLVqwqRHAPDTL--RLINTYGPTETTVVATSCDLqtQPADVAQLPIGLPLAGVNALVL---A 792
Cdd:cd05903 207 LSRLRTFVCGGATV-PRSLA---RRAAELLgaKVCSAYGSTECPGAVTSITP--APEDRRLYTDGRPLPGVEIKVVddtG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 793 AGDRPAAEGELVLLGPTLAAGYIGTEHTAFTLLAVGdrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVE 871
Cdd:cd05903 281 ATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-----WFRTGDLARLdEDGYLRITGRSKDIIIRGGENIPVLEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 872 AHLLAQPEVDEACVQGivYPNgvRRL----VAFVATKEG-EIDARALKQRLSSV-LPPAMIPTDYRAFHQLPKTGSNKVD 945
Cdd:cd05903 356 DLLLGHPGVIEAAVVA--LPD--ERLgeraCAVVVTKSGaLLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQ 431
|
....
gi 499404633 946 RKRL 949
Cdd:cd05903 432 KFRL 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
475-952 |
7.54e-36 |
|
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: 142.84 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 475 IALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIA 554
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 555 GLRTIVTQADYQH---RLASVFSGAIVLAGHLLSS--------------NAQAVALPTAESREGQIAYVMFTSGSTGLPK 617
Cdd:cd05926 86 GSKLVLTPKGELGpasRAASKLGLAILELALDVGVlirapsaeslsnllADKKNAKSEGVPLPDDLALILHTSGTTGRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 618 GVEIG----ASALDHFTAAarqrYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRtdemlesiPTFveqvdaqa 692
Cdd:cd05926 166 GVPLThrnlAASATNITNT----YKLTPDDRTLVVMPlFHVHGLVASLLSTLAAGGSVVLP--------PRF-------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 693 itlldLPTAFWNE-------WVVGLKT-----------GTLTMPSALRAIIIGGEAVYPEQLVQWQR--HAPdtlrLINT 752
Cdd:cd05926 226 -----SASTFWPDvrdynatWYTAVPTihqillnrpepNPESPPPKLRFIRSCSASLPPAVLEALEAtfGAP----VLEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 753 YGPTETTVVATSCDLQTQPADVAQLPIGlplAGVNALVLAAGDR---PAAEGELVLLGPTLAAGYIGTeHTAFTLLAVGD 829
Cdd:cd05926 297 YGMTEAAHQMTSNPLPPGPRKPGSVGKP---VGVEVRILDEDGEilpPGVVGEICLRGPNVTRGYLNN-PEANAEAAFKD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 830 RHLpayRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-E 907
Cdd:cd05926 373 GWF---RTGDLGYLdADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGaS 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 499404633 908 IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRkRLLAE 952
Cdd:cd05926 450 VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQR-RKVAE 493
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
485-949 |
1.54e-35 |
|
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: 140.69 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPE-QPRErQQHIIQIAGLRTIVTQA 563
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMlKERE-LEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 DYQhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVeigasALDHFTAAA-----RQRYG 638
Cdd:cd05935 82 ELD-----------------------------------DLALIPYTSGTTGLPKGC-----MHTHFSAAAnalqsAVWTG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 639 LRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRT----DEMLESIP----TFVEQVDAQAITLLDLPtafwnewvvG 709
Cdd:cd05935 122 LTPSDVILACLPlFHVTGFVGSLNTAVYVGGTYVLMArwdrETALELIEkykvTFWTNIPTMLVDLLATP---------E 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 710 LKTGTLtmpSALRAIIIGGEAVyPEQLVQ--WQRHApdtLRLINTYGPTETTVVATScdlqTQPADVAQLPIGLPLAGVN 787
Cdd:cd05935 193 FKTRDL---SSLKVLTGGGAPM-PPAVAEklLKLTG---LRFVEGYGLTETMSQTHT----NPPLRPKLQCLGIP*FGVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 788 ALVLAAGD----RPAAEGELVLLGPTLAAGYIGTEHT---AFTLLAvGDRHlpaYRTGDR-VRLEKGHLLYLGRMDNEFK 859
Cdd:cd05935 262 ARVIDIETgrelPPNEVGEIVVRGPQIFKGYWNRPEEteeSFIEIK-GRRF---FRTGDLgYMDEEGYFFFVDRVKRMIN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 860 ISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKE---GEIDARALKQRLSSVLPPAMIPTDYRAFHQL 936
Cdd:cd05935 338 VSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyrGKVTEEDIIEWAREQMAAYKYPREVEFVDEL 417
|
490
....*....|...
gi 499404633 937 PKTGSNKVDRKRL 949
Cdd:cd05935 418 PRSASGKILWRLL 430
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
476-949 |
4.17e-34 |
|
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: 136.82 E-value: 4.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 476 ALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAG 555
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 556 LRTIVTQADyqhrlasvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVeIGASALDHFTAAA-- 633
Cdd:cd05919 83 ARLVVTSAD-------------------------------------DIAYLLYSSGTTGPPKGV-MHAHRDPLLFADAma 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 634 RQRYGLRAEDRVLQFAPFNFDASI-EEVFATLTSGATLVLRT-----DEMLESIPTFVEQVdaqaitLLDLPTAFWNewV 707
Cdd:cd05919 125 REALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPgwptaERVLATLARFRPTV------LYGVPTFYAN--L 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 708 VGLKTGTLTMPSALRAIIIGGEAVyPEQLvqWQRHAPDTL-RLINTYGPTETTVVATScdlqTQPADVAQLPIGLPLAGV 786
Cdd:cd05919 197 LDSCAGSPDALRSLRLCVSAGEAL-PRGL--GERWMEHFGgPILDGIGATEVGHIFLS----NRPGAWRLGSTGRPVPGY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 787 NA-LVLAAGDR--PAAEGELVLLGPTLAAGYIGTEHTAFTLLAVGdrhlpAYRTGDRV-RLEKGHLLYLGRMDNEFKISG 862
Cdd:cd05919 270 EIrLVDEEGHTipPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-----WYRTGDKFcRDADGWYTHAGRADDMLKVGG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 863 YRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG----EIDARALKQRLSSVLPPAMIPTDYRAFHQLPK 938
Cdd:cd05919 345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapqESLARDIHRHLLERLSAHKVPRRIAFVDELPR 424
|
490
....*....|.
gi 499404633 939 TGSNKVDRKRL 949
Cdd:cd05919 425 TATGKLQRFKL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
479-949 |
8.58e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 135.64 E-value: 8.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 479 QRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPeqprerqqhiiqiaglrt 558
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFA------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 559 IVTQADYQHRLasvfsgaivlaghllsSNAQAVALPTAESREgqIAYVMFTSGSTGLPKGVeigasaldhftaaarqryg 638
Cdd:cd05971 64 LFGPEALEYRL----------------SNSGASALVTDGSDD--PALIIYTSGTTGPPKGA------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 639 LRAEdRVL-------QFaPFNFDASIEEVFATLTS----GATLVLRTDEMLESIPTFV---EQVDAQAItlLDLpTAFWN 704
Cdd:cd05971 107 LHAH-RVLlghlpgvQF-PFNLFPRDGDLYWTPADwawiGGLLDVLLPSLYFGVPVLAhrmTKFDPKAA--LDL-MSRYG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 705 EWVVGLKTGTLTM-----------PSALRAIIIGGEAVyPEQLVQWQRhapDTLRL-INT-YGPTETTVVATSCDLQTQP 771
Cdd:cd05971 182 VTTAFLPPTALKMmrqqgeqlkhaQVKLRAIATGGESL-GEELLGWAR---EQFGVeVNEfYGQTECNLVIGNCSALFPI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 772 ADVAqlpIGLPLAGVN-ALVLAAGDR--PAAEGELVLLGPTLAA--GYIGTEHTAFTLLAvGDRHlpayRTGDRVRL-EK 845
Cdd:cd05971 258 KPGS---MGKPIPGHRvAIVDDNGTPlpPGEVGEIAVELPDPVAflGYWNNPSATEKKMA-GDWL----LTGDLGRKdSD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 846 GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIvyPNGVRRLV--AFVATKEGEIDARALKQRLSSVLPP 923
Cdd:cd05971 330 GYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGI--PDPIRGEIvkAFVVLNPGETPSDALAREIQELVKT 407
|
490 500 510
....*....|....*....|....*....|
gi 499404633 924 AMIPTDY-RAF---HQLPKTGSNKVDRKRL 949
Cdd:cd05971 408 RLAAHEYpREIefvNELPRTATGKIRRREL 437
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
602-947 |
5.82e-33 |
|
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: 130.53 E-value: 5.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 602 QIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLrtdemLESI 681
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVL-----LERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 682 PTFVEQVDAQAITLLDL-PTAFWNEWVVGLKTGTLTmpsALRAIIIGGEAVYPEQLvqwQRHAPDTLRLINTYGPTET-T 759
Cdd:cd17630 76 QALAEDLAPPGVTHVSLvPTQLQRLLDSGQGPAALK---SLRAVLLGGAPIPPELL---ERAADRGIPLYTTYGMTETaS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 760 VVATSCDLQTQPADVAQLPIGLPLagvnalvlaagdRPAAEGELVLLGPTLAAGYIGtehtaftllavGDRHLPA----- 834
Cdd:cd17630 150 QVATKRPDGFGRGGVGVLLPGREL------------RIVEDGEIWVGGASLAMGYLR-----------GQLVPEFnedgw 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 835 YRTGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATkEGEIDARAL 913
Cdd:cd17630 207 FTTKDLGELHAdGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-RGPADPAEL 285
|
330 340 350
....*....|....*....|....*....|....
gi 499404633 914 KQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRK 947
Cdd:cd17630 286 RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
460-949 |
1.86e-32 |
|
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: 133.02 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 VLTAIAKQARKNPSHIALAQRDRQY--SYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVP 537
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADPARGLrlTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 538 LDPEQPRERQQHIIQIAGLRTIVTQADYQHRLASVFSGAIVLA-GHLLSSNAQAVALPTAESRE---GQIAYVMFTSGST 613
Cdd:cd05923 83 INPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLAlSDLVGLGEPESAGPLIEDPPrepEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 614 GLPKGVEIGASALDHFTAAARQRYGLR--AEDRVLQFAPFNFDASIEEVF-ATLTSGATLVLRTDEMLESIPTFVEQVDA 690
Cdd:cd05923 163 GLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVVEEFDPADALKLIEQERV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 691 QAitLLDLPTAFwnEWVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDtlRLINTYGPTETTvvaTSCDLQtQ 770
Cdd:cd05923 243 TS--LFATPTHL--DALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG--EKVNIYGTTEAM---NSLYMR-D 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 771 PADVAQLPIGL-------PLAGVNALVLAAGDrpaaEGELVLLGPTLAA--GYIGTEHTAFTLLAVGdrhlpAYRTGDRV 841
Cdd:cd05923 313 ARTGTEMRPGFfsevrivRIGGSPDEALANGE----EGELIVAAAADAAftGYLNQPEATAKKLQDG-----WYRTGDVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 842 RLE-KGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEIDARALKQR-LSS 919
Cdd:cd05923 384 YVDpSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFcRAS 463
|
490 500 510
....*....|....*....|....*....|
gi 499404633 920 VLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd05923 464 ELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
482-958 |
3.23e-32 |
|
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: 133.77 E-value: 3.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL----DPEQPRERqqhiIQIAGLR 557
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIfsgfGKEAAATR----LQDAEAK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 558 TIVTQADYQHR----------------LASVFSGAIVLAGHLLSSNAQAVALPTAESREGQIAY-----------VMFTS 610
Cdd:cd05968 166 ALITADGFTRRgrevnlkeeadkacaqCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGaertesedplmIIYTS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 611 GSTGLPKG---VEIG---ASALDhftaaARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLrtdemLESIPTF 684
Cdd:cd05968 246 GTTGKPKGtvhVHAGfplKAAQD-----MYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVL-----YDGAPDH 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 685 V------EQVDAQAITLLDL-PT------AFWNEWVV--GLktgtltmpSALRAIIIGGEAVYPEQLVQWQRHA-PDTLR 748
Cdd:cd05968 316 PkadrlwRMVEDHEITHLGLsPTliralkPRGDAPVNahDL--------SSLRVLGSTGEPWNPEPWNWLFETVgKGRNP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 749 LINTYGPTETTVVATSCDLqTQPadVAQLPIGLPLAGVNALVLAAGDRPAAE--GELVLLGP--TLAAGYIGTEhtaftl 824
Cdd:cd05968 388 IINYSGGTEISGGILGNVL-IKP--IKPSSFNGPVPGMKADVLDESGKPARPevGELVLLAPwpGMTRGFWRDE------ 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 825 lavgDRHLPAYRT--------GDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVR 895
Cdd:cd05968 459 ----DRYLETYWSrfdnvwvhGDFAYYdEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGE 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404633 896 RLVAFVATKEG----EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDAP 958
Cdd:cd05968 535 AIVCFVVLKPGvtptEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKEL 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
482-901 |
6.02e-32 |
|
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: 130.41 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVT 561
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 qadyqhrlasvfsgaivlaghllssnaqavalPTAEsregQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRA 641
Cdd:cd05907 84 --------------------------------EDPD----DLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 642 EDRVLQFAPFnfdASIEE----VFATLTSGATLVL--RTDEMLESIPTFVEQVDAQAITLLDlptAFWNEWVVGLKTG-- 713
Cdd:cd05907 128 GDRHLSFLPL---AHVFErragLYVPLLAGARIYFasSAETLLDDLSEVRPTVFLAVPRVWE---KVYAAIKVKAVPGlk 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 714 ----TLTMPSALRAIIIGGEAVYPEqLVQWQRHApdTLRLINTYGPTETTVVATSCDLQTQPADVaqlpIGLPLAGVNAl 789
Cdd:cd05907 202 rklfDLAVGGRLRFAASGGAPLPAE-LLHFFRAL--GIPVYEGYGLTETSAVVTLNPPGDNRIGT----VGKPLPGVEV- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 790 vlaagdRPAAEGELVLLGPTLAAGYIG-TEHTAFTLLAVGdrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKIS-GYRIQ 866
Cdd:cd05907 274 ------RIADDGEILVRGPNVMLGYYKnPEATAEALDADG-----WLHTGDLGEIdEDGFLHITGRKKDLIITSgGKNIS 342
|
410 420 430
....*....|....*....|....*....|....*
gi 499404633 867 PGEVEAHLLAQPEVDEACVQGivypNGVRRLVAFV 901
Cdd:cd05907 343 PEPIENALKASPLISQAVVIG----DGRPFLVALI 373
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
458-949 |
1.10e-31 |
|
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: 130.14 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 458 EPVLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVP 537
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 538 LDPEQPRERQQHIIQIAGLRTIV---TQADYQHRlasvfsgaiVLAGHLLSSNAqavalptaesregQIAYVMFTSGSTG 614
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIvpdRHAGFDHR---------ALARELAESIP-------------EVALFLLSGGTTG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 615 LPKGVEIGASALDHFTAAARQRYGLRAEDRVLQF--APFNFDASIEEVFATLTSGATLVLRTD-EMLESIPTfveqVDAQ 691
Cdd:cd05920 153 TPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDpSPDAAFPL----IERE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 692 AITLLDLPTAFWNEWVVGLKTGTLTmPSALRAIIIGGeAVYPEQLVqwqRHAPDTL--RLINTYGPTETTVVATSCDlqt 769
Cdd:cd05920 229 GVTVTALVPALVSLWLDAAASRRAD-LSSLRLLQVGG-ARLSPALA---RRVPPVLgcTLQQVFGMAEGLLNYTRLD--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 770 QPADVAQLPIGLPL-AGVNALVLAAGDRPAAEGE---LVLLGP-TLAAGYIGTEHTAFTLLAVGdrhlpAYRTGDRVRL- 843
Cdd:cd05920 301 DPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEegeLLTRGPyTIRGYYRAPEHNARAFTPDG-----FYRTGDLVRRt 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 844 EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSV-LP 922
Cdd:cd05920 376 PDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRERgLA 455
|
490 500
....*....|....*....|....*..
gi 499404633 923 PAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd05920 456 AYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
482-949 |
1.58e-31 |
|
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: 130.44 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIML---NRSPETiisLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRT 558
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLEL---YYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 559 IVTQADYQHRLAS------------VFSGAIVLAG----------HLLSSNAQAVALPtaESREGQIAYVMFTSGSTGLP 616
Cdd:cd12119 101 VFVDRDFLPLLEAiaprlptvehvvVMTDDAAMPEpagvgvlayeELLAAESPEYDWP--DFDENTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 617 KGVEIG--ASALDHFTAAARQRYGLRAEDRVLQFAPFnFDASIEEV-FATLTSGATLVL---RTD-----EMLESI-PTF 684
Cdd:cd12119 179 KGVVYShrSLVLHAMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLpgpYLDpaslaELIEREgVTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 685 VEQVDAQAITLLDLPTAfwnewvvglktgTLTMPSALRAIIIGGEAVyPEQLVQW--QRHapdtLRLINTYGPTETTVVA 762
Cdd:cd12119 258 AAGVPTVWQGLLDHLEA------------NGRDLSSLRRVVIGGSAV-PRSLIEAfeERG----VRVIHAWGMTETSPLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 763 TSCDLqtqPADVAQLPI----------GLPLAGVNALVLAAGDRPA-----AEGELVLLGPTLAAGYIGTEHTAFTLLAV 827
Cdd:cd12119 321 TVARP---PSEHSNLSEdeqlalrakqGRPVPGVELRIVDDDGRELpwdgkAVGELQVRGPWVTKSYYKNDEESEALTED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 828 GdrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG 906
Cdd:cd12119 398 G-----WLRTGDVATIdEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 499404633 907 E-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd12119 473 AtVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
466-952 |
2.87e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 128.93 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 466 KQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRE 545
Cdd:PRK03640 10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 546 RQQHIIQIAGLRTIVTQADYQHRLasvFSGAIVLAGHLLSSNAQAVAlPTAESREGQIAYVMFTSGSTGLPKGVEigASA 625
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKL---IPGISVKFAELMNGPKEEAE-IQEEFDLDEVATIMYTSGTTGKPKGVI--QTY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 626 LDHFTAA--ARQRYGLRAEDRVLQFAPFnFDAS-IEEVFATLTSGATLVLrtdemlesiptfVEQVDAQAITLLdlptaf 702
Cdd:PRK03640 164 GNHWWSAvgSALNLGLTEDDCWLAAVPI-FHISgLSILMRSVIYGMRVVL------------VEKFDAEKINKL------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 703 wnewvvgLKTGTLTM--------------------PSALRAIIIGGEAVYPEQLVQWQRHApdtLRLINTYGPTEttvva 762
Cdd:PRK03640 225 -------LQTGGVTIisvvstmlqrllerlgegtyPSSFRCMLLGGGPAPKPLLEQCKEKG---IPVYQSYGMTE----- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 763 TSCDLQTQPADVAQLPI---GLPLAGVNALVLAAGD--RPAAEGELVLLGPTLAAGYIGTEHTafTLLAVGDRHLpayRT 837
Cdd:PRK03640 290 TASQIVTLSPEDALTKLgsaGKPLFPCELKIEKDGVvvPPFEEGEIVVKGPNVTKGYLNREDA--TRETFQDGWF---KT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 838 GDRVRL-EKGHLLYLGRMdNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIvyPNGVRRLV--AFVaTKEGEIDARAL 913
Cdd:PRK03640 365 GDIGYLdEEGFLYVLDRR-SDLIISgGENIYPAEIEEVLLSHPGVAEAGVVGV--PDDKWGQVpvAFV-VKSGEVTEEEL 440
|
490 500 510
....*....|....*....|....*....|....*....
gi 499404633 914 KQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAE 952
Cdd:PRK03640 441 RHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
484-949 |
3.41e-31 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 128.07 E-value: 3.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDpeqprerqqhiiqiaglrTIVTQA 563
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPAT------------------TLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 DYQHRLAsvfsgaivlaghlLSSNAQAVALPTAESREGQIAYvmFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAED 643
Cdd:cd05974 63 DLRDRVD-------------RGGAVYAAVDENTHADDPMLLY--FTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 644 RVLQFA-PFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAfwneWVVGLKTGTLTMPSALR 722
Cdd:cd05974 128 VHWNISsPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTV----WRMLIQQDLASFDVKLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 723 AIIIGGEAVYPEQLVQWQRHAPDTLRliNTYGPTETTVVATSCdlQTQPADVAQLpiGLPLAGVNALVLAAGDRPAAEGE 802
Cdd:cd05974 204 EVVGAGEPLNPEVIEQVRRAWGLTIR--DGYGQTETTALVGNS--PGQPVKAGSM--GRPLPGYRVALLDPDGAPATEGE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 803 LVL-LGPT----LAAGYIGTEhtAFTLLAVGDRHlpaYRTGDRV-RLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLA 876
Cdd:cd05974 278 VALdLGDTrpvgLMKGYAGDP--DKTAHAMRGGY---YRTGDIAmRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 877 QPEVDEACVqgIVYPNGVRRLV--AFVATKEGEIDARALKQRLSSVLPPAMIPtdYR-----AFHQLPKTGSNKVDRKRL 949
Cdd:cd05974 353 HPAVAEAAV--VPSPDPVRLSVpkAFIVLRAGYEPSPETALEIFRFSRERLAP--YKrirrlEFAELPKTISGKIRRVEL 428
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
469-953 |
7.16e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 128.57 E-value: 7.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 469 RKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIM-LNRsPETIISLLAVMQCGAVYVPLDPEQPRERQ 547
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLsLNR-PEVLMAIGAAQLAGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 548 QHIIQIAGLRT-IVTQADYQHR----------LASVFS-GAIVLAGHLLSSNAQAVALP-TAESREGQIAYVMFTSGSTG 614
Cdd:PRK06188 102 AYVLEDAGISTlIVDPAPFVERalallarvpsLKHVLTlGPVPDGVDLLAAAAKFGPAPlVAAALPPDIAGLAYTGGTTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 615 LPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNfDASIEEVFATLTSGATLVLRT----DEMLESIP----TFVE 686
Cdd:PRK06188 182 KPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVLAkfdpAEVLRAIEeqriTATF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 687 QVDAQAITLLDLPtafwnewvvGLKTGTLtmpSALRAIIIGGEAVYPEQLVQ-WQRHAPdtlRLINTYGPTETTVVATSC 765
Cdd:PRK06188 261 LVPTMIYALLDHP---------DLRTRDL---SSLETVYYGASPMSPVRLAEaIERFGP---IFAQYYGQTEAPMVITYL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 766 D-LQTQPADVAQL-PIGLPLAGVNALVLAAGDRPAAE---GELVLLGPTLAAGYIGT-EHTAFTlLAVGDRHlpayrTGD 839
Cdd:PRK06188 326 RkRDHDPDDPKRLtSCGRPTPGLRVALLDEDGREVAQgevGEICVRGPLVMDGYWNRpEETAEA-FRDGWLH-----TGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 840 RVRLEKGHLLYLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARAL---- 913
Cdd:PRK06188 400 VAREDEDGFYYIVDRKKDMIVTgGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAaVDAAELqahv 479
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499404633 914 KQRLSSVLPPAMIptDYRAfhQLPKTGSNKVDRKRLLAEY 953
Cdd:PRK06188 480 KERKGSVHAPKQV--DFVD--SLPLTALGKPDKKALRARY 515
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
4-251 |
1.03e-30 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 121.68 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 4 LSVAQCGLWLghaLNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpeigfVASQLPVPi 83
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQR-----IDPDADLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 84 gvLPIVELLPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIYT 162
Cdd:COG4908 72 --LEVVDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIrLGEDEHVLLLTIHHIISDGWSLGILLRELAALYA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 163 ALTAGQSAPVAEF-GPFSAVLEEERQRDASGQTAQARDFWLETLNAMPEPASF-SEKKAP--IAARFLRQSCDMPADLWQ 238
Cdd:COG4908 150 ALLEGEPPPLPELpIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELpTDRPRPavQTFRGATLSFTLPAELTE 229
|
250
....*....|...
gi 499404633 239 PLSALCEGNKISW 251
Cdd:COG4908 230 ALKALAKAHGATV 242
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
468-955 |
1.14e-30 |
|
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: 128.13 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALA------QRDRQYSYQQLLGLSGQAAAALHERGvKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL-DP 540
Cdd:cd05931 3 AAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 541 EQPR--ERQQHIIQIAGLRTIVTQADYQHRLASVFSGAIVLAGH-------LLSSNAQAVALPTAESREgqIAYVMFTSG 611
Cdd:cd05931 82 TPGRhaERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPrllvvdlLPDTSAADWPPPSPDPDD--IAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 612 STGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFD-ASIEEVFATLTSGATLVL--------RTDEMLESI- 681
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGPSVLmspaaflrRPLRWLRLIs 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 682 ---------PTF-----VEQVDAQAITLLDLptafwnewvvglktgtltmpSALRAIIIGGEAVYPEQLVQW-QRHAPDT 746
Cdd:cd05931 240 ryratisaaPNFaydlcVRRVRDEDLEGLDL--------------------SSWRVALNGAEPVRPATLRRFaEAFAPFG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 747 LR---LINTYGPTETTVVATSCDLQTQP----------------------ADVAQLPIGLPLAGVNALVL-AAGDRPAAE 800
Cdd:cd05931 300 FRpeaFRPSYGLAEATLFVSGGPPGTGPvvlrvdrdalagravavaaddpAARELVSCGRPLPDQEVRIVdPETGRELPD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 801 ---GELVLLGPTLAAGYIG----TEHTAFTLLAVGDRhlPAYRTGDRVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAH 873
Cdd:cd05931 380 gevGEIWVRGPSVASGYWGrpeaTAETFGALAATDEG--GWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEAT 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 874 L-LAQPEVDEACVQGIVYP-NGVRRL--VAFVATKEGEIDARALKQRLSS-------------VLPPAmiptdyrafHQL 936
Cdd:cd05931 458 AeEAHPALRPGCVAAFSVPdDGEERLvvVAEVERGADPADLAAIAAAIRAavarehgvapadvVLVRP---------GSI 528
|
570
....*....|....*....
gi 499404633 937 PKTGSNKVDRKRLLAEYHD 955
Cdd:cd05931 529 PRTSSGKIQRRACRAAYLD 547
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
449-952 |
1.39e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 128.24 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 449 TSREPE-PFVEPVLTAIAKQ-ARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLL 526
Cdd:PRK06178 22 IPREPEyPHGERPLTEYLRAwARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 527 AVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADY---------QHRLASVF------------------------ 573
Cdd:PRK06178 102 GILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLapvveqvraETSLRHVIvtsladvlpaeptlplpdslrapr 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 574 ---SGAIVLAGHLLSSNAQAVALPTAesrEGQIAYVMFTSGSTGLPKGVEigasaldH------FTAAARQRYGLRAE-- 642
Cdd:PRK06178 182 laaAGAIDLLPALRACTAPVPLPPPA---LDALAALNYTGGTTGMPKGCE-------HtqrdmvYTAAAAYAVAVVGGed 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 643 DRVLQFAPFNFDASieEVFATLT---SGATLVL--RTDEM--LESIPTF-----VEQVDaQAITLLDLPtafwnewvvGL 710
Cdd:PRK06178 252 SVFLSFLPEFWIAG--ENFGLLFplfSGATLVLlaRWDAVafMAAVERYrvtrtVMLVD-NAVELMDHP---------RF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 711 KTGTLTMPSALRAIIIgGEAVYPEQLVQWQRHAPDTLRLInTYGPTETTVVAT-SCDLQTQPADVAQLPI--GLPLAGVN 787
Cdd:PRK06178 320 AEYDLSSLRQVRVVSF-VKKLNPDYRQRWRALTGSVLAEA-AWGMTETHTCDTfTAGFQDDDFDLLSQPVfvGLPVPGTE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 788 ALV--LAAGD-RP-AAEGELVLLGPTLAAGYIGTEHTAFTLLAVGdrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISG 862
Cdd:PRK06178 398 FKIcdFETGElLPlGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-----WLHTGDIGKIdEQGFLHYLGRRKEMLKVNG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 863 YRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTdYRAFHQLPKTGS 941
Cdd:PRK06178 473 MSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGaDLTAAALQAWCRENMAVYKVPE-IRIVDALPMTAT 551
|
570
....*....|.
gi 499404633 942 NKVDRKRLLAE 952
Cdd:PRK06178 552 GKVRKQDLQAL 562
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
484-949 |
2.08e-30 |
|
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: 125.15 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEqprerqqhiiqiaglrtivtqa 563
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 dyqhrlasvfsgaivlaghlLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIgaSALDHFTAA--ARQRYGLRA 641
Cdd:cd05912 60 --------------------LTPNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQ--TFGNHWWSAigSALNLGLTE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 642 EDRVLQFAPFnFDasieevfatlTSGATLVLRTdeMLESIP-TFVEQVDAQAITLLdlptafwnewvvgLKTGTLTM--- 717
Cdd:cd05912 118 DDNWLCALPL-FH----------ISGLSILMRS--VIYGMTvYLVDKFDAEQVLHL-------------INSGKVTIisv 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 718 ----------------PSALRAIIIGGEAVYPEQLVQW-QRHAPdtlrLINTYGPTETT---VVATSCDLQTQPADVaql 777
Cdd:cd05912 172 vptmlqrlleilgegyPNNLRCILLGGGPAPKPLLEQCkEKGIP----VYQSYGMTETCsqiVTLSPEDALNKIGSA--- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 778 piGLPLAGVNALVLAAGDRPAAEGELVLLGPTLAAGYIGTEHTAFTLLAVGdrhlpAYRTGDRVRL-EKGHLLYLGRMdN 856
Cdd:cd05912 245 --GKPLFPVELKIEDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENG-----WFKTGDIGYLdEEGFLYVLDRR-S 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 857 EFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVaTKEGEIDARALKQRLSSVLPPAMIPTDYRAFHQ 935
Cdd:cd05912 317 DLIISgGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFV-VSERPISEEELIAYCSEKLAKYKVPKKIYFVDE 395
|
490
....*....|....
gi 499404633 936 LPKTGSNKVDRKRL 949
Cdd:cd05912 396 LPRTASGKLLRHEL 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
476-949 |
3.44e-30 |
|
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: 124.90 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 476 ALAQRDRQYSYQQLLGLSGQAAAAL-HERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQia 554
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 555 glRTIVTQADYQHRLASVfsgaivlaghllssnaqavalptaesreGQIAYVMFTSGSTGLPKG-VEIGASALDHFTAAA 633
Cdd:cd05958 81 --KARITVALCAHALTAS----------------------------DDICILAFTSGTTGAPKAtMHFHRDPLASADRYA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 634 RQRYGLRAEDRVLQFAP--FNFDASIEEVFATLTSGATLVL--RT-DEMLESIPTFveqvdaQAITLLDLPTAFwnEWVV 708
Cdd:cd05958 131 VNVLRLREDDRFVGSPPlaFTFGLGGVLLFPFGVGASGVLLeeATpDLLLSAIARY------KPTVLFTAPTAY--RAML 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 709 GLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQrhAPDTLRLINTYGPTETTVVATSCDlqtqPADVAQLPIGLPLAGVNA 788
Cdd:cd05958 203 AHPDAAGPDLSSLRKCVSAGEALPAALHRAWK--EATGIPIIDGIGSTEMFHIFISAR----PGDARPGATGKPVPGYEA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 789 LVLAAGDRPAAEGE---LVLLGPTlAAGYIGTEHTAftlLAVGDRHLPayrTGDR-VRLEKGHLLYLGRMDNEFKISGYR 864
Cdd:cd05958 277 KVVDDEGNPVPDGTigrLAVRGPT-GCRYLADKRQR---TYVQGGWNI---TGDTySRDPDGYFRHQGRSDDMIVSGGYN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 865 IQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEID----ARALKQRLSSVLPPAMIPTDYRAFHQLPKTG 940
Cdd:cd05958 350 IAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPgpvlARELQDHAKAHIAPYKYPRAIEFVTELPRTA 429
|
....*....
gi 499404633 941 SNKVDRKRL 949
Cdd:cd05958 430 TGKLQRFAL 438
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
463-944 |
2.23e-29 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 124.61 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIAL------AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYV 536
Cdd:cd17634 58 ALDRHLRENGDRTAIiyegddTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 537 P-------------LDPEQPR---------ERQQHI-----------IQIAGLRTIV----TQADYQhrlasvFSGAIVL 579
Cdd:cd17634 138 VifggfapeavagrIIDSSSRllitadggvRAGRSVplkknvddalnPNVTSVEHVIvlkrTGSDID------WQEGRDL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 580 AGHLLSSNAQAVALPTAESREGQIaYVMFTSGSTGLPKGV--EIGASALdHFTAAARQRYGLRAEDRVLQFAPFNFDASI 657
Cdd:cd17634 212 WWRDLIAKASPEHQPEAMNAEDPL-FILYTSGTTGKPKGVlhTTGGYLV-YAATTMKYVFDYGPGDIYWCTADVGWVTGH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 658 EE-VFATLTSGATLVlrtdeMLESIPT------FVEQVDAQAITLLDL-PTAFWNEWVVGLKTGTLTMPSALRAIIIGGE 729
Cdd:cd17634 290 SYlLYGPLACGATTL-----LYEGVPNwptparMWQVVDKHGVNILYTaPTAIRALMAAGDDAIEGTDRSSLRILGSVGE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 730 AVYPEQLVQWQRHAPDTLR-LINTYGPTETTvvatscdlqtqPADVAQLPIGLPLA---------GVNALVLAAGDRPA- 798
Cdd:cd17634 365 PINPEAYEWYWKKIGKEKCpVVDTWWQTETG-----------GFMITPLPGAIELKagsatrpvfGVQPAVVDNEGHPQp 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 799 --AEGELVL---LGPTLAAGYIGTEHTAFTLLAVGDRHlpaYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEA 872
Cdd:cd17634 434 ggTEGNLVItdpWPGQTRTLFGDHERFEQTYFSTFKGM---YFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIES 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404633 873 HLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEID----ARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKV 944
Cdd:cd17634 511 VLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPspelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
464-949 |
8.05e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 121.81 E-value: 8.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPgERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:PRK07638 7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQHIIQIAGLRTIVTQADYQHRLASVfSGAIVLAGHL--LSSNAQAVALPTaESREGQIAYVMFTSGSTGLPKG-VE 620
Cdd:PRK07638 86 QDELKERLAISNADMIVTERYKLNDLPDE-EGRVIEIDEWkrMIEKYLPTYAPI-ENVQNAPFYMGFTSGSTGKPKAfLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 621 IGASALDHFTAAARQrYGLRAEDRV-----LQFAPFNFDAsieevFATLTSGATL-VLRT---DEMLESIPTfvEQVDaq 691
Cdd:PRK07638 164 AQQSWLHSFDCNVHD-FHMKREDSVliagtLVHSLFLYGA-----ISTLYVGQTVhLMRKfipNQVLDKLET--ENIS-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 692 aiTLLDLPTAfwnewvvglkTGTLTMPSALR----AIIIGG---EAVYPEQLVQWQRHApdtlRLINTYGPTETTVVATS 764
Cdd:PRK07638 234 --VMYTVPTM----------LESLYKENRVIenkmKIISSGakwEAEAKEKIKNIFPYA----KLYEFYGASELSFVTAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 765 cdlqtQPADVAQLP--IGLPLAGVNALVL-AAGDR--PAAEGELVLLGPTLAAGYIGTehtaftllAVGDRHLPA--YRT 837
Cdd:PRK07638 298 -----VDEESERRPnsVGRPFHNVQVRICnEAGEEvqKGEIGTVYVKSPQFFMGYIIG--------GVLARELNAdgWMT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 838 GDRVRL--EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVatkEGEIDARALKQ 915
Cdd:PRK07638 365 VRDVGYedEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQLKS 441
|
490 500 510
....*....|....*....|....*....|....
gi 499404633 916 RLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK07638 442 FCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
465-950 |
8.10e-29 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 122.70 E-value: 8.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 465 AKQARKNpsHIAL----AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL-- 538
Cdd:PRK04319 53 ADGGRKD--KVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfe 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 --DPEQPRERqqhiIQIAGLRTIVTQAD-YQH----RLASVfsGAIVLAGHLLSSNAQAVALPT---AESREGQI----- 603
Cdd:PRK04319 131 afMEEAVRDR----LEDSEAKVLITTPAlLERkpadDLPSL--KHVLLVGEDVEEGPGTLDFNAlmeQASDEFDIewtdr 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 604 ---AYVMFTSGSTGLPKGV-EIGASALDHFtAAARQRYGLRAEDRVLQFA-PFNFDASIEEVFATLTSGATLVLRTDEMl 678
Cdd:PRK04319 205 edgAILHYTSGSTGKPKGVlHVHNAMLQHY-QTGKYVLDLHEDDVYWCTAdPGWVTGTSYGIFAPWLNGATNVIDGGRF- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 679 eSIPTFVEQVDAQAITL-LDLPTAFwnewvvglktgTLTMP-----------SALRAIIIGGEAVYPEqLVQWQRHAPDt 746
Cdd:PRK04319 283 -SPERWYRILEDYKVTVwYTAPTAI-----------RMLMGagddlvkkydlSSLRHILSVGEPLNPE-VVRWGMKVFG- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 747 LRLINTYGPTET---TVVATSCdlqtqpADVAQLPIGLPLAGVNALVL---AAGDRPAAEGELVLLG--PTLAAGYIGTE 818
Cdd:PRK04319 349 LPIHDNWWMTETggiMIANYPA------MDIKPGSMGKPLPGIEAAIVddqGNELPPNRMGNLAIKKgwPSMMRGIWNNP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 819 ---HTAFtllaVGDrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIvyPNGV 894
Cdd:PRK04319 423 ekyESYF----AGD----WYVSGDSAYMdEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK--PDPV 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404633 895 R--RLVAFVATKEG---------EIDARAlKQRLSSVLPPAMIptDYRAfhQLPKTGSNKVDRkRLL 950
Cdd:PRK04319 493 RgeIIKAFVALRPGyepseelkeEIRGFV-KKGLGAHAAPREI--EFKD--KLPKTRSGKIMR-RVL 553
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
465-952 |
8.21e-29 |
|
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: 122.18 E-value: 8.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 465 AKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYV-PLdpeqP 543
Cdd:COG1021 32 RRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVfAL----P 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQ---HIIQIAGLRTIVTQA-----DYQ---HRLASVFSG--AIVLAG---------HLLssnAQAVALPTAESREG 601
Cdd:COG1021 108 AHRRAeisHFAEQSEAVAYIIPDrhrgfDYRalaRELQAEVPSlrHVLVVGdageftsldALL---AAPADLSEPRPDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 602 QIAYVMFTSGSTGLPKGVE---------IGASAldhftaaarQRYGLRAEDRVLQFAP--FNFDASIEEVFATLTSGATL 670
Cdd:COG1021 185 DVAFFQLSGGTTGLPKLIPrthddylysVRASA---------EICGLDADTVYLAALPaaHNFPLSSPGVLGVLYAGGTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 671 VL----RTDEMLESIP----TFVEQVDAQAITLLDLPTAfwnewvvglktgTLTMPSALRAIIIGGeAVYPEQLVqwqRH 742
Cdd:COG1021 256 VLapdpSPDTAFPLIErervTVTALVPPLALLWLDAAER------------SRYDLSSLRVLQVGG-AKLSPELA---RR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 743 APDTL--RLINTYGPTETTVVATSCD------LQTQ-----PAD-VaqlpiglplagvnaLVLAAGDRPAAEGEL-VLL- 806
Cdd:COG1021 320 VRPALgcTLQQVFGMAEGLVNYTRLDdpeeviLTTQgrpisPDDeV--------------RIVDEDGNPVPPGEVgELLt 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 807 -GP-TLAAGYIGTEH--TAFTllAVGdrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVD 881
Cdd:COG1021 386 rGPyTIRGYYRAPEHnaRAFT--PDG-----FYRTGDLVRRtPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVH 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404633 882 EACVQGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSV------LPPAMIPTDyrafhQLPKTGSNKVDRKRLLAE 952
Cdd:COG1021 459 DAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLRERglaafkLPDRLEFVD-----ALPLTAVGKIDKKALRAA 530
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
472-1045 |
1.76e-28 |
|
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: 124.02 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:TIGR03443 259 PSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQA----------DYQHR----------LASVFSGAIVlaGHLLSSNAQAVALPTAESREGQIAYVM---- 607
Cdd:TIGR03443 339 SVAKPRALIVIEkagtldqlvrDYIDKelelrteipaLALQDDGSLV--GGSLEGGETDVLAPYQALKDTPTGVVVgpds 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 608 -----FTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDE------ 676
Cdd:TIGR03443 417 nptlsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADdigtpg 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 677 -----MLES-------IPTFVEQVDAQAITLL-DLPTAFWnewvVGlktGTLTMPSALRAiiiggeavypeqlvqwQRHA 743
Cdd:TIGR03443 497 rlaewMAKYgatvthlTPAMGQLLSAQATTPIpSLHHAFF----VG---DILTKRDCLRL----------------QTLA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 744 PDtLRLINTYGPTET-------TVVATSCD---LQTQpADVaqLPIGLPLAGVNALVLAAGDRPA----AE-GELVLLGP 808
Cdd:TIGR03443 554 EN-VCIVNMYGTTETqravsyfEIPSRSSDstfLKNL-KDV--MPAGKGMKNVQLLVVNRNDRTQtcgvGEvGEIYVRAG 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 809 TLAAGYIGT----------------EHTAFTLLAVG-----------DRhlpAYRTGDRVR-LEKGHLLYLGRMDNEFKI 860
Cdd:TIGR03443 630 GLAEGYLGLpelnaekfvnnwfvdpSHWIDLDKENNkperefwlgprDR---LYRTGDLGRyLPDGNVECCGRADDQVKI 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 861 SGYRIQPGEVEAHLLAQPEVDE-------------ACVQGIVYPNGVRRLVAFVATKEGEIDA----------RAL---- 913
Cdd:TIGR03443 707 RGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeepTLVSYIVPQDKSDELEEFKSEVDDEESSdpvvkglikyRKLikdi 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 914 KQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL----------LAEYHDDAPTQALASETENRVSAIWQQIL--GVS 981
Cdd:TIGR03443 787 REYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALpfpdtaqlaaVAKNRSASAADEEFTETEREIRDLWLELLpnRPA 866
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404633 982 GIQSRDNFFELGGQSLQTIQIVNRLAAEFSVSIKVSDVFDHPQLSDFCRYLDDRLSQDENSVEM 1045
Cdd:TIGR03443 867 TISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKGEELADEG 930
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
464-885 |
1.79e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 122.13 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRD----RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLD 539
Cdd:COG1022 17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 540 PEQPRERQQHIIQIAGLRTIVTQADYQ-HRLASVFSGA------IVLAGHLLSSNAQAVALPT----------------- 595
Cdd:COG1022 97 PTSSAEEVAYILNDSGAKVLFVEDQEQlDKLLEVRDELpslrhiVVLDPRGLRDDPRLLSLDEllalgrevadpaelear 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 596 -AESREGQIAYVMFTSGSTGLPKGVEigasaLDH--FTAAAR---QRYGLRAEDRVLQFAPFN--FDASIEevFATLTSG 667
Cdd:COG1022 177 rAAVKPDDLATIIYTSGTTGRPKGVM-----LTHrnLLSNARallERLPLGPGDRTLSFLPLAhvFERTVS--YYALAAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 668 ATLVL--RTDEMLESI----PTFV-------EQVDAQAIT-----------------------------------LLDLP 699
Cdd:COG1022 250 ATVAFaeSPDTLAEDLrevkPTFMlavprvwEKVYAGIQAkaeeagglkrklfrwalavgrryararlagkspslLLRLK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 700 TAFWNEWVVGL---KTGtltmpSALRAIIIGGEAVypeqlvqwqrhAPDTLR--------LINTYGPTETTVVATscdlq 768
Cdd:COG1022 330 HALADKLVFSKlreALG-----GRLRFAVSGGAAL-----------GPELARffralgipVLEGYGLTETSPVIT----- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 769 TQPADvAQLP--IGLPLAGVNAlvlaagdRPAAEGELVLLGPTLAAGYIG-TEHTAFTLLAVGdrhlpAYRTGDRVRL-E 844
Cdd:COG1022 389 VNRPG-DNRIgtVGPPLPGVEV-------KIAEDGEILVRGPNVMKGYYKnPEATAEAFDADG-----WLHTGDIGELdE 455
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 499404633 845 KGHLLYLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACV 885
Cdd:COG1022 456 DGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
483-949 |
1.98e-28 |
|
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: 121.03 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 483 QYSYQQLLGLSGQAAAALHER-GVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVT 561
Cdd:cd05928 41 KWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 QADYQHRLASVFSGAIVLAGHLLSSnaqavalptAESREGQIAY-----------------------VMFTSGSTGLPKG 618
Cdd:cd05928 121 SDELAPEVDSVASECPSLKTKLLVS---------EKSRDGWLNFkellneastehhcvetgsqepmaIYFTSGTTGSPKM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 619 VEIGASALDH-FTAAARQRYGLRAEDRVLQFAPFNF-DASIEEVFATLTSGATLvlrtdeMLESIPTFveqvDAQAI--T 694
Cdd:cd05928 192 AEHSHSSLGLgLKVNGRYWLDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGACV------FVHHLPRF----DPLVIlkT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 695 LLDLP-TAFWN-----EWVVGLKTGTLTMPSaLRAIIIGGEAVYPEQLVQWQRHApdTLRLINTYGPTETTVV-ATSCDL 767
Cdd:cd05928 262 LSSYPiTTFCGaptvyRMLVQQDLSSYKFPS-LQHCVTGGEPLNPEVLEKWKAQT--GLDIYEGYGQTETGLIcANFKGM 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 768 QTQPADV--AQLPIGLPLAGVNALVLAagdrPAAEGELVL-LGPT----LAAGYIGT-EHTAFTLLavGDrhlpAYRTGD 839
Cdd:cd05928 339 KIKPGSMgkASPPYDVQIIDDNGNVLP----PGTEGDIGIrVKPIrpfgLFSGYVDNpEKTAATIR--GD----FYLTGD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 840 RVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVqgIVYPNGVRRLV--AFVA------TKEGEIDA 910
Cdd:cd05928 409 RGIMDEdGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAV--VSSPDPIRGEVvkAFVVlapqflSHDPEQLT 486
|
490 500 510
....*....|....*....|....*....|....*....
gi 499404633 911 RALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd05928 487 KELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
468-885 |
2.98e-28 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 119.59 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGEriGIML---NrSPETIISLLAVMQCGAVYVPLDPEQPR 544
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGS--GVALrgkN-SPETLLAYLALLQCGARVLPLNPQLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 545 ERQQHIIQIAGLRTIVTQADYQHrlasvFSGaivLAGHLLSSNAQAVALPTAESRegqIAYVMFTSGSTGLPKGVEIGAS 624
Cdd:PRK09029 90 PLLEELLPSLTLDFALVLEGENT-----FSA---LTSLHLQLVEGAHAVAWQPQR---LATMTLTSGSTGLPKAAVHTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 625 AldHFTAAArqryGlraedrVLQFapFNFDAS----------------IeeVFATLTSGATLVLRTDEMLESiptfveqv 688
Cdd:PRK09029 159 A--HLASAE----G------VLSL--MPFTAQdswllslplfhvsgqgI--VWRWLYAGATLVVRDKQPLEQ-------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 689 DAQAITLLDL-PTAFW---NEWVVglktgtltmPSALRAIIIGGEAVyPEQLVQwQRHApdtlRLINT---YGPTE--TT 759
Cdd:PRK09029 215 ALAGCTHASLvPTQLWrllDNRSE---------PLSLKAVLLGGAAI-PVELTE-QAEQ----QGIRCwcgYGLTEmaST 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 760 VVATSCDlqtQPADVaqlpiGLPLAGVN-ALVlaagdrpaaEGELVLLGPTLAAGYigtehtaftllavgdrhlpaYRTG 838
Cdd:PRK09029 280 VCAKRAD---GLAGV-----GSPLPGREvKLV---------DGEIWLRGASLALGY--------------------WRQG 322
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404633 839 ---------------DRVRLEKGHLLYLGRMDNEFkIS-GYRIQPGEVEAHLLAQPEVDEACV 885
Cdd:PRK09029 323 qlvplvndegwfatrDRGEWQNGELTILGRLDNLF-FSgGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
464-953 |
5.32e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 119.22 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:PRK06145 8 IAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQHIIQIAGLRTIVTQADYQHRLASVFSgAIVLAGHLLSSNAQ-----AVALPTAESREGQIAYVMFTSGSTGLPKG 618
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLVDEEFDAIVALETP-KIVIDAAAQADSRRlaqggLEIPPQAAVAPTDLVRLMYTSGTTDRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 619 V-----EIGASALDHFTAaarqrYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQvdaqa 692
Cdd:PRK06145 167 VmhsygNLHWKSIDHVIA-----LGLTASERLLVVGPlYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIER----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 693 itllDLPTAFWNEWVvgLKTGTLTMP-------SALRAIIIGGEAVyPEQLVQWQRHAPDTLRLINTYGPTETTVVATsc 765
Cdd:PRK06145 237 ----HRLTCAWMAPV--MLSRVLTVPdrdrfdlDSLAWCIGGGEKT-PESRIRDFTRVFTRARYIDAYGLTETCSGDT-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 766 dLQTQPADVAQL-PIGLPLAGVNALVLAAGDR---PAAEGELVLLGPTLAAGYI-GTEHTAFTLlaVGDrhlpAYRTGDR 840
Cdd:PRK06145 308 -LMEAGREIEKIgSTGRALAHVEIRIADGAGRwlpPNMKGEICMRGPKVTKGYWkDPEKTAEAF--YGD----WFRSGDV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 841 VRLEKGHLLYLGRMDNEFKISG-YRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG---EIDA--RALK 914
Cdd:PRK06145 381 GYLDEEGFLYLTDRKKDMIISGgENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGatlTLEAldRHCR 460
|
490 500 510
....*....|....*....|....*....|....*....
gi 499404633 915 QRLSSVlppaMIPTDYRAFHQLPKTGSNKVDRKRLLAEY 953
Cdd:PRK06145 461 QRLASF----KVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
468-944 |
1.19e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 118.91 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALH-ERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRER 546
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 547 QQHIIQIAGLRTIVTQADY-------------QHRLASVFSGAIVLAG-----------------------HLLSSNAQA 590
Cdd:PRK08314 100 LAHYVTDSGARVAIVGSELapkvapavgnlrlRHVIVAQYSDYLPAEPeiavpawlraepplqalapggvvAWKEALAAG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 591 VALPTAESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGAT 669
Cdd:PRK08314 180 LAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPlFHVTGMVHSMNAPIYAGAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 670 LVL--RTD-----EMLE--------SIPTFVEQVDAQ-AITLLDLptafwnewvvglktgtltmpSALRaIIIGGEAVYP 733
Cdd:PRK08314 260 VVLmpRWDreaaaRLIEryrvthwtNIPTMVVDFLASpGLAERDL--------------------SSLR-YIGGGGAAMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 734 EQLVQ--WQRHApdtLRLINTYGPTETtvVATScdlQTQPADVAQLP-IGLPLAGVNALV--------LAAGDrpaaEGE 802
Cdd:PRK08314 319 EAVAErlKELTG---LDYVEGYGLTET--MAQT---HSNPPDRPKLQcLGIPTFGVDARVidpetleeLPPGE----VGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 803 LVLLGPTLAAGYIGTEHT---AFTLLAvGDRHLpayRTGDrvrlekghllyLGRMDNE--FKI----------SGYRIQP 867
Cdd:PRK08314 387 IVVHGPQVFKGYWNRPEAtaeAFIEID-GKRFF---RTGD-----------LGRMDEEgyFFItdrlkrminaSGFKVWP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 868 GEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG--------EIDARAlKQRLSSVlppaMIPTDYRAFHQLPKT 939
Cdd:PRK08314 452 AEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEargktteeEIIAWA-REHMAAY----KYPRIVEFVDSLPKS 526
|
....*
gi 499404633 940 GSNKV 944
Cdd:PRK08314 527 GSGKI 531
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
449-949 |
1.47e-27 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 118.71 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 449 TSREPEPFVEPVLTAI-AKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLA 527
Cdd:PRK06155 11 RAVDPLPPSERTLPAMlARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 528 VMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLASVFSGAIVLAGHLLSSNAQAVALPT------------ 595
Cdd:PRK06155 91 CAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAgwstaplpplda 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 596 ----AESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLV 671
Cdd:PRK06155 171 papaAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 672 LR--------TDEMLESIPTFVEQVDAQAITLLDLPtafwnewvvglkTGTLTMPSALRAIIIGGEAVypeqlvqwQRHA 743
Cdd:PRK06155 251 LEprfsasgfWPAVRRHGATVTYLLGAMVSILLSQP------------ARESDRAHRVRVALGPGVPA--------ALHA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 744 PDTLR----LINTYGPTETTVVaTSCDLQTQPADVAqlpiGLPLAGVNALVLAAGDR--PAAE-GELVLLGP---TLAAG 813
Cdd:PRK06155 311 AFRERfgvdLLDGYGSTETNFV-IAVTHGSQRPGSM----GRLAPGFEARVVDEHDQelPDGEpGELLLRADepfAFATG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 814 YIGTehTAFTLLAVgdRHLpAYRTGDRV-RLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPN 892
Cdd:PRK06155 386 YFGM--PEKTVEAW--RNL-WFHTGDRVvRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404633 893 GVRRLVAFVATKEGE-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK06155 461 GEDEVMAAVVLRDGTaLEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
464-949 |
2.24e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 117.22 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPShiALAQRD----RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLD 539
Cdd:PRK09088 1 IAFHARLQPQ--RLAAVDlalgRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 540 PEQPRERQQHIIQIAGLRTIVTQADYQHrlasvfSGAIVLAGHLLSSNAQAVAL-PTAESREGQIAYVMFTSGSTGLPKG 618
Cdd:PRK09088 79 WRLSASELDALLQDAEPRLLLGDDAVAA------GRTDVEDLAAFIASADALEPaDTPSIPPERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 619 VEIGASALDHfTAAARQRYG-LRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVL-------RTDEMLESIPTFVEQ-- 687
Cdd:PRK09088 153 VMLSERNLQQ-TAHNFGVLGrVDAHSSFLCDAPmFHIIGLITSVRPVLAVGGSILVsngfepkRTLGRLGDPALGITHyf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 688 -VDAQAITLLDLPTafwnewvvglktgtlTMPSALR---AIIIGGEAVYPEQLVQWqrhAPDTLRLINTYGPTETTVV-- 761
Cdd:PRK09088 232 cVPQMAQAFRAQPG---------------FDAAALRhltALFTGGAPHAAEDILGW---LDDGIPMVDGFGMSEAGTVfg 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 762 -ATSCDLQTQPADVAqlpiGLPLAGVNALVLAAGDR--PAAE-GELVLLGPTLAAGYIG-TEHTAFTLLAVGdrhlpAYR 836
Cdd:PRK09088 294 mSVDCDVIRAKAGAA----GIPTPTVQTRVVDDQGNdcPAGVpGELLLRGPNLSPGYWRrPQATARAFTGDG-----WFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 837 TGDRVRLE-KGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPN--GVRRLVAFVATkEGEIDARAL 913
Cdd:PRK09088 365 TGDIARRDaDGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwgEVGYLAIVPAD-GAPLDLERI 443
|
490 500 510
....*....|....*....|....*....|....*.
gi 499404633 914 KQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK09088 444 RSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
485-949 |
2.27e-27 |
|
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: 117.43 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLgLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQAD 564
Cdd:cd05909 9 TYRKLL-TGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 565 YQHRLASVFSGAI-----------------------VLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEI 621
Cdd:cd05909 88 FIEKLKLHHLFDVeydarivyledlrakiskadkckAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 622 GASALDHFTAAARQRYGLRAEDRVLQFAP----FNFDASIeevFATLTSGATLVLRTDEM-LESIPTFVEqvDAQAITLL 696
Cdd:cd05909 168 SHKNLLANVEQITAIFDPNPEDVVFGALPffhsFGLTGCL---WLPLLSGIKVVFHPNPLdYKKIPELIY--DKKATILL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 697 DLPTaFWNEWvvgLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHApdTLRLINTYGPTETTVVATscdLQTQPADVAQ 776
Cdd:cd05909 243 GTPT-FLRGY---ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF--GIRILEGYGTTECSPVIS---VNTPQSPNKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 777 LPIGLPLAGVNALVLA-AGDRPAAEGE---LVLLGPTLAAGYIGT-EHTAFtllAVGDRHlpaYRTGDRVRL-EKGHLLY 850
Cdd:cd05909 314 GTVGRPLPGMEVKIVSvETHEEVPIGEgglLLVRGPNVMLGYLNEpELTSF---AFGDGW---YDTGDIGKIdGEGFLTI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 851 LGRMDNEFKISGYRIQPGEVEAHLLAQ-PEVDEACVQGIVYPNGVRRLVAFVATKEGEIDarALKQRLSSV-LPPAMIPT 928
Cdd:cd05909 388 TGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPS--SLNDILKNAgISNLAKPS 465
|
490 500
....*....|....*....|.
gi 499404633 929 DYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd05909 466 YIHQVEEIPLLGTGKPDYVTL 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
482-949 |
3.60e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 117.09 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVT 561
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 QADY---------------QHR-LASVFSGAIVLAGHLLSSNAQAVA----LPTAESREgqIAYVMFTSGSTGLPKGVEI 621
Cdd:PRK08008 116 SAQFypmyrqiqqedatplRHIcLTRVALPADDGVSSFTQLKAQQPAtlcyAPPLSTDD--TAEILFTSGTTSRPKGVVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 622 GASAL---DHFTAAARQrygLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLrtdemlesiptfVEQVDAQaitlld 697
Cdd:PRK08008 194 THYNLrfaGYYSAWQCA---LRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVL------------LEKYSAR------ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 698 lptAFWNEwvVGLKTGTLT--MPSALRAIIiggeaVYPEQLVQWQRHAPDTL-------------------RLINTYGPT 756
Cdd:PRK08008 253 ---AFWGQ--VCKYRATITecIPMMIRTLM-----VQPPSANDRQHCLREVMfylnlsdqekdafeerfgvRLLTSYGMT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 757 ETTVVAtscdLQTQPADVAQLP-IGLPLAGVNALVLAAGDRPAAEGELVLL------GPTLAAGYIG-TEHTAFTLLAVG 828
Cdd:PRK08008 323 ETIVGI----IGDRPGDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEIcikgvpGKTIFKEYYLdPKATAKVLEADG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 829 DRHlpayrTGDR-VRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIvyPNGVR--RLVAFVATKE 905
Cdd:PRK08008 399 WLH-----TGDTgYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI--KDSIRdeAIKAFVVLNE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 499404633 906 GE-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK08008 472 GEtLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
460-955 |
4.04e-26 |
|
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: 114.30 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 VLTAIAKQAR-KNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL 538
Cdd:cd05906 15 LLLRAAERGPtKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 ------DPEQPRERQ-QHIIQIAGLRTIVTQAdyqhRLASVFSGAIVLAGH----------LLSSNAQAVALPtaeSREG 601
Cdd:cd05906 95 tvpptyDEPNARLRKlRHIWQLLGSPVVLTDA----ELVAEFAGLETLSGLpgirvlsieeLLDTAADHDLPQ---SRPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 602 QIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEE--VFATLTSGATLVLRTDEMLE 679
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVElhLRAVYLGCQQVHVPTEEILA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 680 SIPTFVEQVDAQAITLLDLPTAFW---NEWVVGLKTGTLTMpSALRAIIIGGEAVYPEQLVQWQR-HAPDTLR---LINT 752
Cdd:cd05906 248 DPLRWLDLIDRYRVTITWAPNFAFallNDLLEEIEDGTWDL-SSLRYLVNAGEAVVAKTIRRLLRlLEPYGLPpdaIRPA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 753 YGPTET---TVVATSCDLQTQPADVAQLPIGLPLAGVNALVLAAGDRPAAE---GELVLLGPTLAAGYIGT-EHTAFTLL 825
Cdd:cd05906 327 FGMTETcsgVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEgevGRLQVRGPVVTKGYYNNpEANAEAFT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 826 AVGdrhlpAYRTGDRVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDE--ACVQGIVYPNGVR-RLVAFVA 902
Cdd:cd05906 407 EDG-----WFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETeELAIFFV 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404633 903 TKEGEIDA-----RALKQRLS---SVLPPAMIPTDYrafHQLPKTGSNKVDRKRLLAEYHD 955
Cdd:cd05906 482 PEYDLQDAlsetlRAIRSVVSrevGVSPAYLIPLPK---EEIPKTSLGKIQRSKLKAAFEA 539
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
498-1044 |
1.38e-25 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 113.59 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 498 AALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLASvfsGAI 577
Cdd:PRK06060 45 EVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQP---SRV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 578 VLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKG-VEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNF--- 653
Cdd:PRK06060 122 AEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAaIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFayg 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 654 -------------DASIEEVFATLTSGATLVLRTD-EMLESIPTFVEQV-DAQAitlldlPTAFwnewvvglktgtltmp 718
Cdd:PRK06060 202 lgnsvwfplatggSAVINSAPVTPEAAAILSARFGpSVLYGVPNFFARViDSCS------PDSF---------------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 719 SALRAIIIGGEAVYP---EQLVQWQRHAPdtlrLINTYGPTET--TVVATSCDlQTQPADVAQLpigLPLAGVNALV--- 790
Cdd:PRK06060 260 RSLRCVVSAGEALELglaERLMEFFGGIP----ILDGIGSTEVgqTFVSNRVD-EWRLGTLGRV---LPPYEIRVVApdg 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 791 LAAGdrPAAEGELVLLGPTLAAGYIGTEHTaftLLAVGDrhlpAYRTGDRVRLE-KGHLLYLGRMDNEFKISGYRIQPGE 869
Cdd:PRK06060 332 TTAG--PGVEGDLWVRGPAIAKGYWNRPDS---PVANEG----WLDTRDRVCIDsDGWVTYRCRADDTEVIGGVNVDPRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 870 VEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDA---RALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVD 945
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAtIDGsvmRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 946 RKRL-------------LAEYHDDAPTQ---------------ALASETENRVSAIWQQ---------------ILGVS- 981
Cdd:PRK06060 483 RGALrkqsptkpiwelsLTEPGSGVRAQrddlsasnmtiaggnDGGATLRERLVALRQErqrlvvdavcaeaakMLGEPd 562
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404633 982 -GIQSRD-NFFELGGQSLQTIQIVNRLAAEFSVSIKVSDVFDHPQLSDFCRYLDDRLSQDENSVE 1044
Cdd:PRK06060 563 pWSVDQDlAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGHGRLK 627
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
468-946 |
1.44e-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: 112.59 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRD-----RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLdPEQ 542
Cdd:cd05970 27 AKEYPDKLALVWCDdageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA-THQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQ-QHIIQIAGLRTIVtqADYQHRLASVFSGAI---------VLAG-----------HLLSSNAQAVALPTAESREG 601
Cdd:cd05970 106 LTAKDiVYRIESADIKMIV--AIAEDNIPEEIEKAApecpskpklVWVGdpvpegwidfrKLIKNASPDFERPTANSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 602 --QIAYVMFTSGSTGLPKGVE-IGASALDHFtAAARQRYGLRAEDRVLQFAPFNFDASI-EEVFATLTSGATLVLRTDEM 677
Cdd:cd05970 184 geDILLVYFSSGTTGMPKMVEhDFTYPLGHI-VTAKYWQNVREGGLHLTVADTGWGKAVwGKIYGQWIAGAAVFVYDYDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 678 LESiPTFVEQVDAQAITLLDLPTAFWnEWVVGLKTGTLTMpSALRAIIIGGEAVYPEQLVQWQRHApdTLRLINTYGPTE 757
Cdd:cd05970 263 FDP-KALLEKLSKYGVTTFCAPPTIY-RFLIREDLSRYDL-SSLRYCTTAGEALNPEVFNTFKEKT--GIKLMEGFGQTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 758 TTV-VATSCDLQTQPADvaqlpIGLPLAGVNALVLAAGDRP---AAEGELVL-------LGptLAAGYI-GTEHTAFTLl 825
Cdd:cd05970 338 TTLtIATFPWMEPKPGS-----MGKPAPGYEIDLIDREGRSceaGEEGEIVIrtskgkpVG--LFGGYYkDAEKTAEVW- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 826 avgdrHLPAYRTGDRV-RLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGivYPNGVRRLV--AFVA 902
Cdd:cd05970 410 -----HDGYYHTGDAAwMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTG--VPDPIRGQVvkATIV 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 499404633 903 TKEGEIDARALKQRL----SSVLPPAMIPTDYRAFHQLPKTGSNKVDR 946
Cdd:cd05970 483 LAKGYEPSEELKKELqdhvKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
468-892 |
1.77e-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: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIAL--AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRE 545
Cdd:cd05904 15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 546 RQQHIIQIAGLRTIVTQADYQHRLASvFSGAIVLAGH---------LLSSNAQAVALPTAESREGQIAYVMFTSGSTGLP 616
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAEKLAS-LALPVVLLDSaefdslsfsDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 617 KGVeigasALDH--FTAA-----ARQRYGLRAEDRVLQFAPFnFD----ASIeeVFATLTSGATLVL--RTDemlesIPT 683
Cdd:cd05904 174 KGV-----MLTHrnLIAMvaqfvAGEGSNSDSEDVFLCVLPM-FHiyglSSF--ALGLLRLGATVVVmpRFD-----LEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 684 FVEQVDAQAITLLDL--PTafwnewVVGLKTGTLTMP---SALRAIIIGGEAVYPEQLVQWQRHAPDtLRLINTYGPTET 758
Cdd:cd05904 241 LLAAIERYKVTHLPVvpPI------VLALVKSPIVDKydlSSLRQIMSGAAPLGKELIEAFRAKFPN-VDLGQGYGMTES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 759 TVVATSCDLQTQpADVAQLPIGLPLAGVNA--------LVLAAGDRpaaeGELVLLGPTLAAGYIGT-EHTAFTLlaVGD 829
Cdd:cd05904 314 TGVVAMCFAPEK-DRAKYGSVGRLVPNVEAkivdpetgESLPPNQT----GELWIRGPSIMKGYLNNpEATAATI--DKE 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404633 830 RHLpayRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVqgIVYPN 892
Cdd:cd05904 387 GWL---HTGDLCYIdEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV--IPYPD 445
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
468-952 |
1.79e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 112.06 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQ 547
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 548 QHIIQIAGLRTIVTQADYQHRLASV------FSGAIVLAG--------HLLSSNAQAVALPTAESREgQIAYVMFTSGST 613
Cdd:PRK07470 97 AYLAEASGARAMICHADFPEHAAAVraaspdLTHVVAIGGaragldyeALVARHLGARVANAAVDHD-DPCWFFFTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 614 GLPKgveigASALDHFTAA-------ARQRYGLRAEDRVLQFAPFNFDASIEEVfATLTSGATLVLRTDEMLEsiptfve 686
Cdd:PRK07470 176 GRPK-----AAVLTHGQMAfvitnhlADLMPGTTEQDASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFD------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 687 qvdaqaitlldlPTAFW---NEWVVglkTGTLTMP-----------------SALRAIIIGGEAVYPEQlvqwQRHAPDT 746
Cdd:PRK07470 243 ------------PAEVWalvERHRV---TNLFTVPtilkmlvehpavdrydhSSLRYVIYAGAPMYRAD----QKRALAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 747 L--RLINTYGPTETT---VVATSCDLQTQPADVAQL-PIGLPLAGVNALVLAAGDR--PAAE-GELVLLGPTLAAGYIGT 817
Cdd:PRK07470 304 LgkVLVQYFGLGEVTgniTVLPPALHDAEDGPDARIgTCGFERTGMEVQIQDDEGRelPPGEtGEICVIGPAVFAGYYNN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 818 -EHTAFTLlavgdRHlPAYRTGDRVRLEKGHLLYL-GRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVR 895
Cdd:PRK07470 384 pEANAKAF-----RD-GWFRTGDLGHLDARGFLYItGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGE 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404633 896 RLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAE 952
Cdd:PRK07470 458 VGVAVCVARDGaPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
463-949 |
1.96e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 112.17 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIALAQR--DRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDP 540
Cdd:PRK12583 23 AFDATVARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 541 EQPRERQQHIIQIAGLRTIVTQA-----DYQHRLASV-------------------FSGAIVLAG---------HLLSSN 587
Cdd:PRK12583 103 AYRASELEYALGQSGVRWVICADafktsDYHAMLQELlpglaegqpgalacerlpeLRGVVSLAPapppgflawHELQAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 588 AQAVALPTAESREGQIAY-----VMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLqfAPFNFDASIEEVFA 662
Cdd:PRK12583 183 GETVSREALAERQASLDRddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC--VPVPLYHCFGMVLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 663 TL---TSGATLVLRTDEmLESIPTFVEQVDAQAITLLDLPTAFWNEwvvglktgtLTMP-------SALRAIIIGGEAVY 732
Cdd:PRK12583 261 NLgcmTVGACLVYPNEA-FDPLATLQAVEEERCTALYGVPTMFIAE---------LDHPqrgnfdlSSLRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 733 PEQL--VQWQRHAPDTLRlinTYGPTETTVVAtscdLQTQPADvaQLPIGLPLAGVN------ALVLAAGDR--PAAEGE 802
Cdd:PRK12583 331 IEVMrrVMDEMHMAEVQI---AYGMTETSPVS----LQTTAAD--DLERRVETVGRTqphlevKVVDPDGATvpRGEIGE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 803 LVLLGPTLAAGYIGT-EHTAFTLLAVGDRHlpayrTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEV 880
Cdd:PRK12583 402 LCTRGYSVMKGYWNNpEATAESIDEDGWMH-----TGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAV 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 881 DEACVQGIVYPNGVRRLVAFVATKEGEI-DARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK12583 477 ADVQVFGVPDEKYGEEIVAWVRLHPGHAaSEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
461-952 |
3.13e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 110.46 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 461 LTAIAKQARKNPSHIALAQR--DRQYSYQQLLGlsgqAAAALHERgVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL 538
Cdd:PRK07787 1 LASLNPAAVAAAADIADAVRigGRVLSRSDLAG----AATAVAER-VAGARRVAVLATPTLATVLAVVGALIAGVPVVPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 DPEQ-PRERqqhiiqiaglRTIVTQADYQHRLASVFSGAIVLAGHLLSSNAQAvALPTAESREGQIAYVMFTSGSTGLPK 617
Cdd:PRK07787 76 PPDSgVAER----------RHILADSGAQAWLGPAPDDPAGLPHVPVRLHARS-WHRYPEPDPDAPALIVYTSGTTGPPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 618 GVEIGASALDHFTAAARQRYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVlrtdEMLESIPTFVEQVDAQAITLL 696
Cdd:PRK07787 145 GVVLSRRAIAADLDALAEAWQWTADDVLVHGLPlFHVHGLVLGVLGPLRIGNRFV----HTGRPTPEAYAQALSEGGTLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 697 -DLPTAfWNEWVvglktGTLTMPSALRA--IIIGGEAVYP----EQLVQWQRHAPdtlrlINTYGPTETTV-VATSCDLQ 768
Cdd:PRK07787 221 fGVPTV-WSRIA-----ADPEAARALRGarLLVSGSAALPvpvfDRLAALTGHRP-----VERYGMTETLItLSTRADGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 769 TQPADVaqlpiGLPLAGVNA-LVLAAGDRPAAEGELV----LLGPTLAAGYIGT-EHTAFTLLAVGdrhlpAYRTGD-RV 841
Cdd:PRK07787 290 RRPGWV-----GLPLAGVETrLVDEDGGPVPHDGETVgelqVRGPTLFDGYLNRpDATAAAFTADG-----WFRTGDvAV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 842 RLEKGHLLYLGRMDNEF-KISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEgEIDARALKQRLSSV 920
Cdd:PRK07787 360 VDPDGMHRIVGRESTDLiKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGAD-DVAADELIDFVAQQ 438
|
490 500 510
....*....|....*....|....*....|..
gi 499404633 921 LPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAE 952
Cdd:PRK07787 439 LSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
481-957 |
2.67e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 108.25 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIV 560
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 561 TQADYQHRLAS-VFSGAIVL--------------AGHLLSSNAQAVA----LPTAESREG----QIAYVMFTSGSTGLPK 617
Cdd:PRK12406 89 AHADLLHGLASaLPAGVTVLsvptppeiaaayriSPALLTPPAGAIDwegwLAQQEPYDGppvpQPQSMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 618 GVEIGASALDHFTAAARQR---YGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLR----TDEMLESIP----TFVE 686
Cdd:PRK12406 169 GVRRAAPTPEQAAAAEQMRaliYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQprfdPEELLQLIErhriTHMH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 687 QVDAQAITLLDLPTAFWNEWVVglktgtltmpSALRAIIIGGEAVYPE---QLVQWQrhAPdtlrLIN-TYGPTETTVV- 761
Cdd:PRK12406 249 MVPTMFIRLLKLPEEVRAKYDV----------SSLRHVIHAAAPCPADvkrAMIEWW--GP----VIYeYYGSTESGAVt 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 762 -ATSCDLQTQPADVaqlpiGLPLAGVNALVLAAGDRPAAEGElvlLGPTL--AAGYigtehTAFTLLAVGDRHLPAYR-- 836
Cdd:PRK12406 313 fATSEDALSHPGTV-----GKAAPGAELRFVDEDGRPLPQGE---IGEIYsrIAGN-----PDFTYHNKPEKRAEIDRgg 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 837 ---TGDRVRLEKGHLLYLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDAR 911
Cdd:PRK12406 380 fitSGDVGYLDADGYLFLCDRKRDMVISgGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGaTLDEA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499404633 912 ALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDA 957
Cdd:PRK12406 460 DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANA 505
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
462-949 |
4.03e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 107.91 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 462 TAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPE 541
Cdd:PRK06164 14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 542 QPRERQQHIIQIAGLRTIVTQ------------ADYQH-------RLASVFSGAIVLAGHLLSSNAQAVALP------TA 596
Cdd:PRK06164 94 YRSHEVAHILGRGRARWLVVWpgfkgidfaailAAVPPdalpplrAIAVVDDAADATPAPAPGARVQLFALPdpappaAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 597 ESREGQ---IAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLr 673
Cdd:PRK06164 174 GERAADpdaGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVC- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 674 tdemlesIPTFVEQVDAQAITLLDLPTAFWNE--WVVGLKTGTLTMP-SALRAIIIGGEAVYPEQLVQW--QRHAPdtlr 748
Cdd:PRK06164 253 -------EPVFDAARTARALRRHRVTHTFGNDemLRRILDTAGERADfPSARLFGFASFAPALGELAALarARGVP---- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 749 LINTYGPTEttVVA-TSCDLQTQPADVAQLPIGLPL---AGVNAL------VLAAGdrpaAEGELVLLGPTLAAGYIGT- 817
Cdd:PRK06164 322 LTGLYGSSE--VQAlVALQPATDPVSVRIEGGGRPAspeARVRARdpqdgaLLPDG----ESGEIEIRAPSLMRGYLDNp 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 818 EHTAFTLLAVGdrhlpAYRTGDRVRLE-KGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYpNGVRR 896
Cdd:PRK06164 396 DATARALTDDG-----YFRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATR-DGKTV 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404633 897 LVAFVATKEGE-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGS---NKVDRKRL 949
Cdd:PRK06164 470 PVAFVIPTDGAsPDEAGLMAACREALAGFKVPARVQVVEAFPVTESangAKIQKHRL 526
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
446-947 |
7.95e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 106.89 E-value: 7.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 446 ALITSREPEPFVEPVLTAIAK-QARKNPSHIAL--AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETI 522
Cdd:PRK05852 3 FMGGAAPMASDFGPRIADLVEvAATRLPEAPALvvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 523 ISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQAD--YQHRLASV--------------FSGAIVLAgHLLSS 586
Cdd:PRK05852 83 VALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADgpHDRAEPTTrwwpltvnvggdsgPSGGTLSV-HLDAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 587 NAQAVALPTAESREGQIAYVMFTSGSTGLPKGV-----EIGASAldHFTAAArqrYGLRAEDRVLQFAP-FNFDASIEEV 660
Cdd:PRK05852 162 TEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVpwthaNIASSV--RAIITG---YRLSPRDATVAVMPlYHGHGLIAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 661 FATLTSGATLVLRTDEMLeSIPTFVEQVDAQAIT-----------LLDLPTafwnewvvglKTGTLTMPSALRAIIIGGE 729
Cdd:PRK05852 237 LATLASGGAVLLPARGRF-SAHTFWDDIKAVGATwytavptihqiLLERAA----------TEPSGRKPAALRFIRSCSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 730 AVYPE--QLVQWQRHAPdtlrLINTYGPTETTVVATSCDL----QTQPADVAQLPIGLPLAGVNALVLAAGDR--PAAEG 801
Cdd:PRK05852 306 PLTAEtaQALQTEFAAP----VVCAFGMTEATHQVTTTQIegigQTENPVVSTGLVGRSTGAQIRIVGSDGLPlpAGAVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 802 ELVLLGPTLAAGYIGTehTAFTLLAVGDRHLpayRTGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEV 880
Cdd:PRK05852 382 EVWLRGTTVVRGYLGD--PTITAANFTDGWL---RTGDLGSLSAaGDLSIRGRIKELINRGGEKISPERVEGVLASHPNV 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 881 DEACVQGI---VYPNGVRRLVafVATKEGEIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRK 947
Cdd:PRK05852 457 MEAAVFGVpdqLYGEAVAAVI--VPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
459-953 |
1.74e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 106.16 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 459 PVLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL 538
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 DPEQPRERQQHIIQIAGLRTIVTQADYQHRLASV---FSGAIVLAGHLLSSNAQAVALPTAE--------------SREG 601
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALppdLGRLRAWGGNPDDDEPSGSTDETLDdliagsstaplpkpPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 602 QIayVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFnFDASieeVFATLTS----GATLVLRTD-- 675
Cdd:PRK07788 210 GI--VILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPM-FHAT---GWAHLTLamalGSTVVLRRRfd 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 676 -------------EMLESIPTFVEQvdaqaitLLDLPTAFWNEWVVglktgtltmpSALRAIIIGGEAVYPEqLVqwqRH 742
Cdd:PRK07788 284 peatlediakhkaTALVVVPVMLSR-------ILDLGPEVLAKYDT----------SSLKIIFVSGSALSPE-LA---TR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 743 APDTL--RLINTYGPTETTV--VATSCDLQTQPADVAQLPIGLPLAgvnalVLAAGDRPAAEGEL--VLLGPTLA-AGYI 815
Cdd:PRK07788 343 ALEAFgpVLYNLYGSTEVAFatIATPEDLAEAPGTVGRPPKGVTVK-----ILDENGNEVPRGVVgrIFVGNGFPfEGYT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 816 GTEH--TAFTLLAVGDR-HLPayrtgdrvrlEKGHLLYLGRmDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYP 891
Cdd:PRK07788 418 DGRDkqIIDGLLSSGDVgYFD----------EDGLLFVDGR-DDDMIVSgGENVFPAEVEDLLAGHPDVVEAAVIGVDDE 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404633 892 NGVRRLVAFVATKEGE-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVdRKRLLAEY 953
Cdd:PRK07788 487 EFGQRLRAFVVKAPGAaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKV-LKRELREM 548
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
462-949 |
4.87e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 104.31 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 462 TAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPE 541
Cdd:PRK13383 39 TLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 542 QPRERQQHIIQIAGLRTIVTQADYQHRLASVFSGAIVL----AGHLLSSNAQAVALPtaesreGQIayVMFTSGSTGLPK 617
Cdd:PRK13383 119 FRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIdpatAGAEESGGRPAVAAP------GRI--VLLTSGTTGKPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 618 GVE--------IGASAldhfTAAARQRygLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRT--DEMLESIPTFVEQ 687
Cdd:PRK13383 191 GVPrapqlrsaVGVWV----TILDRTR--LRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRhfDAEAALAQASLHR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 688 VDAQAIT------LLDLPTAFwnewvvglkTGTLTMPSaLRAIIIGGEAVYPEQLVQWQRHAPDTLrlINTYGPTETTV- 760
Cdd:PRK13383 265 ADAFTAVpvvlarILELPPRV---------RARNPLPQ-LRVVMSSGDRLDPTLGQRFMDTYGDIL--YNGYGSTEVGIg 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 761 -VATSCDLQTQPADVaqlpiGLPLAGVNALVLAAGDRPAA---EGELVLLGPTLAAGYIGTEHTAftllaVGDrhlPAYR 836
Cdd:PRK13383 333 aLATPADLRDAPETV-----GKPVAGCPVRILDRNNRPVGprvTGRIFVGGELAGTRYTDGGGKA-----VVD---GMTS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 837 TGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALK 914
Cdd:PRK13383 400 TGDMGYLdNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGsGVDAAQLR 479
|
490 500 510
....*....|....*....|....*....|....*
gi 499404633 915 QRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK13383 480 DYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
468-947 |
1.10e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 103.93 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYV---PLDPEQPR 544
Cdd:PRK05605 42 VARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAHEL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 545 ERQ-------------------QHIIQIAGLRTIVT---------------------QADYQHRLASVFSGAI---VLAG 581
Cdd:PRK05605 122 EHPfedhgarvaivwdkvaptvERLRRTTPLETIVSvnmiaampllqrlalrlpipaLRKARAALTGPAPGTVpweTLVD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 582 HLLSSNAQAVALPTAESREgqIAYVMFTSGSTGLPKGVEigasaLDH---FTAAARQRY---GLRAED-RVLQFAPFnFD 654
Cdd:PRK05605 202 AAIGGDGSDVSHPRPTPDD--VALILYTSGTTGKPKGAQ-----LTHrnlFANAAQGKAwvpGLGDGPeRVLAALPM-FH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 655 A---SIEEVFATLTsGATLVL----RTDEMLESI----PTFVEQVDaqaiTLLDLPTAFWNEWVVGLktgtltmpSALRA 723
Cdd:PRK05605 274 AyglTLCLTLAVSI-GGELVLlpapDIDLILDAMkkhpPTWLPGVP----PLYEKIAEAAEERGVDL--------SGVRN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 724 IIIGGEAVYPEQLVQWQRHAPDtlRLINTYGPTETTVVATScdlqtQPADVAQLP--IGLPLAGVNALVL----AAGDRP 797
Cdd:PRK05605 341 AFSGAMALPVSTVELWEKLTGG--LLVEGYGLTETSPIIVG-----NPMSDDRRPgyVGVPFPDTEVRIVdpedPDETMP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 798 AAE-GELVLLGPTLAAGYIGT-EHTAFTLLAvgdrhlPAYRTGDRVRLEK-GHLLYLGRMdNEFKIS-GYRIQPGEVEAH 873
Cdd:PRK05605 414 DGEeGELLVRGPQVFKGYWNRpEETAKSFLD------GWFRTGDVVVMEEdGFIRIVDRI-KELIITgGFNVYPAEVEEV 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404633 874 LLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRK 947
Cdd:PRK05605 487 LREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAaLDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
3-427 |
1.28e-22 |
|
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: 101.90 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLwLGHAL-NDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpeigFVASQLPV 81
Cdd:cd19543 3 PLSPMQEGM-LFHSLlDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQ----VVLKDRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 82 PIGVLPIVELLPApmtDEEQTIRQWARDEISLPLDLLNGLPCRFAL--LCGEKRDFLYSCvHHIALDGFGTTMLFQRIAQ 159
Cdd:cd19543 78 PWRELDLSHLSEA---EQEAELEALAEEDRERGFDLARAPLMRLTLirLGDDRYRLVWSF-HHILLDGWSLPILLKELFA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 160 IYTALTAGQSAPVAEFGPFSAVLEEERQRDAsgqtAQARDFWLETLNAMPEPASFSEKKAPIAA---RFLRQSCDMPADL 236
Cdd:cd19543 154 IYAALGEGQPPSLPPVRPYRDYIAWLQRQDK----EAAEAYWREYLAGFEEPTPLPKELPADADgsyEPGEVSFELSAEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 237 WQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNR------IGSaslMVpSMQMNIVPLCIQVDEQANFV 310
Cdd:cd19543 230 TARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRpaelpgIET---MV-GLFINTLPVRVRLDPDQTVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 311 ALAQQVARTKRTLRRHQHYryehlrrDLNRVGGEQRLFGPLI-NIMPFDhplNYGSLSSSTLNLSAGPVE---------- 379
Cdd:cd19543 306 ELLKDLQAQQLELREHEYV-------PLYEIQAWSEGKQALFdHLLVFE---NYPVDESLEEEQDEDGLRitdvsaeeqt 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 499404633 380 --DLTIEIHfkPDGTPVLDFDANPACYSAEALASLQETLFTLLQRWLAQP 427
Cdd:cd19543 376 nyPLTVVAI--PGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
483-923 |
1.38e-22 |
|
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: 102.93 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 483 QYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTI-VT 561
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALfVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 QADYQHRLASVFSGAIVLAGHLLSSNA---------QAVALPTAESR---EGQIAYVMFTSGSTGLPKGVEIGASALDHF 629
Cdd:cd05932 86 KLDDWKAMAPGVPEGLISISLPPPSAAncqyqwddlIAQHPPLEERPtrfPEQLATLIYTSGTTGQPKGVMLTFGSFAWA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 630 TAAARQRYGLRAEDRVLQFAPFnfdASI-EEVF---ATLTSGATLVLrtdemLESIPTFVEQVDAQAITLLDLPTAFWNE 705
Cdd:cd05932 166 AQAGIEHIGTEENDRMLSYLPL---AHVtERVFvegGSLYGGVLVAF-----AESLDTFVEDVQRARPTLFFSVPRLWTK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 706 WVVGL--KTGTLTMPSALRAIIIG---------------------GEAVYPEQLVQWQRHApdTLRLINTYGPTETTVVA 762
Cdd:cd05932 238 FQQGVqdKIPQQKLNLLLKIPVVNslvkrkvlkglgldqcrlagcGSAPVPPALLEWYRSL--GLNILEAYGMTENFAYS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 763 TSCdlqtQPADVAQLPIGLPLAGVNalvlaagDRPAAEGELVLLGPTLAAG-YIGTEHTAFTLLAVGdrhlpAYRTGDRV 841
Cdd:cd05932 316 HLN----YPGRDKIGTVGNAGPGVE-------VRISEDGEILVRSPALMMGyYKDPEATAEAFTADG-----FLRTGDKG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 842 RL-EKGHLLYLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQG--------IVYPNGVRRLVAFVAT-KEGEIDA 910
Cdd:cd05932 380 ELdADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGsglpaplaLVVLSEEARLRADAFArAELEASL 459
|
490
....*....|...
gi 499404633 911 RALKQRLSSVLPP 923
Cdd:cd05932 460 RAHLARVNSTLDS 472
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
463-960 |
1.96e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 102.70 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQ 542
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQQHIIQIAGLRTIVTQADyqhrLASVFSGAIVLAGHLLS---------------------SNAQAVALPTAESREG 601
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPA----LAPTAEAALALLPVDTLilslvlggreapggwldfadwAEAGSVAEPDVELADD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 602 QIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIeEVFAT--LTSGATLVL----RTD 675
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQL-DVFLGpyLYVGATNVIldapDPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 676 EMLESIptfveqvDAQAITLLDLPTAFWnewvVGLktgtLTMP-------SALRAIIIGGEAVYPEQLVQWQRHAPDtLR 748
Cdd:PRK08316 251 LILRTI-------EAERITSFFAPPTVW----ISL----LRHPdfdtrdlSSLRKGYYGASIMPVEVLKELRERLPG-LR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 749 LINTYGPTETTVVATScdlqTQPADVAQLP--IGLPLAGVNALVLAAGDRPAAE---GELVLLGPTLAAGYIG-TEHTAf 822
Cdd:PRK08316 315 FYNCYGQTEIAPLATV----LGPEEHLRRPgsAGRPVLNVETRVVDDDGNDVAPgevGEIVHRSPQLMLGYWDdPEKTA- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 823 tllavgdrhlPAYR-----TGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRR 896
Cdd:PRK08316 390 ----------EAFRggwfhSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 897 LVAFVATKEG-EIDARAL----KQRLSSV-LPPAMIPTDyrafhQLPKTGSNKVdRKRLLAEYHDDAPTQ 960
Cdd:PRK08316 460 VTAVVVPKAGaTVTEDELiahcRARLAGFkVPKRVIFVD-----ELPRNPSGKI-LKRELRERYAGAFTD 523
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
603-951 |
3.35e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 99.73 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 603 IAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGlrAEDRVLQFAPFNFDASIEEVFATLTSGAT-LVLRTDEMLEsI 681
Cdd:PRK07824 37 VALVVATSGTTGTPKGAMLTAAALTASADATHDRLG--GPGQWLLALPAHHIAGLQVLVRSVIAGSEpVELDVSAGFD-P 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 682 PTFVEQVDA-------------QAITLLDLPTAfwnewvvglkTGTLtmpSALRAIIIGGEAVYPEQLvqwQRHAPDTLR 748
Cdd:PRK07824 114 TALPRAVAElgggrrytslvpmQLAKALDDPAA----------TAAL---AELDAVLVGGGPAPAPVL---DAAAAAGIN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 749 LINTYGPTETtvvATSC--DlqtqpadvaqlpiGLPLAGVNALVlaagdrpaAEGELVLLGPTLAAGYIGT-EHTAFTLl 825
Cdd:PRK07824 178 VVRTYGMSET---SGGCvyD-------------GVPLDGVRVRV--------EDGRIALGGPTLAKGYRNPvDPDPFAE- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 826 avgdrhlPA-YRTGDRVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATK 904
Cdd:PRK07824 233 -------PGwFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGD 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 499404633 905 EGEIDA-RALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLA 951
Cdd:PRK07824 306 GGPAPTlEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
603-946 |
3.90e-22 |
|
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: 98.87 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 603 IAYVMFTSGSTGLPKGVEIGA----SALDHFTAAARQrygLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMl 678
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANktffAVPDILQKEGLN---WVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 679 eSIPTFVEQVDAQAITLLDLPTAFWNEWVVGLKTGTLTMPSaLRAIIIGGEAVYpEQLVQWQRHAPDTlRLINTYGPTET 758
Cdd:cd17635 79 -TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPS-LRLIGYGGSRAI-AADVRFIEATGLT-NTAQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 759 TvvaTSCDLQTQPADVAQLPIGLPLAGVNALVLA---AGDRPAAEGELVLLGPTLAAGYIGTEHTAFTLLAVGdrhlpAY 835
Cdd:cd17635 155 G---TALCLPTDDDSIEINAVGRPYPGVDVYLAAtdgIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG-----WV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 836 RTGDRVRLEKGHLLYL-GRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVyPNGVRRLVAFVATKEGEID---AR 911
Cdd:cd17635 227 NTGDLGERREDGFLFItGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIS-DEEFGELVGLAVVASAELDenaIR 305
|
330 340 350
....*....|....*....|....*....|....*
gi 499404633 912 ALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDR 946
Cdd:cd17635 306 ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
463-1028 |
4.14e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 103.71 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIAL------AQRDRQYSYQQLLGLSGQAAAALHERGVkPGERIGIMLNRSPETIISLLAVMQCGAVYV 536
Cdd:PRK05691 14 ALQRRAAQTPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFGCLYAGVIAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 537 PLDP-----EQPRERQQHIIQIAGLRTIVTQADYQHRLASVFSGAIVLAGHLLSSNA---------QAVALPtaesrEGQ 602
Cdd:PRK05691 93 PAYPpesarRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTldpalaeawQEPALQ-----PDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 603 IAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYG--LRAEDRVLQFAPFNFDAS-IEEVFATLTSGATLVL------- 672
Cdd:PRK05691 168 IAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLmspayfl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 673 -RTDEMLESI----------PTF-----VEQVDAQAITLLDLptafwnewvvglktgtltmpSALRAIIIGGEAVYPEQL 736
Cdd:PRK05691 248 eRPLRWLEAIseyggtisggPDFayrlcSERVSESALERLDL--------------------SRWRVAYSGSEPIRQDSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 737 VQW-QRHAP---DTLRLINTYGPTETT-----------VVATSCDLQTQPADVAQLPIGLPLAG---------------V 786
Cdd:PRK05691 308 ERFaEKFAAcgfDPDSFFASYGLAEATlfvsggrrgqgIPALELDAEALARNRAEPGTGSVLMScgrsqpghavlivdpQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 787 NALVLAAGdrpaAEGELVLLGPTLAAGYI-GTEHTAFTLLAVGDRHLpaYRTGDRVRLEKGHLLYLGRMDNEFKISGYRI 865
Cdd:PRK05691 388 SLEVLGDN----RVGEIWASGPSIAHGYWrNPEASAKTFVEHDGRTW--LRTGDLGFLRDGELFVTGRLKDMLIVRGHNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 866 QPGEVEAHLlaQPEVDEacvqgivypngVR--RLVAFVATKEGEID---ARALKQRLSSVLPP-AMIPTDYR----AFHQ 935
Cdd:PRK05691 462 YPQDIEKTV--EREVEV-----------VRkgRVAAFAVNHQGEEGigiAAEISRSVQKILPPqALIKSIRQavaeACQE 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 936 ------------LPKTGSNKVDRK----RL------------LAEYHDDAPTQALASETENRVSAIWQQILGVSGIQSRD 987
Cdd:PRK05691 529 apsvvlllnpgaLPKTSSGKLQRSacrlRLadgsldsyalfpALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADD 608
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 499404633 988 NFFELGGQSLQTIQIVNRLAAEFSVSIKVSDVFDHPQLSDF 1028
Cdd:PRK05691 609 HFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAF 649
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
463-963 |
1.54e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 100.41 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIAL-----AQRDRQ---YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCG-- 532
Cdd:PRK07529 30 LLSRAAARHPDAPALsflldADPLDRpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGia 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 533 -AVYVPLDPEQPRErqqhIIQIAGLRTIVT-----QADYQHRLASVFSGA-----IV---LAGHLLSSNAQAVALPTAES 598
Cdd:PRK07529 110 nPINPLLEPEQIAE----LLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALpelrtVVevdLARYLPGPKRLAVPLIRRKA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 599 REGQIAY------------------------VMF-TSGSTGLPK------GVEIgasaLDHFTAAARQRYGlraEDRVLq 647
Cdd:PRK07529 186 HARILDFdaelarqpgdrlfsgrpigpddvaAYFhTGGTTGMPKlaqhthGNEV----ANAWLGALLLGLG---PGDTV- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 648 FAP---FNFDASIEEVFATLTSGATLVL------RTDEMLESIPTFVEQVDAQAITLLdlPTAFwnewvvglkTGTLTMP 718
Cdd:PRK07529 258 FCGlplFHVNALLVTGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGV--PTVY---------AALLQVP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 719 ------SALRAIIIGGEAVYPEQLVQWQRHApdTLRLINTYGPTETTVVaTSCDlqtqPADVAQLP--IGLPLAG--VNA 788
Cdd:PRK07529 327 vdghdiSSLRYALCGAAPLPVEVFRRFEAAT--GVRIVEGYGLTEATCV-SSVN----PPDGERRIgsVGLRLPYqrVRV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 789 LVLAAGDR------PAAEGELVLLGPTLAAGYIGTEHTAFtlLAVGDRHLpayRTGDRVRL-EKGHLLYLGRMDNEFKIS 861
Cdd:PRK07529 400 VILDDAGRylrdcaVDEVGVLCIAGPNVFSGYLEAAHNKG--LWLEDGWL---NTGDLGRIdADGYFWLTGRAKDLIIRG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 862 GYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLP-PAMIPTDYRAFHQLPKT 939
Cdd:PRK07529 475 GHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGaSATEAELLAFARDHIAeRAAVPKHVRILDALPKT 554
|
570 580
....*....|....*....|....
gi 499404633 940 GSNKVDRKRLLAEYHDDAPTQALA 963
Cdd:PRK07529 555 AVGKIFKPALRRDAIRRVLRAALR 578
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
603-944 |
1.76e-21 |
|
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: 96.80 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 603 IAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPF----NFDASIeevFATLTSGATLVlrtDEML 678
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhtfGYKAGI---VACLLTGATVV---PVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 679 ESIPTFVEQVDAQAITLL-DLPTAFWNEWVV-GLKTGTLtmpSALRAIIIGGEAVyPEQLVQWQRHAPDTLRLINTYGPT 756
Cdd:cd17638 76 FDVDAILEAIERERITVLpGPPTLFQSLLDHpGRKKFDL---SSLRAAVTGAATV-PVELVRRMRSELGFETVLTAYGLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 757 ETtVVATSCDLQTQPADVAQlPIGLPLAGVNAlvlaagdRPAAEGELVLLGPTLAAGYI-GTEHTAFTLLAVGDRHlpay 835
Cdd:cd17638 152 EA-GVATMCRPGDDAETVAT-TCGRACPGFEV-------RIADDGEVLVRGYNVMQGYLdDPEATAEAIDADGWLH---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 836 rTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIvyPNgvRRL----VAFVATKEGE-ID 909
Cdd:cd17638 219 -TGDVGELdERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGV--PD--ERMgevgKAFVVARPGVtLT 293
|
330 340 350
....*....|....*....|....*....|....*....
gi 499404633 910 ARAL----KQRLSSVlppaMIPTDYRAFHQLPKTGSNKV 944
Cdd:cd17638 294 EEDViawcRERLANY----KVPRFVRFLDELPRNASGKV 328
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
472-945 |
1.87e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 99.57 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII 551
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADYQHRLASVF---------------SGAIVLAGHLlsSNAQAVALPTAE----SREGQIAYVMFTSGS 612
Cdd:PRK07798 97 DDSDAVALVYEREFAPRVAEVLprlpklrtlvvvedgSGNDLLPGAV--DYEDALAAGSPErdfgERSPDDLYLLYTGGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 613 TGLPKGV--------EIGASALDHFTAAARQRYGLRAED-------RVLQFAPFNFDASIEEVFATLTSGATLVLRTDEM 677
Cdd:PRK07798 175 TGMPKGVmwrqedifRVLLGGRDFATGEPIEDEEELAKRaaagpgmRRFPAPPLMHGAGQWAAFAALFSGQTVVLLPDVR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 678 L--ESIPTFVEQVDAQAITLL-DlptAFWNEWVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTLrLINTYG 754
Cdd:PRK07798 255 FdaDEVWRTIEREKVNVITIVgD---AMARPLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVV-LTDSIG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 755 PTET----TVVATSCDLQTQPADVAqlpiglplAGVNALVLAAGDRPAAEGE----LVLLGPTLAAGYIG-TEHTAFTLL 825
Cdd:PRK07798 331 SSETgfggSGTVAKGAVHTGGPRFT--------IGPRTVVLDEDGNPVEPGSgeigWIARRGHIPLGYYKdPEKTAETFP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 826 AVGDRH--LPayrtGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVA 902
Cdd:PRK07798 403 TIDGVRyaIP----GDRARVEAdGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 499404633 903 TKEG-EIDARALKQRLSSVLPPAMIPtdyRAFH---QLPKTGSNKVD 945
Cdd:PRK07798 479 LREGaRPDLAELRAHCRSSLAGYKVP---RAIWfvdEVQRSPAGKAD 522
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
605-946 |
2.67e-21 |
|
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: 95.94 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 605 YVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTF 684
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 685 VEQVDAQAITLLdlPTafwnewVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDtLRLINTYGPTETTVVATS 764
Cdd:cd17633 84 INQYNATVIYLV--PT------MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPK-ANLIEFYGTSELSFITYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 765 CDLQTQPAdvaqLPIGLPLAGVNALVLAAGDRpaAEGELVLLGPTLAAGYI-GTEHTAFTLLAVGDRhlpAYRTgdrvrl 843
Cdd:cd17633 155 FNQESRPP----NSVGRPFPNVEIEIRNADGG--EIGKIFVKSEMVFSGYVrGGFSNPDGWMSVGDI---GYVD------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 844 EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKegEIDARALKQRLSSVLPP 923
Cdd:cd17633 220 EEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--KLTYKQLKRFLKQKLSR 297
|
330 340
....*....|....*....|...
gi 499404633 924 AMIPTDYRAFHQLPKTGSNKVDR 946
Cdd:cd17633 298 YEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
482-952 |
3.51e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 97.92 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEqprerqqhiIQIAGLRTIVT 561
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG---------MGRKNLKQCLQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 QADYQhrlasVFSGaivlaghllssnaqavalptaESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRA 641
Cdd:cd05910 72 EAEPD-----AFIG---------------------IPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 642 EDRVLQ-FAPFNfdasieeVFATLTSGATLVLRTDemlesiPTFVEQVDAQAI----------TLLDLPtAFWNEWVVGL 710
Cdd:cd05910 126 GEVDLAtFPLFA-------LFGPALGLTSVIPDMD------PTRPARADPQKLvgairqygvsIVFGSP-ALLERVARYC 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 711 KTGTLTMPSaLRAIIIGGEAVYPEQLVQWQRHAPDTLRLINTYGPTETTVVAT--SCDLQTQ----PADVAQLPIGLPLA 784
Cdd:cd05910 192 AQHGITLPS-LRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEALPVSSigSRELLATttaaTSGGAGTCVGRPIP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 785 GVNALVLAAGDRPAAE------------GELVLLGPTLAAGYIG-TEHTAFTLLAVGDrHLPAYRTGDRVRL-EKGHLLY 850
Cdd:cd05910 271 GVRVRIIEIDDEPIAEwddtlelprgeiGEITVTGPTVTPTYVNrPVATALAKIDDNS-EGFWHRMGDLGYLdDEGRLWF 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 851 LGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSVLppAMIPTDY 930
Cdd:cd05910 350 CGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALA--KDYPHTQ 427
|
490 500
....*....|....*....|....*....
gi 499404633 931 RA----FHQLPKTG---SNKVDRKRLLAE 952
Cdd:cd05910 428 RIgrflIHPSFPVDirhNAKIFREKLAVW 456
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
465-952 |
4.35e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 98.67 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 465 AKQARKNPSHIALA-QRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:PRK06087 30 QQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 RERQQHIIQIAGLR-----TIVTQADY-------QHRLAS----VF-------SGAIVLAgHLLSSNAQAVALPTAESRE 600
Cdd:PRK06087 110 EAELVWVLNKCQAKmffapTLFKQTRPvdlilplQNQLPQlqqiVGvdklapaTSSLSLS-QIIADYEPLTTAITTHGDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 601 gqIAYVMFTSGSTGLPKGVeigasALDHFTAAARQRY-----GLRAEDRVLQFAPFNFDAS-IEEVFATLTSGATLVLRT 674
Cdd:PRK06087 189 --LAAVLFTSGTEGLPKGV-----MLTHNNILASERAycarlNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 675 DEMLEsipTFVEQVDAQAITLLDLPTAFWNEWVVGLKTGTLTMPSaLRAIIIGGeAVYPEQLVQ--WQRHapdtLRLINT 752
Cdd:PRK06087 262 IFTPD---ACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSA-LRFFLCGG-TTIPKKVARecQQRG----IKLLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 753 YGPTET---TVVatscdlqtQPADVAQLPI---GLPLAGVNALVLaAGDR----PAAEGELVLLGPTLAAGYIGT-EHTA 821
Cdd:PRK06087 333 YGSTESsphAVV--------NLDDPLSRFMhtdGYAAAGVEIKVV-DEARktlpPGCEGEEASRGPNVFMGYLDEpELTA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 822 FTLLAVGdrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAF 900
Cdd:PRK06087 404 RALDEEG-----WYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAY 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499404633 901 VATKEG-------EIDARALKQRLSSVLPPAMIPTdyraFHQLPKTGSNKVdRKRLLAE 952
Cdd:PRK06087 479 VVLKAPhhsltleEVVAFFSRKRVAKYKYPEHIVV----IDKLPRTASGKI-QKFLLRK 532
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
3-425 |
7.11e-21 |
|
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: 96.68 E-value: 7.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpEIgfvasqLPVP 82
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQ-EI------LPPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPIVELlPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:cd19539 76 PAPLEVRDL-SDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGrFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAEF-GPFSAVLEEERQRDASGQTAQARDFWLETLNAMPEPASFSEKKAPiaARFLR----QSCDMPADL 236
Cdd:cd19539 155 AARRKGPAAPLPELrQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPTALPTDRPRP--AGFPYpgadLRFELDAEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 237 WQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFVALaqqV 316
Cdd:cd19539 233 VAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDL---I 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 317 ARTKRTL---RRHQHYRYEHL------RRDLNRVGGEQRLFGpLINIMPFDHPLNYGSLSSSTLNLSAGPVEDLTIEIHF 387
Cdd:cd19539 310 ARVRKALvdaQRHQELPFQQLvaelpvDRDAGRHPLVQIVFQ-VTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTE 388
|
410 420 430
....*....|....*....|....*....|....*...
gi 499404633 388 KPDGTpVLDFDANPACYSAEALASLQETLFTLLqRWLA 425
Cdd:cd19539 389 EGTGL-RGSLGYATSLFDEETIQGFLADYLQVL-RQLL 424
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
492-949 |
1.77e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 96.78 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 492 LSGQAAA---ALHER-GVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQH 567
Cdd:PRK05620 44 IGARAAAlahALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 568 RLASVFSG-----AIVLAGHLLSSNAQAVALP--TAESREGQI-----------------AYVMFTSGSTGLPKGVEIGA 623
Cdd:PRK05620 124 QLGEILKEcpcvrAVVFIGPSDADSAAAHMPEgiKVYSYEALLdgrstvydwpeldettaAAICYSTGTTGAPKGVVYSH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 624 SALdhftaaARQRYGLRAEDR--VLQFAPFNFDASIEEV------FATLTSGATLVLrTDEMLeSIPTFVEQV-DAQAIT 694
Cdd:PRK05620 204 RSL------YLQSLSLRTTDSlaVTHGESFLCCVPIYHVlswgvpLAAFMSGTPLVF-PGPDL-SAPTLAKIIaTAMPRV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 695 LLDLPTAFWNEWVVGLKTGTLTMpsALRAIIIGGEAVYPEQLVQW-QRHAPDtlrLINTYGPTETTVVATscdLQTQPAD 773
Cdd:PRK05620 276 AHGVPTLWIQLMVHYLKNPPERM--SLQEIYVGGSAVPPILIKAWeERYGVD---VVHVWGMTETSPVGT---VARPPSG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 774 VA------------QLPIGLPLAGVN-ALVLAAGDRpaAEGELVLLGPTLAAGYI--------GTEHTaFTLLAV--GDR 830
Cdd:PRK05620 348 VSgearwayrvsqgRFPASLEYRIVNdGQVMESTDR--NEGEIQVRGNWVTASYYhspteeggGAAST-FRGEDVedAND 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 831 HLPA---YRTGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG 906
Cdd:PRK05620 425 RFTAdgwLRTGDVGSVTRdGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPG 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 499404633 907 ----EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK05620 505 ieptRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
482-949 |
3.84e-20 |
|
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: 95.28 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVt 561
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 qadyqhrlasVFSGAIVLAGHllSSNaqavalPTaesregqiayVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRA 641
Cdd:cd17647 98 ----------VIRAAGVVVGP--DSN------PT----------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 642 EDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNEWVVGLKTgtlTMPSAL 721
Cdd:cd17647 150 NDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATT---PFPKLH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 722 RAIIIgGEAVYPEQLVQWQRHAPDtLRLINTYGPTETTVVATSCDLQTQPADVAQL-------PIGLPLAGVNALVLAAG 794
Cdd:cd17647 227 HAFFV-GDILTKRDCLRLQTLAEN-VRIVNMYGTTETQRAVSYFEVPSRSSDPTFLknlkdvmPAGRGMLNVQLLVVNRN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 795 DRP-----AAEGELVLLGPTLAAGYIGT----------------EHTAFTLLAVG-----------DRhlpAYRTGDRVR 842
Cdd:cd17647 305 DRTqicgiGEVGEIYVRAGGLAEGYRGLpelnkekfvnnwfvepDHWNYLDKDNNepwrqfwlgprDR---LYRTGDLGR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 843 -LEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEV------------DEACVQGIVYPNGVRRLVAFVATKEGEID 909
Cdd:cd17647 382 yLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVrenitlvrrdkdEEPTLVSYIVPRFDKPDDESFAQEDVPKE 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 499404633 910 ARA----------------LKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd17647 462 VSTdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
457-952 |
4.94e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 95.49 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 457 VEPVLTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYV 536
Cdd:PRK06710 23 IQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 537 ---PLDPEQPRERQQH-------------IIQIAGLRT-------IVTQ-ADY------------QHRLASVF-----SG 575
Cdd:PRK06710 103 qtnPLYTERELEYQLHdsgakvilcldlvFPRVTNVQSatkiehvIVTRiADFlpfpknllypfvQKKQSNLVvkvseSE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 576 AIVLAGHLLSSNAQAVALPTaeSREGQIAYVMFTSGSTGLPKGVeigasALDHFTAAARQRYGLR-------AEDRVLQF 648
Cdd:PRK06710 183 TIHLWNSVEKEVNTGVEVPC--DPENDLALLQYTGGTTGFPKGV-----MLTHKNLVSNTLMGVQwlynckeGEEVVLGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 649 APFNFDASIEEVF-ATLTSGATLVLrtdemlesIPTF-----VEQVDAQAITLL-DLPTAFwnewvVGLKTGTLTMP--- 718
Cdd:PRK06710 256 LPFFHVYGMTAVMnLSIMQGYKMVL--------IPKFdmkmvFEAIKKHKVTLFpGAPTIY-----IALLNSPLLKEydi 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 719 SALRAIIiGGEAVYPEQlVQWQRHAPDTLRLINTYGPTETTVVATSCDLQTQpadvaQLP--IGLPLAGVNALV--LAAG 794
Cdd:PRK06710 323 SSIRACI-SGSAPLPVE-VQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEK-----RVPgsIGVPWPDTEAMImsLETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 795 D--RPAAEGELVLLGPTLAAGYIGTEHTAFTLLAVGDRHlpayrTGDRVRLEKGHLLYL-GRMDNEFKISGYRIQPGEVE 871
Cdd:PRK06710 396 EalPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLH-----TGDVGYMDEDGFFYVkDRKKDMIVASGFNVYPREVE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 872 AHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEI-DARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLL 950
Cdd:PRK06710 471 EVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTEcSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLI 550
|
..
gi 499404633 951 AE 952
Cdd:PRK06710 551 EE 552
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
464-949 |
6.60e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 94.54 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAAL-HERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQ 542
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQQHIIQIAGLRTIVTQADYQHRLASVFSGA-----IVLAGHLLSSNAQAVAL-PTAESREGQIAYvmfTSGSTGLP 616
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSyvqrvISITSLKEIEDRKIDNFvEKNESASFIICY---TSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 617 KGVEIgaSALDHFTAAARQRYG--LRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVL----RTDEMLESIPTfvEQVd 689
Cdd:PRK06839 165 KGAVL--TQENMFWNALNNTFAidLTMHDRSIVLLPlFHIGGIGLFAFPTLFAGGVIIVprkfEPTKALSMIEK--HKV- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 690 aqaITLLDLPTAfwNEWVVGLKTGTLTMPSALRAIIIGGeAVYPEQLVqwqRHAPDT-LRLINTYGPTET--TVVATSCD 766
Cdd:PRK06839 240 ---TVVMGVPTI--HQALINCSKFETTNLQSVRWFYNGG-APCPEELM---REFIDRgFLFGQGFGMTETspTVFMLSEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 767 lqtqpaDVAQLP--IGLPLAGVNALVL--AAGDRPAAE-GELVLLGPTLAAGYIGTEHTAFTLLAVGDRHlpayrTGDRV 841
Cdd:PRK06839 311 ------DARRKVgsIGKPVLFCDYELIdeNKNKVEVGEvGELLIRGPNVMKEYWNRPDATEETIQDGWLC-----TGDLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 842 RL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSS 919
Cdd:PRK06839 380 RVdEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSvLIEKDVIEHCRL 459
|
490 500 510
....*....|....*....|....*....|
gi 499404633 920 VLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK06839 460 FLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
463-950 |
2.41e-19 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 93.39 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 463 AIAKQARKNPSHIAL------AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGA--- 533
Cdd:cd05966 58 CLDRHLKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhs 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 534 -VYVPLDPEQPRERqqhiIQIAGLRTIVTqADYQHR--------------LASVFSGAIVLA-----------------G 581
Cdd:cd05966 138 vVFAGFSAESLADR----INDAQCKLVIT-ADGGYRggkviplkeivdeaLEKCPSVEKVLVvkrtggevpmtegrdlwW 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 582 HLLSSNAQAVALPTAESREgQIAYVMFTSGSTGLPKGVEigasaldHFT------AAARQRYglraedrvlqfapfNFDA 655
Cdd:cd05966 213 HDLMAKQSPECEPEWMDSE-DPLFILYTSGSTGKPKGVV-------HTTggyllyAATTFKY--------------VFDY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 656 SIEEVFAT-----------------LTSGATLVlrtdeMLESIPT------FVEQVDAQAITLL-DLPTA------FWNE 705
Cdd:cd05966 271 HPDDIYWCtadigwitghsyivygpLANGATTV-----MFEGTPTypdpgrYWDIVEKHKVTIFyTAPTAiralmkFGDE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 706 WVVGLKTgtltmpSALRaiIIG--GEAVYPEQLVQWQRHAPDT-LRLINTYGPTET-TVVATSCdlqtqPADVAQLP--I 779
Cdd:cd05966 346 WVKKHDL------SSLR--VLGsvGEPINPEAWMWYYEVIGKErCPIVDTWWQTETgGIMITPL-----PGATPLKPgsA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 780 GLPLAGVNALVLAAGDRPAA---EGELVLLGPtlaagYIGTEHTAFtllavGD--RHLPAY--------RTGDRVRLEK- 845
Cdd:cd05966 413 TRPFFGIEPAILDEEGNEVEgevEGYLVIKRP-----WPGMARTIY-----GDheRYEDTYfskfpgyyFTGDGARRDEd 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 846 GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGivYPNGVR--RLVAFVATKEGEIDARALKQRL----SS 919
Cdd:cd05966 483 GYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVG--RPHDIKgeAIYAFVTLKDGEEPSDELRKELrkhvRK 560
|
570 580 590
....*....|....*....|....*....|.
gi 499404633 920 VLPPAMIPTDYRAFHQLPKTGSNKVDRkRLL 950
Cdd:cd05966 561 EIGPIATPDKIQFVPGLPKTRSGKIMR-RIL 590
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
3-340 |
2.77e-19 |
|
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: 91.65 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEhAEQpeigFVASQLPVP 82
Cdd:cd19531 3 PLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGE-PVQ----VILPPLPLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 igvLPIVELLPAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:cd19531 78 ---LPVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLrLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 162 TALTAGQSAPVAE----FGPFSAvleEERQRDASGQTAQARDFWLETLNAMPE----------PA--SFSekkapiAArf 225
Cdd:cd19531 155 AAFLAGRPSPLPPlpiqYADYAV---WQREWLQGEVLERQLAYWREQLAGAPPvlelptdrprPAvqSFR------GA-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 226 lRQSCDMPADLWQPLSALCEGNKISwpdLFLAMLAThLKLV----SGSDRLTFGMMVMNR--------IGsasLMVpsmq 293
Cdd:cd19531 224 -RVRFTLPAELTAALRALARREGAT---LFMTLLAA-FQVLlhrySGQDDIVVGTPVAGRnraeleglIG---FFV---- 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 499404633 294 mNIVPLCIQVDEQANFVALaqqVARTKRTLRR---HQHYRYEHL------RRDLNR 340
Cdd:cd19531 292 -NTLVLRTDLSGDPTFREL---LARVRETALEayaHQDLPFEKLvealqpERDLSR 343
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
439-949 |
3.80e-19 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 92.51 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 439 LREERELALITSREPEPFVEPVLTAIAkqARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRS 518
Cdd:PRK13382 26 MRPDRYLRIVAAMRREGMGPTSGFAIA--AQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 519 PETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLASVFSGA-----IV-------LAGHLLSS 586
Cdd:PRK13382 104 RGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCpqatrIVawtdedhDLTVEVLI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 587 NAQAVALPTAESREGQIayVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAEDRVLQFAP-FNFDASIEEVFATLT 665
Cdd:PRK13382 184 AAHAGQRPEPTGRKGRV--ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPmFHAWGFSQLVLAASL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 666 SgATLVLRTDEMLESIPTFVEQVDAQAIT--------LLDLPTAFWNEWvvglktgtltMPSALRAIIIGGEAVYPEQLV 737
Cdd:PRK13382 262 A-CTIVTRRRFDPEATLDLIDRHRATGLAvvpvmfdrIMDLPAEVRNRY----------SGRSLRFAAASGSRMRPDVVI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 738 QWQRHAPDTLrlINTYGPTETTVVATSC--DLQTQPaDVAqlpiGLPLAGVNALVLAAGDRPAAEGELvllgptlaaGYI 815
Cdd:PRK13382 331 AFMDQFGDVI--YNNYNATEAGMIATATpaDLRAAP-DTA----GRPAEGTEIRILDQDFREVPTGEV---------GTI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 816 ----GTEHTAFTLLAVGDRHLPAYRTGDRVRL-EKGHLLYLGRmDNEFKISG-YRIQPGEVEAHLLAQPEVDEACVQGIV 889
Cdd:PRK13382 395 fvrnDTQFDGYTSGSTKDFHDGFMASGDVGYLdENGRLFVVGR-DDEMIVSGgENVYPIEVEKTLATHPDVAEAAVIGVD 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404633 890 YPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK13382 474 DEQYGQRLAAFVVLKPGaSATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
459-949 |
6.43e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 93.06 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 459 PVLTAIAKQARKNPSHIALAQ-RDRQYSYQQLLGLSgQAAAALHERGVKPGERIGIMLnrsPETIISLLAVMQC---GAV 534
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADsTGGELSYGKALTGA-LALARLLKRELKDEENVGILL---PPSVAGALANLALllaGKV 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 535 YVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRL-ASVFSGAIVLAGHLL---------SSNAQAVALPTA-------- 596
Cdd:PRK08633 692 PVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLkNKGFDLELPENVKVIyledlkakiSKVDKLTALLAArllparll 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 597 ESREGQ------IAYVMFTSGSTGLPKGVEigasaLDHFT-----AAARQRYGLRAEDRVLQ----FAPFNFDASIeevF 661
Cdd:PRK08633 772 KRLYGPtfkpddTATIIFSSGSEGEPKGVM-----LSHHNilsniEQISDVFNLRNDDVILSslpfFHSFGLTVTL---W 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 662 ATLTSGATLVLRTDemlesiPTFVEQVdAQAIT------LLDLPTaFWNEWVVGLKTGTLtMPSALRAIIIGGEAVYPEQ 735
Cdd:PRK08633 844 LPLLEGIKVVYHPD------PTDALGI-AKLVAkhratiLLGTPT-FLRLYLRNKKLHPL-MFASLRLVVAGAEKLKPEV 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 736 LVQWQRHApdTLRLINTYGPTETTVVAtSCDL-QTQPADVAQLP------IGLPLAGV--------NALVLAAGdrpaAE 800
Cdd:PRK08633 915 ADAFEEKF--GIRILEGYGATETSPVA-SVNLpDVLAADFKRQTgskegsVGMPLPGVavrivdpeTFEELPPG----ED 987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 801 GELVLLGPTLAAGYIGT-EHTAFTL-LAVGDRHlpaYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVE---AHL 874
Cdd:PRK08633 988 GLILIGGPQVMKGYLGDpEKTAEVIkDIDGIGW---YVTGDKGHLdEDGFLTITDRYSRFAKIGGEMVPLGAVEeelAKA 1064
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404633 875 LAQPEVdEACVQGIvyPNGVR--RLVafVATKEGEIDARALKQRLS-SVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK08633 1065 LGGEEV-VFAVTAV--PDEKKgeKLV--VLHTCGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
447-918 |
1.03e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 91.26 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 447 LITSREPEPFVEPVLT-AIAKQARKNPSHIALAQRD------RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSP 519
Cdd:PRK12582 37 VIKSRHPLGPYPRSIPhLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 520 ETIISLLAVMQCGAVYVPLDPE------------------QPR----------ERQQHIIQIAGLRTIVTQADYQHRLAS 571
Cdd:PRK12582 117 EHALMTLAAMQAGVPAAPVSPAyslmshdhaklkhlfdlvKPRvvfaqsgapfARALAALDLLDVTVVHVTGPGEGIASI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 572 VFsgAIVLAGHLLSSNAQAVALPTAESregqIAYVMFTSGSTGLPKGVeIGASALdhFTAAARQRYGLRAEDR------V 645
Cdd:PRK12582 197 AF--ADLAATPPTAAVAAAIAAITPDT----VAKYLFTSGSTGMPKAV-INTQRM--MCANIAMQEQLRPREPdppppvS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 646 LQFAPFNFDASIEEVF-ATLTSGATLVLrtDEMlESIPTFVEQvdaqaiTLLDL----PTAFWNEWV-VGLKTGTLTMPS 719
Cdd:PRK12582 268 LDWMPWNHTMGGNANFnGLLWGGGTLYI--DDG-KPLPGMFEE------TIRNLreisPTVYGNVPAgYAMLAEAMEKDD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 720 ALRA-------IIIGGEAVYPEQLVQ-WQRHAPDT----LRLINTYGPTETTVVATSCDLQTQPADVaqlpIGLPLAGVN 787
Cdd:PRK12582 339 ALRRsffknlrLMAYGGATLSDDLYErMQALAVRTtghrIPFYTGYGATETAPTTTGTHWDTERVGL----IGLPLPGVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 788 ALVLAAGDRPaaegELVLLGPTLAAGYIGT-EHTAftllAVGDRHlPAYRTGDRVRL------EKGhLLYLGRMDNEFKI 860
Cdd:PRK12582 415 LKLAPVGDKY----EVRVKGPNVTPGYHKDpELTA----AAFDEE-GFYRLGDAARFvdpddpEKG-LIFDGRVAEDFKL 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404633 861 -SGYRIQPGEVEAHLLA--QPEVDEACVQG--------IVYPN--GVRRLVAFVATKEGEIDAR-----ALKQRLS 918
Cdd:PRK12582 485 sTGTWVSVGTLRPDAVAacSPVIHDAVVAGqdrafiglLAWPNpaACRQLAGDPDAAPEDVVKHpavlaILREGLS 560
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
456-959 |
1.56e-18 |
|
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: 90.84 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 456 FVEPVLT----AIAKQARK-NPSHIAL------AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIIS 524
Cdd:cd05967 44 FVGGRLNtcynALDRHVEAgRGDQIALiydspvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 525 LLAVMQCGAVY-VPLDPEQPRERQQHIiQIAGLRTIVTqADYQHRLASV------FSGAIVLAGH-------LLSSNAQA 590
Cdd:cd05967 124 MLACARIGAIHsVVFGGFAAKELASRI-DDAKPKLIVT-ASCGIEPGKVvpykplLDKALELSGHkphhvlvLNRPQVPA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 591 VA------------LPTAESRE------GQIAYVMFTSGSTGLPKGV--EIG--ASALdhfTAAARQRYGLRAEDrVLqf 648
Cdd:cd05967 202 DLtkpgrdldwselLAKAEPVDcvpvaaTDPLYILYTSGTTGKPKGVvrDNGghAVAL---NWSMRNIYGIKPGD-VW-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 649 apfnFDAS----------IeeVFATLTSGATLVlrtdeMLESIPTFVEQvdaqaitlldlPTAFW---NEWVVglkTGTL 715
Cdd:cd05967 276 ----WAASdvgwvvghsyI--VYGPLLHGATTV-----LYEGKPVGTPD-----------PGAFWrviEKYQV---NALF 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 716 TMPSALRAI---------------------IIGGEAVYPEQLvQWqrhAPDTLR--LINTYGPTET-TVVATSCdlqtqp 771
Cdd:cd05967 331 TAPTAIRAIrkedpdgkyikkydlsslrtlFLAGERLDPPTL-EW---AENTLGvpVIDHWWQTETgWPITANP------ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 772 ADVAQLPI-----GLPLAGVNALVLAAGDRPAA---EGELVLLGPtLAAGYIGT---EHTAFTLLAVGDrHLPAYRTGDR 840
Cdd:cd05967 401 VGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGpneLGNIVIKLP-LPPGCLLTlwkNDERFKKLYLSK-FPGYYDTGDA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 841 -VRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRL- 917
Cdd:cd05967 479 gYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGvKITAEELEKELv 558
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 499404633 918 ---SSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDAPT 959
Cdd:cd05967 559 alvREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYT 603
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3-421 |
1.63e-18 |
|
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: 89.44 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLY-CQFVEVAGEHAEQpeigfvasqlpv 81
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRtCFFTDPEDGEPMQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 82 piGVL--PIVELLPAPMTDEEQtirqwARDEI----SLPLDLLNGLPCRFALLC-GEKRDFLYSCVHHIALDGFGTTMLF 154
Cdd:cd19532 71 --GVLasSPLRLEHVQISDEAE-----VEEEFerlkNHVYDLESGETMRIVLLSlSPTEHYLIFGYHHIAMDGVSFQIFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 155 QRIAQIYTALTagQSAPVAEFGPFSavleeERQRDA--SGQTAQARDFWLETLNAMPEP------ASFSEKKAPIAARFL 226
Cdd:cd19532 144 RDLERAYNGQP--LLPPPLQYLDFA-----ARQRQDyeSGALDEDLAYWKSEFSTLPEPlpllpfAKVKSRPPLTRYDTH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 227 RQSCDMPADLWQPLSALCEGNKISwP-DLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDE 305
Cdd:cd19532 217 TAERRLDAALAARIKEASRKLRVT-PfHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 306 QANFVALAQQVARTKRTLRRHQHYRYEHLRRDLN-----------------RVG-GEQRLFGplinimpfdhplnyGSLS 367
Cdd:cd19532 296 SQTFADVLKETRDKAYAALAHSRVPFDVLLDELGvprsathsplfqvfinyRQGvAESRPFG--------------DCEL 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 499404633 368 SSTLNLSAGPVEDLTIEIHFKPDGTPVLDFDANPACYSAEALASLQETLFTLLQ 421
Cdd:cd19532 362 EGEEFEDARTPYDLSLDIIDNPDGDCLLTLKVQSSLYSEEDAELLLDSYVNLLE 415
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
453-949 |
2.21e-18 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 89.89 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 453 PEPFVE-------PVLTAIAKQARKNPSHIAL--AQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETII 523
Cdd:cd17642 5 PGPFYPledgtagEQLHKAMKRYASVPGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 524 SLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLASVFS------GAIVLAG---------------- 581
Cdd:cd17642 85 PVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKklkiikTIIILDSkedykgyqclytfitq 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 582 HLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIG-ASALDHFTAAARQRYG--LRAEDRVLQFAPFNFDASIE 658
Cdd:cd17642 165 NLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLThKNIVARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 659 EVFATLTSGATLVLrtdemlesIPTFVEQVDAQAI------TLLDLPTAFwnewvVGLKTGTLTMP---SALRAIIIGGE 729
Cdd:cd17642 245 TTLGYLICGFRVVL--------MYKFEEELFLRSLqdykvqSALLVPTLF-----AFFAKSTLVDKydlSNLHEIASGGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 730 AVYPE--QLVQWQRHAPdTLRliNTYGPTETT-VVATSCDLQTQPADVAQLpigLPLAGVNALVLAAGDR--PAAEGELV 804
Cdd:cd17642 312 PLSKEvgEAVAKRFKLP-GIR--QGYGLTETTsAILITPEGDDKPGAVGKV---VPFFYAKVVDLDTGKTlgPNERGELC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 805 LLGPTLAAGYIGTEHTAFTLLaVGDRHLpayRTGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEA 883
Cdd:cd17642 386 VKGPMIMKGYVNNPEATKALI-DKDGWL---HSGDIAYYDEdGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDA 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404633 884 CVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPA-MIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd17642 462 GVAGIPDEDAGELPAAVVVLEAGKtMTEKEVMDYVASQVSTAkRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
468-853 |
2.55e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 89.96 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALA----------QRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVP 537
Cdd:PRK09274 16 AQERPDQLAVAvpggrgadgkLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 538 LDPEQPRERQQHIIQIAGLRTIVTQADYQ-------------HRLASV----FSGAIVLAGhlLSSNAQAVALPTAESRE 600
Cdd:PRK09274 96 VDPGMGIKNLKQCLAEAQPDAFIGIPKAHlarrlfgwgkpsvRRLVTVggrlLWGGTTLAT--LLRDGAAAPFPMADLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 601 GQIAYVMFTSGSTGLPKGVeigASALDHFTA---AARQRYGLRAEDRVLQ-FAPFN-FDASIeevfatltsGATLVLrtD 675
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGV---VYTHGMFEAqieALREDYGIEPGEIDLPtFPLFAlFGPAL---------GMTSVI--P 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 676 EMLESIPTFV------EQVDAQAITLLDLPTAFWNewVVG--LKTGTLTMPSaLRAIIIGGEAVYPEQLVQWQRHAPDTL 747
Cdd:PRK09274 240 DMDPTRPATVdpaklfAAIERYGVTNLFGSPALLE--RLGryGEANGIKLPS-LRRVISAGAPVPIAVIERFRAMLPPDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 748 RLINTYGPTET---TVVATSCDLQTQPADVAQLP---IGLPLAGVNALVLAAGDRPAAE------------GELVLLGPT 809
Cdd:PRK09274 317 EILTPYGATEAlpiSSIESREILFATRAATDNGAgicVGRPVDGVEVRIIAISDAPIPEwddalrlatgeiGEIVVAGPM 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 499404633 810 LAAGYIGTEHTafTLLA------VGDRHlpayRTGDRVRL-EKGHLLYLGR 853
Cdd:PRK09274 397 VTRSYYNRPEA--TRLAkipdgqGDVWH----RMGDLGYLdAQGRLWFCGR 441
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
464-972 |
2.99e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 89.45 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGI-MLNRsPETIISLLAVMQCGAVYVPLDPEQ 542
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLIlMLNR-TEFVESVLAANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQQHIIQIAGLRTIVTQADYQHRLASV------FSGAIVLAG----------HLLSSNAQAVALptAESREGQIAYV 606
Cdd:PRK07786 102 TPPEIAFLVSDCGAHVVVTEAALAPVATAVrdivplLSTVVVAGGssddsvlgyeDLLAEAGPAHAP--VDIPNDSPALI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 607 MFTSGSTGLPKGveigaSALDHFTAAARQRYGLRA------EDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLEs 680
Cdd:PRK07786 180 MYTSGTTGRPKG-----AVLTHANLTGQAMTCLRTngadinSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFD- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 681 iPT-FVEQVDAQAITLLDLPTAFWNewVVGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRHAPDTLrLINTYGPTETT 759
Cdd:PRK07786 254 -PGqLLDVLEAEKVTGIFLVPAQWQ--AVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQ-ILAAFGQTEMS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 760 VVatSCDLQTQPADVAQLPIGLPLAGVNALVL--AAGDRPAAE-GELVLLGPTLAAGYIGTEHTAFTLLAVGDRHlpayr 836
Cdd:PRK07786 330 PV--TCMLLGEDAIRKLGSVGKVIPTVAARVVdeNMNDVPVGEvGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH----- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 837 TGDRVRLEKGHLLYLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG--EIDARAL 913
Cdd:PRK07786 403 SGDLVRQDEEGYVWVVDRKKDMIISgGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdaALTLEDL 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499404633 914 KQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDAPTQALASETENRVSA 972
Cdd:PRK07786 483 AEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNVERRSASAGFTERR 541
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
435-948 |
4.83e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.16 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 435 LGRWLREereLALITSREPEPfvePVL--TAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIG 512
Cdd:PRK08279 18 LPGILRG---LKRTALITPDS---KRSlgDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 513 IMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLAS------------VFSGAIVLA 580
Cdd:PRK08279 92 LLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEaradlarpprlwVAGGDTLDD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 581 GHLLSS-NAQAVALPTA--ESREG----QIAYVMFTSGSTGLPKgveigASALDH--FTAAARQRYGL---RAEDRVLQF 648
Cdd:PRK08279 172 PEGYEDlAAAAAGAPTTnpASRSGvtakDTAFYIYTSGTTGLPK-----AAVMSHmrWLKAMGGFGGLlrlTPDDVLYCC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 649 APF---NfdASIEEVFATLTSGATLVLRtdemlesiPTF--------VEQVDAQAIT--------LLDLPtafwnewvvg 709
Cdd:PRK08279 247 LPLyhnT--GGTVAWSSVLAAGATLALR--------RKFsasrfwddVRRYRATAFQyigelcryLLNQP---------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 710 lktgtltmPSA------LRAIIigGEAVYPEQLVQWQ-RHAPDtlRLINTYGPTETTV-----------VATSCDLQTQP 771
Cdd:PRK08279 307 --------PKPtdrdhrLRLMI--GNGLRPDIWDEFQqRFGIP--RILEFYAASEGNVgfinvfnfdgtVGRVPLWLAHP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 772 ADVAQLPI--GLPLAGVNALVlaagdRPAAEGEL-VLLGPTLAA----GYIGTEHTAFTLL----AVGDRHlpaYRTGDR 840
Cdd:PRK08279 375 YAIVKYDVdtGEPVRDADGRC-----IKVKPGEVgLLIGRITDRgpfdGYTDPEASEKKILrdvfKKGDAW---FNTGDL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 841 VRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYP--NGVRRLVAFVATKEGEIDARALKQRL 917
Cdd:PRK08279 447 MRDdGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPgtDGRAGMAAIVLADGAEFDLAALAAHL 526
|
570 580 590
....*....|....*....|....*....|....
gi 499404633 918 SSVLPPAMIPTDYRAFHQLPKTG---SNKVDRKR 948
Cdd:PRK08279 527 YERLPAYAVPLFVRLVPELETTGtfkYRKVDLRK 560
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
472-955 |
7.94e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 88.01 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 472 PSHIALAQRD-RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHI 550
Cdd:PRK07514 16 RDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 551 IQIAGLRTIV---TQADYQHRLASVFSGAIVL------AGHLLSSNAQA-VALPTAESREGQIAYVMFTSGSTGLPKGve 620
Cdd:PRK07514 96 IGDAEPALVVcdpANFAWLSKIAAAAGAPHVEtldadgTGSLLEAAAAApDDFETVPRGADDLAAILYTSGTTGRSKG-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 621 igaSALDH----FTAAARQRY-GLRAEDRVLQFAP-FN----FDASieevFATLTSGATLVLR----TDEMLESIPtfve 686
Cdd:PRK07514 174 ---AMLSHgnllSNALTLVDYwRFTPDDVLIHALPiFHthglFVAT----NVALLAGASMIFLpkfdPDAVLALMP---- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 687 qvdaQAITLLDLPTaFwneWVVGLKTGTLTMPSA--LRAIIIGGEAVYPEQLVQWQR---HApdtlrLINTYGPTEtTVV 761
Cdd:PRK07514 243 ----RATVMMGVPT-F---YTRLLQEPRLTREAAahMRLFISGSAPLLAETHREFQErtgHA-----ILERYGMTE-TNM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 762 ATScdlqtQPADVAQLP--IGLPLAGVNALVLAAGD-RPAAEGELVLL---GPTLAAGYIGT-EHTAFTLLAVGdrhlpA 834
Cdd:PRK07514 309 NTS-----NPYDGERRAgtVGFPLPGVSLRVTDPETgAELPPGEIGMIevkGPNVFKGYWRMpEKTAEEFRADG-----F 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 835 YRTGDRVRL-EKGHLLYLGRmDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYPN---GVRRLVafVATKEGEID 909
Cdd:PRK07514 379 FITGDLGKIdERGYVHIVGR-GKDLIISgGYNVYPKEVEGEIDELPGVVESAVIGVPHPDfgeGVTAVV--VPKPGAALD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 499404633 910 ARALKQRLSSVLPPAMIPTdyRAF--HQLPKTGSNKVDRKRLLAEYHD 955
Cdd:PRK07514 456 EAAILAALKGRLARFKQPK--RVFfvDELPRNTMGKVQKNLLREQYAD 501
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
482-949 |
9.02e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 88.19 E-value: 9.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQpRERQ-QHIIQIAGLRTIV 560
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIF-RERElSFMLKHAESKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 561 TQA-----DY--------------QHRLASVFSGAIVLAGHLLS---SNAQAVALPTAESREG--QIAYVMFTSGSTGLP 616
Cdd:PRK13295 133 VPKtfrgfDHaamarrlrpelpalRHVVVVGGDGADSFEALLITpawEQEPDAPAILARLRPGpdDVTQLIYTSGTTGEP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 617 KGVEIGASALDHFTAAARQRYGLRAEDRVLQFAPfnfdasieevFATLTS-----------GATLVLR----TDEMLESI 681
Cdd:PRK13295 213 KGVMHTANTLMANIVPYAERLGLGADDVILMASP----------MAHQTGfmyglmmpvmlGATAVLQdiwdPARAAELI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 682 PTfveqvdaQAITLLDLPTAFWNEWVVGLKTGTLTMPSaLRAIIIGGEAVyPEQLVQWQRHAPDTlRLINTYGPTETTVV 761
Cdd:PRK13295 283 RT-------EGVTFTMASTPFLTDLTRAVKESGRPVSS-LRTFLCAGAPI-PGALVERARAALGA-KIVSAWGMTENGAV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 762 ATscdlqTQPADVAQLPI---GLPLAGVNALVLAAGDRP---AAEGELVLLGPTLAAGYIGTEHTAFTlLAVGdrhlpAY 835
Cdd:PRK13295 353 TL-----TKLDDPDERASttdGCPLPGVEVRVVDADGAPlpaGQIGRLQVRGCSNFGGYLKRPQLNGT-DADG-----WF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 836 RTGDRVRLE-KGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGivYPNgvRRL----VAFVATKEGE-ID 909
Cdd:PRK13295 422 DTGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVA--YPD--ERLgeraCAFVVPRPGQsLD 497
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 499404633 910 ARALKQRLSSV-LPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK13295 498 FEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1-358 |
2.91e-17 |
|
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: 85.58 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 1 MKPLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEHAEQpeigFVASQLP 80
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQ----VVHRQAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 81 VPIGVLPIvellpAPMTDEEQTIRQWARDEISLPLDLLNGLPCRFALLC--GEKRDFLYSCVHHIALDGFGTTMLFQRIA 158
Cdd:cd19536 77 VPVTELDL-----TPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRkdERERFLLVISDHHSILDGWSLYLLVKEIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 159 QIYTALTAGQS---APVAEFGPFSAVLEEERQRDASGQtaqardFWLETLNAMPEPASFSEKKAPIAARFLRQSCDMPAD 235
Cdd:cd19536 152 AVYNQLLEYKPlslPPAQPYRDFVAHERASIQQAASER------YWREYLAGATLATLPALSEAVGGGPEQDSELLVSVP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 236 LWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRI----GSASLMvpSMQMNIVPLCIQVDEQaNFVA 311
Cdd:cd19536 226 LPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSeettGAERLL--GLFLNTLPLRVTLSEE-TVED 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 499404633 312 LAQQVARTKRTLRRHQHYRYehlrRDLNRVGGEQRLFGPLINIMPFD 358
Cdd:cd19536 303 LLKRAQEQELESLSHEQVPL----ADIQRCSEGEPLFDSIVNFRHFD 345
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
32-427 |
9.56e-17 |
|
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: 83.51 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 32 FDGKVDIDAMLSAIRQAVMECECLYCQFVEVageHAEQPEIGFVASQLPVPIGVLpivellpapmTDEEQTIRQWARDEI 111
Cdd:cd19542 30 LDSSVDVERLRNAWRQLVQRHDILRTVFVES---SAEGTFLQVVLKSLDPPIEEV----------ETDEDSLDALTRDLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 112 SLPlDLLNGLPCRFALLCGEK-RDFLYSCVHHIALDGFGTTMLFQRIAQIYtaltagQSAPVAEFGPFSAVLEEERQRDA 190
Cdd:cd19542 97 DDP-TLFGQPPHRLTLLETSSgEVYLVLRISHALYDGVSLPIILRDLAAAY------NGQLLPPAPPFSDYISYLQSQSQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 191 SgqtaQARDFWLETLN---AMPEPASFSEKKApiaarflRQSCDMPADLWQPLSALCEGNKISWPDLFLAMLATHLKLVS 267
Cdd:cd19542 170 E----ESLQYWRKYLQgasPCAFPSLSPKRPA-------ERSLSSTRRSLAKLEAFCASLGVTLASLFQAAWALVLARYT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 268 GSDRLTFGMMVMNRigsaSLMVPSMQ------MNIVPLCIQVDEQANFVALAQQVARTKRTLRRHQHYRYEHLRRDLNRV 341
Cdd:cd19542 239 GSRDVVFGYVVSGR----DLPVPGIDdivgpcINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLW 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 342 GGEQrLFGPLINIMPF-DHP-LNYGSLSSSTLNLSAGPVE-DLTIEIhFKPDGTPVLDFDANPACYSAEALASLQETLFT 418
Cdd:cd19542 315 PSGT-LFNTLVSYQNFeASPeSELSGSSVFELSAAEDPTEyPVAVEV-EPSGDSLKVSLAYSTSVLSEEQAEELLEQFDD 392
|
....*....
gi 499404633 419 LLQRWLAQP 427
Cdd:cd19542 393 ILEALLANP 401
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
484-916 |
4.80e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 82.10 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQiaglrtivtqa 563
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILN----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 dyqhrlasvfsgaivlaghllssNAQAVALPTaeSREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAED 643
Cdd:cd05914 77 -----------------------HSEAKAIFV--SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 644 RVLQFAPFN--FDASIEEVFATLTsGATLVLRTD--------------EMLESIPTFVEQVDAQAITLLDLPTAFWNEWV 707
Cdd:cd05914 132 KILSILPLHhiYPLTFTLLLPLLN-GAHVVFLDKipsakiialafaqvTPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 708 VGLKTGTLTMPSA------------LRAIIIGGEAVYPEQLvqwqrhapDTLRLIN-----TYGPTETTVVATScdlqTQ 770
Cdd:cd05914 211 LAKKINNRKIRKLafkkvheafggnIKEFVIGGAKINPDVE--------EFLRTIGfpytiGYGMTETAPIISY----SP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 771 PADVAQLPIGLPLAGVNALVlAAGDRPAAEGELVLLGPTLAAGYIGT-EHTAFTLLAVGdrhlpAYRTGDRVRLEKGHLL 849
Cdd:cd05914 279 PNRIRLGSAGKVIDGVEVRI-DSPDPATGEGEIIVRGPNVMKGYYKNpEATAEAFDKDG-----WFHTGDLGKIDAEGYL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404633 850 YL-GRMDNEFKI-SGYRIQPGEVEAHLLAQPEVDEACVqgivypnGVR--RLVAFVATKEGEIDARALKQR 916
Cdd:cd05914 353 YIrGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLV-------VVQekKLVALAYIDPDFLDVKALKQR 416
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
481-950 |
7.16e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 82.50 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGA----VYVPLDPEQPRERqqhiIQIAGL 556
Cdd:PRK00174 96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAvhsvVFGGFSAEALADR----IIDAGA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 557 RTIVTqADYQHRlasvfSGAIVLaghlLSSNA-QAVALPTA-----------------ESR--------EGQIAY----- 605
Cdd:PRK00174 172 KLVIT-ADEGVR-----GGKPIP----LKANVdEALANCPSvekvivvrrtggdvdwvEGRdlwwhelvAGASDEcepep 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 606 --------VMFTSGSTGLPKGVEigasaldHFT------AAARQRYglraedrVlqfapfnFDASIEEVF---------- 661
Cdd:PRK00174 242 mdaedplfILYTSGSTGKPKGVL-------HTTggylvyAAMTMKY-------V-------FDYKDGDVYwctadvgwvt 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 662 -------ATLTSGATLVlrtdeMLESIPT------FVEQVDAQAITLLdlptafwnewvvglktgtLTMPSALRAIIIGG 728
Cdd:PRK00174 301 ghsyivyGPLANGATTL-----MFEGVPNypdpgrFWEVIDKHKVTIF------------------YTAPTAIRALMKEG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 729 EAVYpeqlvqwQRHAPDTLRLINTYG----P-----------------------TETTVVATScdlqTQPADVAQLP--I 779
Cdd:PRK00174 358 DEHP-------KKYDLSSLRLLGSVGepinPeawewyykvvggercpivdtwwqTETGGIMIT----PLPGATPLKPgsA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 780 GLPLAGVNA-LVLAAGDR--PAAEGELVLLGPtlaagYIGTEHTAFtllavGD----------RHLPAYRTGD-RVRLEK 845
Cdd:PRK00174 427 TRPLPGIQPaVVDEEGNPleGGEGGNLVIKDP-----WPGMMRTIY-----GDherfvktyfsTFKGMYFTGDgARRDED 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 846 GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGivYPNGVR--RLVAFVATKEGEIDARALKQRL----SS 919
Cdd:PRK00174 497 GYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVG--RPDDIKgqGIYAFVTLKGGEEPSDELRKELrnwvRK 574
|
570 580 590
....*....|....*....|....*....|.
gi 499404633 920 VLPPAMIPTDYRAFHQLPKTGSNKVDRkRLL 950
Cdd:PRK00174 575 EIGPIAKPDVIQFAPGLPKTRSGKIMR-RIL 604
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
460-951 |
9.56e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 81.59 E-value: 9.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 460 VLTAIAKQARKNPSHIALAQRD--RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVP 537
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 538 LDPEQPRERQQHIIQIAGLRTI-------VTQADYQHRLASVFSGAI-VLAGHLLSSNAQAVALPTAESREG--QIAYVM 607
Cdd:PRK05857 96 ADGNLPIAAIERFCQITDPAAAlvapgskMASSAVPEALHSIPVIAVdIAAVTRESEHSLDAASLAGNADQGseDPLAMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 608 FTSGSTGLPKGVEIGASALDHFTAAARQRyGLRAEDRVL---QFAPFNFD--ASIEEVFATLTSGATLVLRTDEMLesip 682
Cdd:PRK05857 176 FTSGTTGEPKAVLLANRTFFAVPDILQKE-GLNWVTWVVgetTYSPLPAThiGGLWWILTCLMHGGLCVTGGENTT---- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 683 TFVEQVDAQAITLLDLPTAFWNEWVVGLKTGTLTMPsALRAIIIGGEAVYPEQlVQWQRHApdTLRLINTYGPTETTVVA 762
Cdd:PRK05857 251 SLLEILTTNAVATTCLVPTLLSKLVSELKSANATVP-SLRLVGYGGSRAIAAD-VRFIEAT--GVRTAQVYGLSETGCTA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 763 TsCdLQTQPADVAQL---PIGLPLAGVNA-LVLAAGDRP--------AAEGELVLLGPTLAAGYIGTEHTAFTLLAVGdr 830
Cdd:PRK05857 327 L-C-LPTDDGSIVKIeagAVGRPYPGVDVyLAATDGIGPtapgagpsASFGTLWIKSPANMLGYWNNPERTAEVLIDG-- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 831 hlpAYRTGDRV-RLEKGHLLYLGRmDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYPN-GVRRLVAFVATKE-G 906
Cdd:PRK05857 403 ---WVNTGDLLeRREDGFFYIKGR-SSEMIICgGVNIAPDEVDRIAEGVSGVREAACYEIPDEEfGALVGLAVVASAElD 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499404633 907 EIDARALKQRLS--------SVLPPAMIPTdyraFHQLPKTGSNKVDRKRLLA 951
Cdd:PRK05857 479 ESAARALKHTIAarfrresePMARPSTIVI----VTDIPRTQSGKVMRASLAA 527
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
482-961 |
3.38e-15 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 80.05 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLD-PEQPRERQQHIIQIAGL---- 556
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYIAQLRGMlasa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 557 --RTIVTQADYQHRLASVFSGA---IVLAGHLLSS-NAQAVALPTAESREgqIAYVMFTSGSTGLPKGVEIGASALDHfT 630
Cdd:PRK09192 128 qpAAIITPDELLPWVNEATHGNpllHVLSHAWFKAlPEADVALPRPTPDD--IAYLQYSSGSTRFPRGVIITHRALMA-N 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 631 AAARQRYGL--RAEDRVLQFAPFNFDASIEEVFAT-LTSGATL-VLRTDEM-------LESI----------PTF----- 684
Cdd:PRK09192 205 LRAISHDGLkvRPGDRCVSWLPFYHDMGLVGFLLTpVATQLSVdYLPTRDFarrplqwLDLIsrnrgtisysPPFgyelc 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 685 VEQVDAQAITLLDLptafwnewvvglktgtltmpSALRAIIIGGEAVYPEQLVQW-QRHAP---DTLRLINTYGPTETTV 760
Cdd:PRK09192 285 ARRVNSKDLAELDL--------------------SCWRVAGIGADMIRPDVLHQFaEAFAPagfDDKAFMPSYGLAEATL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 761 VAT----SCDLQTQPADVAQLP--------------------IGLPLAGVNALVLAAGDRPAAE---GELVLLGPTLAAG 813
Cdd:PRK09192 345 AVSfsplGSGIVVEEVDRDRLEyqgkavapgaetrrvrtfvnCGKALPGHEIEIRNEAGMPLPErvvGHICVRGPSLMSG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 814 YIGTEHTAFTLLAVG--DrhlpayrTGDRVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVD--EACVQGIV 889
Cdd:PRK09192 425 YFRDEESQDVLAADGwlD-------TGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIA 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 890 YPNGVrRLVAFVATKEGEIDAR-ALKQRLSSVLppamiptdYRAF-----------HQLPKTGSNKVDR----KRLLAEY 953
Cdd:PRK09192 498 QENGE-KIVLLVQCRISDEERRgQLIHALAALV--------RSEFgveaavelvppHSLPRTSSGKLSRakakKRYLSGA 568
|
....*...
gi 499404633 954 HDDAPTQA 961
Cdd:PRK09192 569 FASLDVAA 576
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
464-918 |
4.28e-15 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 79.78 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRD-----RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL 538
Cdd:cd05921 1 LAHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 DPE-----QPRERQQHIIQIAGLRTIVTQ--ADYQHRLASVFS---GAIVLAGHLLSSNAQAVAL-----PTAESREG-- 601
Cdd:cd05921 81 SPAyslmsQDLAKLKHLFELLKPGLVFAQdaAPFARALAAIFPlgtPLVVSRNAVAGRGAISFAElaatpPTAAVDAAfa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 602 -----QIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAED--RVLQFAPFNFDASIEEVF-ATLTSGATLVLr 673
Cdd:cd05921 161 avgpdTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFnLVLYNGGTLYI- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 674 tDEMlESIPTFVEQvdaqaiTLLDL----PTAF------WNEWVvglktGTLTMPSALRA--------IIIGGEAVYPEQ 735
Cdd:cd05921 240 -DDG-KPMPGGFEE------TLRNLreisPTVYfnvpagWEMLV-----AALEKDEALRRrffkrlklMFYAGAGLSQDV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 736 LVQWQRHAPDT----LRLINTYGPTETTVVATSCdlqTQPADVAQLpIGLPLAGVNALVLAAGDRPaaegELVLLGPTLA 811
Cdd:cd05921 307 WDRLQALAVATvgerIPMMAGLGATETAPTATFT---HWPTERSGL-IGLPAPGTELKLVPSGGKY----EVRVKGPNVT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 812 AGYIGT-EHTAFTLLAVGdrhlpAYRTGDRVRL------EKGhLLYLGRMDNEFKI-SGYRIQPGEVEAHLLAQ--PEV- 880
Cdd:cd05921 379 PGYWRQpELTAQAFDEEG-----FYCLGDAAKLadpddpAKG-LVFDGRVAEDFKLaSGTWVSVGPLRARAVAAcaPLVh 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499404633 881 -------DEACVQGIVYPN--GVRRLVAFVATKEGEIDAR-----ALKQRLS 918
Cdd:cd05921 453 davvageDRAEVGALVFPDllACRRLVGLQEASDAEVLRHakvraAFRDRLA 504
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
481-943 |
7.10e-15 |
|
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: 78.16 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIV 560
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 561 TQAdyqhrlasvfsgaivlaghllssnaqavalptaesregqiAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLR 640
Cdd:cd05940 81 VDA----------------------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 641 AEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRtdemlesiptfvEQVDAqaitlldlpTAFWNEWV---------VG- 709
Cdd:cd05940 121 PSDVLYTCLPlYHSTALIVGWSACLASGATLVIR------------KKFSA---------SNFWDDIRkyqatifqyIGe 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 710 LKTGTLTMPSA-------LRAIIigGEAVYPEqlvQWQR-----HAPDTLRLintYGPTETTVvaTSCDLQTQPADVAQL 777
Cdd:cd05940 180 LCRYLLNQPPKpterkhkVRMIF--GNGLRPD---IWEEfkerfGVPRIAEF---YAATEGNS--GFINFFGKPGAIGRN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 778 PIGLPLAGVNALV---LAAGD---------RPAAEGELVLLGPTLAA-----GYIG----TEHTAFTLLAVGDRhlpAYR 836
Cdd:cd05940 250 PSLLRKVAPLALVkydLESGEpirdaegrcIKVPRGEPGLLISRINPlepfdGYTDpaatEKKILRDVFKKGDA---WFN 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 837 TGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPN--GVRRLVAFVATKEGEIDARAL 913
Cdd:cd05940 327 TGDLMRLdGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGtdGRAGMAAIVLQPNEEFDLSAL 406
|
490 500 510
....*....|....*....|....*....|
gi 499404633 914 KQRLSSVLPPAMIPTDYRAFHQLPKTGSNK 943
Cdd:cd05940 407 AAHLEKNLPGYARPLFLRLQPEMEITGTFK 436
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
3-348 |
7.43e-15 |
|
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: 78.08 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGehaeqpeigfVASQLPVP 82
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDG----------VPYQLILE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IG-VLPIVELLPAPMTDEEQTIRQwardEISLPLDLLNGLPCRFALLC-GEKRDFLYSCVHHIALDGFGTTMLFQRIAQI 160
Cdd:cd19538 73 EDeATPKLEIKEVDEEELESEINE----AVRYPFDLSEEPPFRATLFElGENEHVLLLLLHHIAADGWSLAPLTRDLSKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 161 YTALTAGQSAPVA----EFGPFSAVLEEERQRDASGQTAQAR--DFWLETLNAMPEPASF-SEKKAPIAARFLRQSCD-- 231
Cdd:cd19538 149 YRARCKGEAPELAplpvQYADYALWQQELLGDESDPDSLIARqlAYWKKQLAGLPDEIELpTDYPRPAESSYEGGTLTfe 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 232 MPADLWQPLSALCEGNKISwpdLF------LAMLAThlKLVSGSDrLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDE 305
Cdd:cd19538 229 IDSELHQQLLQLAKDNNVT---LFmvlqagFAALLT--RLGAGTD-IPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSG 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499404633 306 QANFVALAQQVARTKRTLRRHQHYRYEHLRRDLN--RVGGEQRLF 348
Cdd:cd19538 303 NPSFRELLERVKETNLEAYEHQDIPFERLVEALNptRSRSRHPLF 347
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
482-951 |
8.64e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 78.48 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDP-EQPRERQQHIIQiAGLRTIV 560
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPfYTPAEIAKQAKA-SGAKLII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 561 TQADYQHRLASVFSGAIVL--------AGHLLSS---NAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIGASALdhF 629
Cdd:PLN02246 128 TQSCYVDKLKGLAEDDGVTvvtiddppEGCLHFSeltQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGL--V 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 630 TAAARQRYG------LRAEDRVLQFAPFNFDASIEEV-FATLTSGATLVL----RTDEMLESI------------PTFVE 686
Cdd:PLN02246 206 TSVAQQVDGenpnlyFHSDDVILCVLPMFHIYSLNSVlLCGLRVGAAILImpkfEIGALLELIqrhkvtiapfvpPIVLA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 687 QVDAQAITLLDLptafwnewvvglktgtltmpSALRaIIIGGEAVYPEQLVqwqrhapDTLR-------LINTYGPTET- 758
Cdd:PLN02246 286 IAKSPVVEKYDL--------------------SSIR-MVLSGAAPLGKELE-------DAFRaklpnavLGQGYGMTEAg 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 759 TVVATSCDLQTQPADV-----------AQLPIGLPLAGVNalvlAAGDRPaaeGELVLLGPTLAAGYIG-TEHTAFTLLA 826
Cdd:PLN02246 338 PVLAMCLAFAKEPFPVksgscgtvvrnAELKIVDPETGAS----LPRNQP---GEICIRGPQIMKGYLNdPEATANTIDK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 827 VGDRHlpayrTGDrVRL--EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATK 904
Cdd:PLN02246 411 DGWLH-----TGD-IGYidDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRS 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499404633 905 EG-EIDARALKQ----------RLSSVLppamiptdyraF-HQLPKTGSNKVDRKRLLA 951
Cdd:PLN02246 485 NGsEITEDEIKQfvakqvvfykRIHKVF-----------FvDSIPKAPSGKILRKDLRA 532
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
601-949 |
1.73e-14 |
|
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: 76.37 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 601 GQIAYVMFTSGSTGLPKGVEIGASAlDHFTAAARQRYGLRAEDRVLQFA-P-FNFDASIEEVFATLTSGATLVL------ 672
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGlPlFHVNGSVVTLLTPLASGAHVVLagpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 673 RTDEMLESIPTFVEQVDAQAitLLDLPTAFwnewvvglkTGTLTMP-----SALRAIIIGGEAVYPEQLVQWQRHApdTL 747
Cdd:cd05944 81 RNPGLFDNFWKLVERYRITS--LSTVPTVY---------AALLQVPvnadiSSLRFAMSGAAPLPVELRARFEDAT--GL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 748 RLINTYGPTETTVVaTSCDLQTQPADVAQLPIGLPLAGVNALVLAAGDR------PAAEGELVLLGPTLAAGYIGTEH-- 819
Cdd:cd05944 148 PVVEGYGLTEATCL-VAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRllrdcaPDEVGEICVAGPGVFGGYLYTEGnk 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 820 TAFtllaVGDRHLpayRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLV 898
Cdd:cd05944 227 NAF----VADGWL---NTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPV 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 499404633 899 AFVATKEG-EIDARALKQRLSSVLPP-AMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:cd05944 300 AYVQLKPGaVVEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
447-952 |
2.42e-14 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 77.23 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 447 LITSREP-EPFVEPVLTAIAKQARKNPSHIALAQRD-----RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPE 520
Cdd:PRK08180 27 YLRSAEPlGDYPRRLTDRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 521 TIISLLAVMQCGAVYVPLDPE-----QPRERQQHIIQI--AGLrTIVTQAD-YQHRLASVF---------------SGAI 577
Cdd:PRK08180 107 HALLALAAMYAGVPYAPVSPAyslvsQDFGKLRHVLELltPGL-VFADDGAaFARALAAVVpadvevvavrgavpgRAAT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 578 VLAGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGV-----EIGASAldhftAAARQRYG-LRAEDRVL-QFAP 650
Cdd:PRK08180 186 PFAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVinthrMLCANQ-----QMLAQTFPfLAEEPPVLvDWLP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 651 FN--FDASIeEVFATLTSGATLVL--------RTDEML----ESIPTFVEQVdaqaitlldlPTAfWNEWVVGLKT-GTL 715
Cdd:PRK08180 261 WNhtFGGNH-NLGIVLYNGGTLYIddgkptpgGFDETLrnlrEISPTVYFNV----------PKG-WEMLVPALERdAAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 716 --TMPSALRAIIIGGeAVYPEQLvqW-------QRHAPDTLRLINTYGPTETTVVATSCdlqTQPADVAQLpIGLPLAGV 786
Cdd:PRK08180 329 rrRFFSRLKLLFYAG-AALSQDV--WdrldrvaEATCGERIRMMTGLGMTETAPSATFT---TGPLSRAGN-IGLPAPGC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 787 NALVLAAGDRPaaegELVLLGPTLAAGYIG-TEHTAftllAVGDRHlPAYRTGDRVRL------EKGhLLYLGRMDNEFK 859
Cdd:PRK08180 402 EVKLVPVGGKL----EVRVKGPNVTPGYWRaPELTA----EAFDEE-GYYRSGDAVRFvdpadpERG-LMFDGRIAEDFK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 860 I-SGYRIQPGEVEAHLLAQ--PEVDEACVQGI--------VYPN--GVRRLV--AFVATKEGEIDARALKQRLSSVLppa 924
Cdd:PRK08180 472 LsSGTWVSVGPLRARAVSAgaPLVQDVVITGHdrdeigllVFPNldACRRLAglLADASLAEVLAHPAVRAAFRERL--- 548
|
570 580
....*....|....*....|....*...
gi 499404633 925 miptdyRAFHQLPKTGSNKVDRKRLLAE 952
Cdd:PRK08180 549 ------ARLNAQATGSSTRVARALLLDE 570
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
485-918 |
2.48e-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: 76.87 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAvyvpldpeqprerqqhiiqiaglrTIVT--- 561
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNI------------------------PIVTvya 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 ---QADYQHRLASVFSGAIVLaghllSSNAQAVALptaesregqiayVMFTSGSTGLPKGVEIGASALDHFTAAARQRYG 638
Cdd:cd17639 63 tlgEDALIHSLNETECSAIFT-----DGKPDDLAC------------IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 639 --LRAEDRVLQFAPFnfdASIEEVFAT---LTSGATL---------------------------------VLRT-----D 675
Cdd:cd17639 126 elLGPDDRYLAYLPL---AHIFELAAEnvcLYRGGTIgygsprtltdkskrgckgdltefkptlmvgvpaIWDTirkgvL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 676 EMLESIPTFVEQV-----DAQAITLLDLP-TAFWNEWVVGlKTGTLTmPSALRAIIIGGEAVypeqlvqwqrhAPDTLRL 749
Cdd:cd17639 203 AKLNPMGGLKRTLfwtayQSKLKALKEGPgTPLLDELVFK-KVRAAL-GGRLRYMLSGGAPL-----------SADTQEF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 750 INT--------YGPTETTVVATSCDlqtqPADVAQLPIGLPLAGVNALVL---AAG---DRPAAEGELVLLGPTLAAGYI 815
Cdd:cd17639 270 LNIvlcpviqgYGLTETCAGGTVQD----PGDLETGRVGPPLPCCEIKLVdweEGGystDKPPPRGEILIRGPNVFKGYY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 816 GTEH---TAFTllavGDRHLpayRTGDRVRLEK-GHLLYLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVqgIVY 890
Cdd:cd17639 346 KNPEktkEAFD----GDGWF---HTGDIGEFHPdGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICV--YAD 416
|
490 500
....*....|....*....|....*...
gi 499404633 891 PNGVrRLVAFVATKEGEIDARALKQRLS 918
Cdd:cd17639 417 PDKS-YPVAIVVPNEKHLTKLAEKHGVI 443
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
467-958 |
2.85e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 76.99 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 467 QARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGE-RIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRE 545
Cdd:PRK13388 10 RDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 546 RQQHIIQIAGLRTIVTQADYQHRLASV-FSGAIVL----AGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVE 620
Cdd:PRK13388 90 ALAADIRRADCQLLVTDAEHRPLLDGLdLPGVRVLdvdtPAYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 621 IGASALDHFTAAARQRYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRtdemlesiPTF--------VEQVDAQ 691
Cdd:PRK13388 170 CSHGRLAFAGRALTERFGLTRDDVCYVSMPlFHSNAVMAGWAPAVASGAAVALP--------AKFsasgflddVRRYGAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 692 AITLLDLPTAFwnewvvglktgTLTMPSA-------LRaIIIGGEAVyPEQLVQWQRHApdTLRLINTYGPTETTVVAts 764
Cdd:PRK13388 242 YFNYVGKPLAY-----------ILATPERpddadnpLR-VAFGNEAS-PRDIAEFSRRF--GCQVEDGYGSSEGAVIV-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 765 cdlqTQPADVAQLPIGLPLAGVNALVLAAG-DRPAAE--------------GELV-LLGPTLAAGYIGTEHtaftllAVG 828
Cdd:PRK13388 305 ----VREPGTPPGSIGRGAPGVAIYNPETLtECAVARfdahgallnadeaiGELVnTAGAGFFEGYYNNPE------ATA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 829 D--RHlPAYRTGDRVRLEKGHLLYL-GRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYP-NGVRRLVAFVATK 904
Cdd:PRK13388 375 ErmRH-GMYWSGDLAYRDADGWIYFaGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDErVGDQVMAALVLRD 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 499404633 905 EGEIDARALKQRLSSV--LPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAE-YHDDAP 958
Cdd:PRK13388 454 GATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIAQgWATGDP 510
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
481-952 |
4.30e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 76.26 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQYSYQQLLGLSGQAAAALHERGVKPGER-IGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTI 559
Cdd:PRK07867 26 DSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 560 VTQADYQHRLASVFSGAIVLA------GHLLSSNAQAvALPTAESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAA 633
Cdd:PRK07867 106 LTESAHAELLDGLDPGVRVINvdspawADELAAHRDA-EPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVML 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 634 RQRYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRTDEmleSIPTFVEQVDAQAITLLDL---PTAFwnewvvg 709
Cdd:PRK07867 185 AQRFGLGPDDVCYVSMPlFHSNAVMAGWAVALAAGASIALRRKF---SASGFLPDVRRYGATYANYvgkPLSY------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 710 lktgTLTMP-------SALRaIIIGGEAVypeqlvqwqrhAPDT--------LRLINTYGPTETTVvATSCDLQTQPADV 774
Cdd:PRK07867 255 ----VLATPerpddadNPLR-IVYGNEGA-----------PGDIarfarrfgCVVVDGFGSTEGGV-AITRTPDTPPGAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 775 AQLPIGLPLAGVN-------ALVLAAGDRPAAE--GELV-LLGPTLAAGYIGTEHTAFTLLAVGdrhlpAYRTGDRV-RL 843
Cdd:PRK07867 318 GPLPPGVAIVDPDtgtecppAEDADGRLLNADEaiGELVnTAGPGGFEGYYNDPEADAERMRGG-----VYWSGDLAyRD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 844 EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPN-GVRRLVAFVATKEGEIDARALKQRLS--SV 920
Cdd:PRK07867 393 ADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVvGDQVMAALVLAPGAKFDPDAFAEFLAaqPD 472
|
490 500 510
....*....|....*....|....*....|..
gi 499404633 921 LPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAE 952
Cdd:PRK07867 473 LGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
481-906 |
1.63e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 74.45 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIV 560
Cdd:PLN02860 30 NRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 561 TQADYQHRLASVFSGAI-VLAGHLL-------SSNAQAVALPTAESRE--------------GQIAYVMFTSGSTGLPKG 618
Cdd:PLN02860 110 TDETCSSWYEELQNDRLpSLMWQVFlespsssVFIFLNSFLTTEMLKQralgtteldyawapDDAVLICFTSGTTGRPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 619 VEIGASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLrtdemlesIPTFVEQVDAQAI----- 693
Cdd:PLN02860 190 VTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVL--------LPKFDAKAALQAIkqhnv 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 694 -TLLDLPTAFWNEWVVGLKTGTLTMPSALRAIIIGGEAVyPEQLVQWQRHAPDTLRLINTYGPTET------------TV 760
Cdd:PLN02860 262 tSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSL-SSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhdpTL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 761 VATSCDLQTQPA---DVAQLP----IGLPLAGVNALVLAagDRPAAEGELVLLGPTLAAGYIG-TEHTAftllavGDRHL 832
Cdd:PLN02860 341 ESPKQTLQTVNQtksSSVHQPqgvcVGKPAPHVELKIGL--DESSRVGRILTRGPHVMLGYWGqNSETA------SVLSN 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404633 833 PAY-RTGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG 906
Cdd:PLN02860 413 DGWlDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDG 488
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
465-949 |
1.78e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 465 AKQARKNPShIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPR 544
Cdd:PRK13390 7 AQIAPDRPA-VIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 545 ERQQHIIQIAGLRTIVTQA-----------DYQHRLAsvFSGAIVLAGHLLSSNAQAvALPTAESREGqiAYVMFTSGST 613
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAaldglaakvgaDLPLRLS--FGGEIDGFGSFEAALAGA-GPRLTEQPCG--AVMLYSSGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 614 GLPKGVE-------IGASAlDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLESIPTFVE 686
Cdd:PRK13390 161 GFPKGIQpdlpgrdVDAPG-DPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQATLGHVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 687 QVDAQAITLldLPTAFWNEWVVGLKTGTLTMPSALRAIIiggEAVYP------EQLVQWQrhAPdtlRLINTYGPTET-- 758
Cdd:PRK13390 240 RYRITVTQM--VPTMFVRLLKLDADVRTRYDVSSLRAVI---HAAAPcpvdvkHAMIDWL--GP---IVYEYYSSTEAhg 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 759 -TVVATScDLQTQPADVAQLPIGlplagvnALVLAAGDrpaaegelvllGPTLAAGYIGT---EHTAFTLLAVGD----- 829
Cdd:PRK13390 310 mTFIDSP-DWLAHPGSVGRSVLG-------DLHICDDD-----------GNELPAGRIGTvyfERDRLPFRYLNDpekta 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 830 --RHlPAY----RTGDRVRLEKGHLLYLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVA 902
Cdd:PRK13390 371 aaQH-PAHpfwtTVGDLGSVDEDGYLYLADRKSFMIISgGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQ 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 499404633 903 TKEG----EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK13390 450 LVEGirgsDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
482-943 |
2.33e-13 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 74.23 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPE-------------QP----- 543
Cdd:cd05943 97 TEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDfgvpgvldrfgqiEPkvlfa 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 544 -------------RERQQHIiqIAGLRTIvtqadyqhrLASVFSGAIVLAG-HLLSSNAQAVALPTAESRE--GQIA--- 604
Cdd:cd05943 177 vdaytyngkrhdvREKVAEL--VKGLPSL---------LAVVVVPYTVAAGqPDLSKIAKALTLEDFLATGaaGELEfep 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 605 -------YVMFTSGSTGLPKGVEIGASA--LDHFTAAARQrYGLRAEDRVLQFAP-----FNFDASieevfaTLTSGATL 670
Cdd:cd05943 246 lpfdhplYILYSSGTTGLPKCIVHGAGGtlLQHLKEHILH-CDLRPGDRLFYYTTcgwmmWNWLVS------GLAVGATI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 671 VL-------RTDEMLESIptfveqVDAQAITLLDLPTAFWNEWV-VGLKTGTLTMPSALRAIIIGGEAVYPEQLVQWQRH 742
Cdd:cd05943 319 VLydgspfyPDTNALWDL------ADEEGITVFGTSAKYLDALEkAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDH 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 743 APDTLRLINTYGPTETtvvaTSCDLQTQP-ADVAQLPIGLPLAGVNALVLAAGDRPAAE--GELVLLG--PTLAAGYIGT 817
Cdd:cd05943 393 IKPDVLLASISGGTDI----ISCFVGGNPlLPVYRGEIQCRGLGMAVEAFDEEGKPVWGekGELVCTKpfPSMPVGFWND 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 818 E-----HTAFTllavgDRHLPAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYP 891
Cdd:cd05943 469 PdgsryRAAYF-----AKYPGVWAHGDWIEItPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWK 543
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 499404633 892 NGVRRLVAFVATKEG-EID---ARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNK 943
Cdd:cd05943 544 DGDERVILFVKLREGvELDdelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
476-951 |
2.70e-13 |
|
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: 73.57 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 476 ALAQRDRQYSYQQLLGLSG--QAAAALHER-----GVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQ 548
Cdd:cd05929 3 ARDLDRAQVFHQRRLLLLDvySIALNRNARaaaaeGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEAC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 549 HIIQIAGLrtivtqadyqHRLASVFSGAIVLAGhlLSSNAQAVAL----PTAESREGQiaYVMFTSGSTGLPKGVEIGAS 624
Cdd:cd05929 83 AIIEIKAA----------ALVCGLFTGGGALDG--LEDYEAAEGGspetPIEDEAAGW--KMLYSGGTTGRPKGIKRGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 625 A--LDHFT-AAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVL--RTD--EMLESIP----TFVEQVDAQAI 693
Cdd:cd05929 149 GgpPDNDTlMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLmeKFDpeEFLRLIEryrvTFAQFVPTMFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 694 TLLDLPTAFWNEW-VVGLKTGTLT---MPSALRAIII--GGEavypeqlvqwqrhapdtlRLINTYGPTE---TTVVaTS 764
Cdd:cd05929 229 RLLKLPEAVRNAYdLSSLKRVIHAaapCPPWVKEQWIdwGGP------------------IIWEYYGGTEgqgLTII-NG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 765 CDLQTQPADVaqlpiGLPLAGVNALVLAAGDR--PAAEGELVLLGPtlaAGYIGTEHTAFTLLAVGDRhlpAYRT-GDRV 841
Cdd:cd05929 290 EEWLTHPGSV-----GRAVLGKVHILDEDGNEvpPGEIGEVYFANG---PGFEYTNDPEKTAAARNEG---GWSTlGDVG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 842 RLEKGHLLYLGRMDNEFKISGYR-IQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVAT----KEGEIDARALKQR 916
Cdd:cd05929 359 YLDEDGYLYLTDRRSDMIISGGVnIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPapgaDAGTALAEELIAF 438
|
490 500 510
....*....|....*....|....*....|....*
gi 499404633 917 LSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLA 951
Cdd:cd05929 439 LRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3-328 |
2.81e-13 |
|
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: 73.06 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEvAGEHAEQpeigfvasQLPVP 82
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFE-GDDFGEQ--------QVLDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGV-LPIVELLPApmTDEEQTIRQWARDEISLPLDLLNGLPCRFALLCGEKRDF-LYSCVHHIALDGFGTTMLFQRIAQI 160
Cdd:cd20483 74 PSFhLIVIDLSEA--ADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFaLVLASHHIAWDRGSSKSIFEQFTAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 161 YTALTAGQ-----SAPVAEFGPFSaVLEEERQRDASGQTAQarDFWLETLNAMPEPAS---FSEKKAPIAARFLRQSCD- 231
Cdd:cd20483 152 YDALRAGRdlatvPPPPVQYIDFT-LWHNALLQSPLVQPLL--DFWKEKLEGIPDASKllpFAKAERPPVKDYERSTVEa 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 232 -MPADLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLMVPSMQMNIVPLCIQVDEQANFV 310
Cdd:cd20483 229 tLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFD 308
|
330
....*....|....*...
gi 499404633 311 ALAQQVArtKRTLRRHQH 328
Cdd:cd20483 309 DLLESTK--TTCLEAYEH 324
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
608-949 |
4.17e-13 |
|
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: 71.93 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 608 FTSGSTGLPKGVeigasALDHFTAA-----ARQRYGLRAEDRVLQFAPFnFDA--SIEEVFATLTSGATLVLRTdEMLES 680
Cdd:cd05917 9 FTSGTTGSPKGA-----TLTHHNIVnngyfIGERLGLTEQDRLCIPVPL-FHCfgSVLGVLACLTHGATMVFPS-PSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 681 IPTFVEQVDAQAITLLDLPTAFWNEwvVGLKTGTLTMPSALRAIIIGGEAVYPEQL--VQWQRHAPDtlrLINTYGPTET 758
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPTMFIAE--LEHPDFDKFDLSSLRTGIMAGAPCPPELMkrVIEVMNMKD---VTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 759 TVVATsCDLQTQPADVAQLPIGLPLAGVNALVLAAGDR----PAAEGELVLLGPTLAAGYIGT-EHTAFTLLAVGdrhlp 833
Cdd:cd05917 157 SPVST-QTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGivppVGVPGELCIRGYSVMKGYWNDpEKTAEAIDGDG----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 834 AYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG----EI 908
Cdd:cd05917 231 WLHTGDLAVMdEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGaeltEE 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 499404633 909 DARA-LKQRLSSVLPPAMIptdyRAFHQLPKTGSNKVDRKRL 949
Cdd:cd05917 311 DIKAyCKGKIAHYKVPRYV----FFVDEFPLTVSGKIQKFKL 348
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
469-949 |
4.74e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 73.13 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 469 RKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDP-EQPRErQ 547
Cdd:PRK07059 34 RQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPlYTPRE-L 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 548 QHIIQIAGLRTIVTQADYQHRLASV-------------------FSGAIV---------------LAGHLLSSNAQA--- 590
Cdd:PRK07059 113 EHQLKDSGAEAIVVLENFATTVQQVlaktavkhvvvasmgdllgFKGHIVnfvvrrvkkmvpawsLPGHVRFNDALAega 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 591 -VALPTAESREGQIAYVMFTSGSTGLPKGV-----EIGASALDhftAAARQRYGLRAEDRVLQFapfNFDASIE--EVFA 662
Cdd:PRK07059 193 rQTFKPVKLGPDDVAFLQYTGGTTGVSKGAtllhrNIVANVLQ---MEAWLQPAFEKKPRPDQL---NFVCALPlyHIFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 663 tLTSGATLVLRTDEM------LESIPTFVEQVDAQAITLLDLPTAFWNewvvglktGTLTMP-------SALRAIIIGGE 729
Cdd:PRK07059 267 -LTVCGLLGMRTGGRnilipnPRDIPGFIKELKKYQVHIFPAVNTLYN--------ALLNNPdfdkldfSKLIVANGGGM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 730 AVYPEQLVQWQR--HAPdtlrLINTYGPTETTVVATsCDlqtqPADVAQLP--IGLPLAGVNALVL--AAGDRPAAE-GE 802
Cdd:PRK07059 338 AVQRPVAERWLEmtGCP----ITEGYGLSETSPVAT-CN----PVDATEFSgtIGLPLPSTEVSIRddDGNDLPLGEpGE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 803 LVLLGPTLAAGYIGT-EHTAFTLLAVGdrhlpAYRTGDR-VRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEV 880
Cdd:PRK07059 409 ICIRGPQVMAGYWNRpDETAKVMTADG-----FFRTGDVgVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404633 881 DEACVQGIVYPNGVRRLVAFVATKEGEIDARAL----KQRLSSVLPPAMIptDYRAfhQLPKTGSNKVDRKRL 949
Cdd:PRK07059 484 LEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVkafcKERLTNYKRPKFV--EFRT--ELPKTNVGKILRREL 552
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
485-883 |
2.33e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 70.62 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLglsgQAAAALHERGVK-PGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQA 563
Cdd:PRK06334 47 SYNQVR----KAVIALATKVSKyPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 DYQHRLASVFSGAIVLAGHLLSSN--------------AQAVALP---------TAESREGQIAYVMFTSGSTGLPKGVe 620
Cdd:PRK06334 123 QLMQHLAQTHGEDAEYPFSLIYMEevrkelsfwekcriGIYMSIPfewlmrwfgVSDKDPEDVAVILFTSGTEKLPKGV- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 621 igasALDHFTAAARQRYGLR-----AEDRVLQFAP----FNFDASieEVFATLtSGATLVLRTDEMLESipTFVEQVDAQ 691
Cdd:PRK06334 202 ----PLTHANLLANQRACLKffspkEDDVMMSFLPpfhaYGFNSC--TLFPLL-SGVPVVFAYNPLYPK--KIVEMIDEA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 692 AITLLDLPTAFWNEWVVGLKTGTLTMPSaLRAIIIGGEAVYPEQLVQWQRHAPDtLRLINTYGPTETTVVATscdLQTQP 771
Cdd:PRK06334 273 KVTFLGSTPVFFDYILKTAKKQESCLPS-LRFVVIGGDAFKDSLYQEALKTFPH-IQLRQGYGTTECSPVIT---INTVN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 772 ADVAQLPIGLPLAGVNALVLAAGDR-PAAEGE--LVLL-GPTLAAGYIGT-EHTAFTLLAvGDRHlpaYRTGDRVRLEKG 846
Cdd:PRK06334 348 SPKHESCVGMPIRGMDVLIVSEETKvPVSSGEtgLVLTrGTSLFSGYLGEdFGQGFVELG-GETW---YVTGDLGYVDRH 423
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 499404633 847 HLLYL-GRMDNEFKISGYRIQPGEVEAHLL---AQPEVDEA 883
Cdd:PRK06334 424 GELFLkGRLSRFVKIGAEMVSLEALESILMegfGQNAADHA 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
485-955 |
5.67e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.40 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQAD 564
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 565 Y-------QHRLASVfSGAIVLAGhllSSNAQAVALPTA-------ESREGQIAYVMF----------TSGSTGLPKGVE 620
Cdd:PRK06018 121 FvpilekiADKLPSV-ERYVVLTD---AAHMPQTTLKNAvayeewiAEADGDFAWKTFdentaagmcyTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 621 IG--ASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVL---RTD-----EMLESiptfvEQVDA 690
Cdd:PRK06018 197 YShrSNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMpgaKLDgasvyELLDT-----EKVTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 691 QAitllDLPTAfWNEWVVGLKTGTLTMPSaLRAIIIGGEAVyPEQLVQW-------QRHApdtlrlintYGPTETTVVAT 763
Cdd:PRK06018 272 TA----GVPTV-WLMLLQYMEKEGLKLPH-LKMVVCGGSAM-PRSMIKAfedmgveVRHA---------WGMTEMSPLGT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 764 SCDLQTQPADV---AQLPI----GLPLAGVNALVL--AAGDRP---AAEGELVLLGPTLAAGYIGtehtaftllaVGDRH 831
Cdd:PRK06018 336 LAALKPPFSKLpgdARLDVlqkqGYPPFGVEMKITddAGKELPwdgKTFGRLKVRGPAVAAAYYR----------VDGEI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 832 LPA---YRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE 907
Cdd:PRK06018 406 LDDdgfFDTGDVATIdAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGE 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499404633 908 IDARA-LKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHD 955
Cdd:PRK06018 486 TATREeILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
481-952 |
5.74e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 68.91 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQYSyQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIV 560
Cdd:PRK08308 6 DEEYS-KSDFDLRLQRYEEMEQFQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 561 TQAdyqhrlasvFSGAIVLAGHLLSSnaqavalptaesrEGQIayVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLR 640
Cdd:PRK08308 85 YGE---------SDFTKLEAVNYLAE-------------EPSL--LQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 641 AEDRVLQFAPFNFDAS-IEEVFATLTSGATLVLRTDemleSIPTFVEQVdaqaitLLDLPtafwNEWVVGLKTGTLTMPS 719
Cdd:PRK08308 141 QDETPIVACPVTHSYGlICGVLAALTRGSKPVIITN----KNPKFALNI------LRNTP----QHILYAVPLMLHILGR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 720 ALR------AIIIGGeAVYPEQLVQWQRHApdTLRLINTYGPTETTVVATSCDLQTQpadvaqLPIGLPLAGVNalvLAA 793
Cdd:PRK08308 207 LLPgtfqfhAVMTSG-TPLPEAWFYKLRER--TTYMMQQYGCSEAGCVSICPDMKSH------LDLGNPLPHVS---VSA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 794 GDRPAAEGELVLlgptlaagyigtehtaftllAVGDRHLpayRTGDR-VRLEKGHLLYLGRMDNEFKISGYRIQPGEVEA 872
Cdd:PRK08308 275 GSDENAPEEIVV--------------------KMGDKEI---FTKDLgYKSERGTLHFMGRMDDVINVSGLNVYPIEVED 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 873 HLLAQPEVDEACVQGIVYP-NGVRRLVAFVAtkEGEIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLA 951
Cdd:PRK08308 332 VMLRLPGVQEAVVYRGKDPvAGERVKAKVIS--HEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
.
gi 499404633 952 E 952
Cdd:PRK08308 410 G 410
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
481-953 |
7.08e-12 |
|
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: 69.05 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQY---SYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL---DPEQPRERQQHIIQIA 554
Cdd:cd05908 10 DKKEkfvSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVsigSNEEHKLKLNKVWNTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 555 GLRTIVTQADYQHRLASvfsgaivlaghllssnaqavalptaesregQIAYVMFTSGSTGLPKGVEIGASALDHFTAAAR 634
Cdd:cd05908 90 KNPYLITEEEVLCELAD------------------------------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 635 QRYGLRAEDRVLQFAPFNFDAS-IEEVFATLTSGAT-LVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNEWVVGLKT 712
Cdd:cd05908 140 NSTEWKTKDRILSWMPLTHDMGlIAFHLAPLIAGMNqYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 713 GTLTM--PSALRAIIIGGEAVYPEQLVQWQRH-APDTLR---LINTYGPTETTVVATSCDLQ----TQPADVAQLPIGLP 782
Cdd:cd05908 220 EKANDwdLSSIRMILNGAEPIDYELCHEFLDHmSKYGLKrnaILPVYGLAEASVGASLPKAQspfkTITLGRRHVTHGEP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 783 LAGV-----NALVLAAGDRPAAE------------------GELVLLGPTLAAGYIGT-EHTAFTLLAVGdrhlpAYRTG 838
Cdd:cd05908 300 EPEVdkkdsECLTFVEVGKPIDEtdiricdednkilpdgyiGHIQIRGKNVTPGYYNNpEATAKVFTDDG-----WLKTG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 839 DRVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGI-VYPNGVR--RLVAFVATKEGEIDARALKQ 915
Cdd:cd05908 375 DLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACgVNNSNTRneEIFCFIEHRKSEDDFYPLGK 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 499404633 916 RLSSVLppamiptDYRA---------FHQLPKTGSNKVDRKRLLAEY 953
Cdd:cd05908 455 KIKKHL-------NKRGgwqinevlpIRRIPKTTSGKVKRYELAQRY 494
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2-339 |
9.20e-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: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 2 KPLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMlsaiRQAvmececlyCQFVEvaGEHA-------EQPEIGF 74
Cdd:cd20484 2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKF----KQA--------CQFVL--EQHPilksvieEEDGVPF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 75 VASQLPVPIGVLP--IVELlpapmtdEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTT 151
Cdd:cd20484 68 QKIEPSKPLSFQEedISSL-------KESEIIAYLREKAKEPFVLENGPLMRVHLFsRSEQEHFVLITIHHIIFDGSSSL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 152 MLFQRIAQIYTALTAGQSAPVAEFGP-FSAVLEEERQRDASGQTAQARDFWLETLN-AMPEPASFSEKKAPIAARFLRQS 229
Cdd:cd20484 141 TLIHSLLDAYQALLQGKQPTLASSPAsYYDFVAWEQDMLAGAEGEEHRAYWKQQLSgTLPILELPADRPRSSAPSFEGQT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 230 CDM--PADLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNR--------IGSAslmvpsmqMNIVPL 299
Cdd:cd20484 221 YTRrlPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRpeerfdslIGYF--------INMLPI 292
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 499404633 300 CIQVDEQANFVALAQQVARTKRTLRRHQHYRYEHLRRDLN 339
Cdd:cd20484 293 RSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLN 332
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
719-949 |
9.95e-12 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 68.48 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 719 SALRAIIIGGEAVYPEQLVQWQRHapdTLRLINTYGPTET-TVVATscdlqTQPADVAQLPIGL--PLAGVNaLVLAAGD 795
Cdd:PRK07445 230 AQFRTILLGGAPAWPSLLEQARQL---QLRLAPTYGMTETaSQIAT-----LKPDDFLAGNNSSgqVLPHAQ-ITIPANQ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 796 RpaaeGELVLLGPTLAAGYigtehtaFTLLAVGDRHLPayrTGDRVRLEKGHLLY-LGRMDNEFKISGYRIQPGEVEAHL 874
Cdd:PRK07445 301 T----GNITIQAQSLALGY-------YPQILDSQGIFE---TDDLGYLDAQGYLHiLGRNSQKIITGGENVYPAEVEAAI 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404633 875 LAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK07445 367 LATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
452-949 |
1.22e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 68.64 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 452 EPEPFvePVLTAIAKQA-RKNPSHIALAQRDRQYSYQQLLGLSGQAAAAL-HERGVKPGERIGIMLNRSPETIISLLAVM 529
Cdd:PRK05677 19 NPDEY--PNIQAVLKQScQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 530 QCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQADYQHRLASVFSGA------IVLAGHLLSS------NA--------- 588
Cdd:PRK05677 97 RAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTgvkhviVTEVADMLPPlkrlliNAvvkhvkkmv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 589 ------QAVALPTAESR-EGQ-----------IAYVMFTSGSTGLPKGveigaSALDHFTAAARqryglraedrVLQFAP 650
Cdd:PRK05677 177 payhlpQAVKFNDALAKgAGQpvteanpqaddVAVLQYTGGTTGVAKG-----AMLTHRNLVAN----------MLQCRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 651 F---NFDASIEEVFA----------TLTSGATLVLRTDEMLES----IPTFVEQVDAQAIT-LLDLPTAFW----NEWVV 708
Cdd:PRK05677 242 LmgsNLNEGCEILIAplplyhiyafTFHCMAMMLIGNHNILISnprdLPAMVKELGKWKFSgFVGLNTLFValcnNEAFR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 709 GLKTgtltmpSALRAIIIGGEAVYPEQLVQWQRHApdTLRLINTYGPTETTVVATscdlqTQPADVAQL-PIGLPLAGVN 787
Cdd:PRK05677 322 KLDF------SALKLTLSGGMALQLATAERWKEVT--GCAICEGYGMTETSPVVS-----VNPSQAIQVgTIGIPVPSTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 788 ALVL--AAGDRPAAE-GELVLLGPTLAAGYIG-TEHTAFTLLAVGdrhlpAYRTGD-RVRLEKGHLLYLGRMDNEFKISG 862
Cdd:PRK05677 389 CKVIddDGNELPLGEvGELCVKGPQVMKGYWQrPEATDEILDSDG-----WLKTGDiALIQEDGYMRIVDRKKDMILVSG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 863 YRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGS 941
Cdd:PRK05677 464 FNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGEtLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNV 543
|
....*...
gi 499404633 942 NKVDRKRL 949
Cdd:PRK05677 544 GKILRREL 551
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
869-943 |
1.45e-11 |
|
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: 61.02 E-value: 1.45e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404633 869 EVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNK 943
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGvELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
483-887 |
1.52e-11 |
|
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: 67.77 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 483 QYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIiqiaglrtivtq 562
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYI------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 563 adyqhrLASVFSGAIVLaghllssnaqavalptaESREGQIAYVMFTSGSTGLPKGVEIGASAL----DHFTAAARQRYG 638
Cdd:cd17640 73 ------LNHSESVALVV-----------------ENDSDDLATIIYTSGTTGNPKGVMLTHANLlhqiRSLSDIVPPQPG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 639 lraeDRVLQFAP-----------FNFDASIEEVFATLTSgatlvLRTD------EMLESIPTFVEQVDAQAITLLDLPTA 701
Cdd:cd17640 130 ----DRFLSILPiwhsyersaeyFIFACGCSQAYTSIRT-----LKDDlkrvkpHYIVSVPRLWESLYSGIQKQVSKSSP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 702 FWNEWVVGLKTGtltmpSALRAIIIGGEAVYPeqlvqwqrHApDT------LRLINTYGPTETTVVATScdlQTQPADVA 775
Cdd:cd17640 201 IKQFLFLFFLSG-----GIFKFGISGGGALPP--------HV-DTffeaigIEVLNGYGLTETSPVVSA---RRLKCNVR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 776 QlPIGLPLAGVNALVLAAGDR----PAAEGELVLLGPTLAAGYIGT-EHTAFTLLAVGdrhlpAYRTGDRVRLEK-GHLL 849
Cdd:cd17640 264 G-SVGRPLPGTEIKIVDPEGNvvlpPGEKGIVWVRGPQVMKGYYKNpEATSKVLDSDG-----WFNTGDLGWLTCgGELV 337
|
410 420 430
....*....|....*....|....*....|....*....
gi 499404633 850 YLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQG 887
Cdd:cd17640 338 LTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
484-668 |
1.99e-11 |
|
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: 68.01 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 484 YSYQQLLGLSGQAAAALHERGVK--PGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVT 561
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 QADYQhrlasVFSGAIVLagHLLSSNAQAVALPTAESregqIAYVMFTSGSTGLPKGVEI-------GASALDHFTaaaR 634
Cdd:cd05927 86 DAGVK-----VYSLEEFE--KLGKKNKVPPPPPKPED----LATICYTSGTTGNPKGVMLthgnivsNVAGVFKIL---E 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 499404633 635 QRYGLRAEDRVLQFAPFN--FDASIEEVFatLTSGA 668
Cdd:cd05927 152 ILNKINPTDVYISYLPLAhiFERVVEALF--LYHGA 185
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
485-949 |
2.82e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 67.54 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQAAAAL-HERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQA 563
Cdd:PRK12492 51 SYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 564 DYQHRLASVFSGAIV--------------LAGHLLSSNAQAV-------ALPTAES-----REGQ-------------IA 604
Cdd:PRK12492 131 MFGKLVQEVLPDTGIeylieakmgdllpaAKGWLVNTVVDKVkkmvpayHLPQAVPfkqalRQGRglslkpvpvglddIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 605 YVMFTSGSTGLPKGVEIGASAL----DHFTAAARQR----YGLRAEDRVLQFAP---FNFDASIEEVFATLTSGATLVLR 673
Cdd:PRK12492 211 VLQYTGGTTGLAKGAMLTHGNLvanmLQVRACLSQLgpdgQPLMKEGQEVMIAPlplYHIYAFTANCMCMMVSGNHNVLI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 674 TDEmlESIPTFVEQVDAQAIT-LLDLPTAFwnewvVGLktgtLTMP-------SALRAIIIGGEAVYPEQLVQWQRHApd 745
Cdd:PRK12492 291 TNP--RDIPGFIKELGKWRFSaLLGLNTLF-----VAL----MDHPgfkdldfSALKLTNSGGTALVKATAERWEQLT-- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 746 TLRLINTYGPTETTVVATscdlqTQP-ADVAQL-PIGLPLAGV-------NALVLAAGDRpaaeGELVLLGPTLAAGYIG 816
Cdd:PRK12492 358 GCTIVEGYGLTETSPVAS-----TNPyGELARLgTVGIPVPGTalkviddDGNELPLGER----GELCIKGPQVMKGYWQ 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 817 T-EHTAFTLLAVGdrhlpAYRTGD-RVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGV 894
Cdd:PRK12492 429 QpEATAEALDAEG-----WFKTGDiAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSG 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499404633 895 RRLVAFVATKEGEIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK12492 504 EAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
605-945 |
3.13e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 66.25 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 605 YVMFTSGSTGLPKGV----------EIGASALDHFTAAARQRYGLRAED----RVLQFAPFNFDASIEEVFATLTSGATL 670
Cdd:cd05924 7 YILYTGGTTGMPKGVmwrqedifrmLMGGADFGTGEFTPSEDAHKAAAAaagtVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 671 VL-----RTDEMLESIPTfvEQV-------DAQAITLLDlptafwnewvvGLKTGTLTMPSALRAIIIGGEAVYPEQLVQ 738
Cdd:cd05924 87 VLpddrfDPEEVWRTIEK--HKVtsmtivgDAMARPLID-----------ALRDAGPYDLSSLFAISSGGALLSPEVKQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 739 WQRHAPDtLRLINTYGPTET----TVVATSCDLQTQPADVAQlpiglplagvNALVLAAGDR---PAAEGELVLLGPT-- 809
Cdd:cd05924 154 LLELVPN-ITLVDAFGSSETgftgSGHSAGSGPETGPFTRAN----------PDTVVLDDDGrvvPPGSGGVGWIARRgh 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 810 LAAGYIG-TEHTAFTLLAVGD-RH-LPayrtGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACV 885
Cdd:cd05924 223 IPLGYYGdEAKTAETFPEVDGvRYaVP----GDRATVEAdGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLV 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404633 886 QGIVYPNGVRRLVAFVATKEG-EIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVD 945
Cdd:cd05924 299 VGRPDERWGQEVVAVVQLREGaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
476-921 |
3.55e-11 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 67.10 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 476 ALAQRDRQ---------YSYQQLLGLSGQAAAALHERG------------VKPGERIGIMLNRSPETIISLLAVMQCGAV 534
Cdd:cd17632 40 ALGQRATElvtdpatgrTTLRLLPRFETITYAELWERVgavaaahdpeqpVRPGDFVAVLGFTSPDYATVDLALTRLGAV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 535 YVPLDPEQPRERQQHIIQIAGLRTIVTQADY------------------------------------QHRLASVFSGAIV 578
Cdd:cd17632 120 SVPLQAGASAAQLAPILAETEPRLLAVSAEHldlaveavleggtpprlvvfdhrpevdahraalesaRERLAAVGIPVTT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 579 L-AGHLLSSNAQAVALPTAESREGQIAYVMFTSGSTGLPKGVEIGASALDHF------TAAARQRYGLraedrVLQFAPF 651
Cdd:cd17632 200 LtLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFwlkvssIQDIRPPASI-----TLNFMPM 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 652 NFDASIEEVFATLTSGAT-------------------------LVLRTDEML------ESIPTFVEQVDAQaiTLLDLPT 700
Cdd:cd17632 275 SHIAGRISLYGTLARGGTayfaaasdmstlfddlalvrptelfLVPRVCDMLfqryqaELDRRSVAGADAE--TLAERVK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 701 AFWNEWVVGLKTGTLTMPSA-----LRAIIiggeavypEQLVQwqrhapdtLRLINTYGPTETTVVATSCDLQTQPAdva 775
Cdd:cd17632 353 AELRERVLGGRLLAAVCGSAplsaeMKAFM--------ESLLD--------LDLHDGYGSTEAGAVILDGVIVRPPV--- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 776 qlpIGLPLAGVNALVLAAGDRPAAEGELVLLGPTLAAGYIGT-EHTAFTLLAVGdrhlpAYRTGDRV-RLEKGHLLYLGR 853
Cdd:cd17632 414 ---LDYKLVDVPELGYFRTDRPHPRGELLVKTDTLFPGYYKRpEVTAEVFDEDG-----FYRTGDVMaELGPDRLVYVDR 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404633 854 MDNEFKIS-GYRIQPGEVEAHLLAQPEVDeacvQGIVYPNGVRR-LVAFVATKEGEIDA---RALKQRLSSVL 921
Cdd:cd17632 486 RNNVLKLSqGEFVTVARLEAVFAASPLVR----QIFVYGNSERAyLLAVVVPTQDALAGedtARLRAALAESL 554
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
964-1037 |
5.33e-11 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 59.48 E-value: 5.33e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404633 964 SETENRVSAIWQQILGV--SGIQSRDNFF-ELGGQSLQTIQIVNRLAAEFSVSIKVSDVFDHPQLSDFCRYLDDRLS 1037
Cdd:COG0236 4 EELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
480-952 |
1.84e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 64.38 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 480 RDRQYSYQQLLGLSGQAAAALH-ERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRT 558
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 559 IVTQADYqhrlasvfsgaivlaghllssnaqavalptaesregqIAYVMFTSGSTGLPKGVEI-------GASALDHFta 631
Cdd:cd05937 82 VIVDPDD-------------------------------------PAILIYTSGTTGLPKAAAIswrrtlvTSNLLSHD-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 632 aarqrYGLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRT--------DEMLESIPTFVEQVDAQAITLLDLPTAF 702
Cdd:cd05937 123 -----LNLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRkfsasqfwKDVRDSGATIIQYVGELCRYLLSTPPSP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 703 WNE-------WVVGLKTGTLTMPSALRAIIIGGE--AVYPEQLVQWQRHAPD-TLRLINTYGPT-----ETTVVATSCDL 767
Cdd:cd05937 198 YDRdhkvrvaWGNGLRPDIWERFRERFNVPEIGEfyAATEGVFALTNHNVGDfGAGAIGHHGLIrrwkfENQVVLVKMDP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 768 QTqpadvaQLPIGLPLAGVnALVLAAGDrpaaEGELVLLGP----TLAAGYIGTEH-TAFTLLA----VGDRHlpaYRTG 838
Cdd:cd05937 278 ET------DDPIRDPKTGF-CVRAPVGE----PGEMLGRVPfknrEAFQGYLHNEDaTESKLVRdvfrKGDIY---FRTG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 839 DRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFV------ATKEGEIDAR 911
Cdd:cd05937 344 DLLRQdADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAitleesSAVPTEFTKS 423
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 499404633 912 ALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAE 952
Cdd:cd05937 424 LLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
485-953 |
2.44e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 64.15 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQAD 564
Cdd:PRK08276 13 TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 565 YQHRLASVFSGAIVLAGHLLSSNAQAV-ALPTAESREGQIAY---------VM-FTSGSTGLPKGVEIGASALD------ 627
Cdd:PRK08276 93 LADTAAELAAELPAGVPLLLVVAGPVPgFRSYEEALAAQPDTpiadetagaDMlYSSGTTGRPKGIKRPLPGLDpdeapg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 628 HFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVL--RTD--EMLESIP----TFVEQVDAQAITLLDLP 699
Cdd:PRK08276 173 MMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVmeKFDaeEALALIEryrvTHSQLVPTMFVRMLKLP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 700 TAFWNEWVVglktgtltmpSALRAIIIGGEAVYPE---QLVQWQrhAPdtlRLINTYGPTET--TVVATSCDLQTQPADV 774
Cdd:PRK08276 253 EEVRARYDV----------SSLRVAIHAAAPCPVEvkrAMIDWW--GP---IIHEYYASSEGggVTVITSEDWLAHPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 775 aqlpiGLPLAGVNALVLAAGDRpaaegelvllgptLAAGYIGTEH-----TAFTLLAVGDRHLPAYRTGDRVRL-EKGHL 848
Cdd:PRK08276 318 -----GKAVLGEVRILDEDGNE-------------LPPGEIGTVYfemdgYPFEYHNDPEKTAAARNPHGWVTVgDVGYL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 849 -----LYLGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEIDARAL--------K 914
Cdd:PRK08276 380 dedgyLYLTDRKSDMIISgGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALaaeliawlR 459
|
490 500 510
....*....|....*....|....*....|....*....
gi 499404633 915 QRLSSVLPPAMIptDYRAfhQLPKTGSNKVDRKRLLAEY 953
Cdd:PRK08276 460 GRLAHYKCPRSI--DFED--ELPRTPTGKLYKRRLRDRY 494
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
718-946 |
2.83e-10 |
|
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: 63.06 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 718 PSALRaIIIGGEAvyPEQLVQWQRHAPDTLRLinTYGPTETTVVATSCDLQTQPADVaqlpiGLPLAGVNALVLAAGDRP 797
Cdd:cd17637 113 LSSLR-HVLGLDA--PETIQRFEETTGATFWS--LYGQTETSGLVTLSPYRERPGSA-----GRPGPLVRVRIVDDNDRP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 798 A---AEGELVLLGPTLAAGYIG-TEHTAFTLLavGDRHlpayRTGDRVRL-EKGHLLYLGRM-DNEF-KISGYRIQPGEV 870
Cdd:cd17637 183 VpagETGEIVVRGPLVFQGYWNlPELTAYTFR--NGWH----HTGDLGRFdEDGYLWYAGRKpEKELiKPGGENVYPAEV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 871 EAHLLAQPEVDEACVQGIVYPN---GVRrlvAFVATKEGE-IDARAL----KQRLSSVLPPAmiptdYRAF-HQLPKTGS 941
Cdd:cd17637 257 EKVILEHPAIAEVCVIGVPDPKwgeGIK---AVCVLKPGAtLTADELiefvGSRIARYKKPR-----YVVFvEALPKTAD 328
|
....*
gi 499404633 942 NKVDR 946
Cdd:cd17637 329 GSIDR 333
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
968-1027 |
2.86e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 56.80 E-value: 2.86e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404633 968 NRVSAIWQQILGVSG--IQSRDNFFELGGQSLQTIQIVNRLAAEFSVSIKVSDVFDHPQLSD 1027
Cdd:pfam00550 1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
461-949 |
2.92e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 64.24 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 461 LTAI-AKQArkNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYV-PL 538
Cdd:PRK10946 27 LTDIlTRHA--ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVnAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 DPEQPRERQQHIIQIAGLRTIvtqADYQHRL-----------ASVFSGAIVLAGH----------LLSSNAQAVALPTAe 597
Cdd:PRK10946 105 FSHQRSELNAYASQIEPALLI---ADRQHALfsdddflntlvAEHSSLRVVLLLNddgehslddaINHPAEDFTATPSP- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 598 srEGQIAYVMFTSGSTGLPKgvEIGASALDHFtaaarqrYGLRAEDRVLQF-----------APFNFDASIEEVFATLTS 666
Cdd:PRK10946 181 --ADEVAFFQLSGGSTGTPK--LIPRTHNDYY-------YSVRRSVEICGFtpqtrylcalpAAHNYPMSSPGALGVFLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 667 GATLVLRTDEMLESIPTFVEQVDAQAITLLDLPTAFWNEWVVglKTGTLTMPSALRAIIIGGeAVYPEQLVqwqRHAPDT 746
Cdd:PRK10946 250 GGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIA--EGGSRAQLASLKLLQVGG-ARLSETLA---RRIPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 747 L--RLINTYGPTETTVVATSCD------LQTQpadvaqlpiGLPLAGVNAL-VLAAGDRPAAEGELVLL---GPTLAAGY 814
Cdd:PRK10946 324 LgcQLQQVFGMAEGLVNYTRLDdsderiFTTQ---------GRPMSPDDEVwVADADGNPLPQGEVGRLmtrGPYTFRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 815 IGT-EHTAFTLLAVGdrhlpAYRTGDRV-RLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPN 892
Cdd:PRK10946 395 YKSpQHNASAFDANG-----FYCSGDLVsIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDEL 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404633 893 GVRRLVAFVATKEgEIDARALKQRLSSV-LPPAMIPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PRK10946 470 MGEKSCAFLVVKE-PLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
770-1040 |
4.14e-10 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 62.07 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 770 QPADVAQLPIGLPLAGVNALVLAAGDRPAAEGELVLLGPTLAAGYIGTEHTAFTLLAVGDRHLPAYRTGDRVRLEKGH-L 848
Cdd:COG3433 17 PPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGpG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 849 LYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDeACVQGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSVLPPAMIPT 928
Cdd:COG3433 97 GGLERLVQQVVIRAERGEEEELLLVLRAAAVVR-VAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 929 DYRAFHQLPKTGSNKVDRKR--------LLAEYHDDAPTQALAsETENRVSAIWQQILGVS--GIQSRDNFFELGGQSLQ 998
Cdd:COG3433 176 SAVVALDALLLLALKVVARAapalaaaeALLAAASPAPALETA-LTEEELRADVAELLGVDpeEIDPDDNLFDLGLDSIR 254
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499404633 999 TIQIVNRLAAEfSVSIKVSDVFDHPQLSDFCRYLDDRLSQDE 1040
Cdd:COG3433 255 LMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
485-949 |
1.44e-09 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 61.78 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQAAAALHER-GVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDP-EQPRERQQHI------------ 550
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPsSSLGEIKKRVvdcsvglaftsp 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 551 -----IQIAGLRTIVTQADYQHRlasvfSGAIVLAG--HLLSSNAQAVALPTAesREGQIAYVMFTSGSTGLPKGVEIG- 622
Cdd:PLN02574 148 envekLSPLGVPVIGVPENYDFD-----SKRIEFPKfyELIKEDFDFVPKPVI--KQDDVAAIMYSSGTTGASKGVVLTh 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 623 ---ASALDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFAT--LTSGATLVL--RTD--EMLESIPTF-VEQVDAQA 692
Cdd:PLN02574 221 rnlIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVglLSLGSTIVVmrRFDasDMVKVIDRFkVTHFPVVP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 693 ITLLDLPTAfwNEWVVGLKTGTLTMPSALRAIIIGGeavYPEQLVQWQRHapdtLRLINTYGPTETTVVATSCDLQTQPA 772
Cdd:PLN02574 301 PILMALTKK--AKGVCGEVLKSLKQVSCGAAPLSGK---FIQDFVQTLPH----VDFIQGYGMTESTAVGTRGFNTEKLS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 773 DVAQlpIGLPLAGVNALVL----AAGDRPAAEGELVLLGPTLAAGYI-GTEHTAFTllAVGDRHLpayRTGDRVRL-EKG 846
Cdd:PLN02574 372 KYSS--VGLLAPNMQAKVVdwstGCLLPPGNCGELWIQGPGVMKGYLnNPKATQST--IDKDGWL---RTGDIAYFdEDG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 847 HLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE-IDARALKQRLSSVLPPAM 925
Cdd:PLN02574 445 YLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGStLSQEAVINYVAKQVAPYK 524
|
490 500
....*....|....*....|....
gi 499404633 926 IPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PLN02574 525 KVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
485-949 |
1.75e-09 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 61.43 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQ-AAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDP-EQPRERQQHIIQiAGLRTIVTQ 562
Cdd:PRK08751 52 TYREADQLVEQfAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPlYTPRELKHQLID-SGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 563 ADYQHRLASVFSGAIVLA------GHLLS-----------------------SNA----QAVAL------PTAESREGQI 603
Cdd:PRK08751 131 DNFGTTVQQVIADTPVKQvittglGDMLGfpkaalvnfvvkyvkklvpeyriNGAirfrEALALgrkhsmPTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 604 AYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYG-----LRAEDRVLQFAP----FNFDASiEEVFATLTSGATLVLRT 674
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPlyhiFALTAN-GLVFMKIGGCNHLISNP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 675 DEMlesiPTFVEQVDAQAITLLDLPTAFWNewvvglktGTLTMP-------SALRAIIIGGEAVYPEQLVQWQRHApdTL 747
Cdd:PRK08751 290 RDM----PGFVKELKKTRFTAFTGVNTLFN--------GLLNTPgfdqidfSSLKMTLGGGMAVQRSVAERWKQVT--GL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 748 RLINTYGPTETTVVAtsCdlqTQPADVAQL--PIGLPLAGVNALV-------LAAGDRpaaeGELVLLGPTLAAGYIG-T 817
Cdd:PRK08751 356 TLVEAYGLTETSPAA--C---INPLTLKEYngSIGLPIPSTDACIkddagtvLAIGEI----GELCIKGPQVMKGYWKrP 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 818 EHTAFTLLAVGDRHlpayrTGDRVRLEKGHLLYL-GRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRR 896
Cdd:PRK08751 427 EETAKVMDADGWLH-----TGDIARMDEQGFVYIvDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEI 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499404633 897 LVAFVATKEGEIDARALKQRLSSVLPPAMIP--TDYRAfhQLPKTGSNKVDRKRL 949
Cdd:PRK08751 502 VKVVIVKKDPALTAEDVKAHARANLTGYKQPriIEFRK--ELPKTNVGKILRREL 554
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
481-956 |
3.10e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 60.52 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 481 DRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIV 560
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 561 TQadyqhrlasvfsgaivLAGHLLSsnAQAVALPTAESRE--GQIAYVmFTSGSTGLPKGVEIGASALDHFTAAARQRYG 638
Cdd:cd05939 81 FN----------------LLDPLLT--QSSTEPPSQDDVNfrDKLFYI-YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 639 LRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRT--------DEMLESIPTFVEQVDAQAITLLDLP-TAFWNEWVV 708
Cdd:cd05939 142 MRPEDVVYDCLPlYHSAGGIMGVGQALLHGSTVVIRKkfsasnfwDDCVKYNCTIVQYIGEICRYLLAQPpSEEEQKHNV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 709 GLKTGtltmpSALRAIIIggeavypEQLVQwQRHAPdtlRLINTYGPTETTVVATSCDLQT-----QPADVAQL-PIGL- 781
Cdd:cd05939 222 RLAVG-----NGLRPQIW-------EQFVR-RFGIP---QIGEFYGATEGNSSLVNIDNHVgacgfNSRILPSVyPIRLi 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 782 --------PLAGVNALVLAAgdRPAAEGELVllG------PTLA-AGYIGTEHT----AFTLLAVGDRhlpAYRTGD-RV 841
Cdd:cd05939 286 kvdedtgeLIRDSDGLCIPC--QPGEPGLLV--GkiiqndPLRRfDGYVNEGATnkkiARDVFKKGDS---AFLSGDvLV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 842 RLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRL-VAFVATKEGEIDARALKQRLSSV 920
Cdd:cd05939 359 MDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAgMAAIVDPERKVDLDRFSAVLAKS 438
|
490 500 510
....*....|....*....|....*....|....*.
gi 499404633 921 LPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDD 956
Cdd:cd05939 439 LPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
465-671 |
4.24e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 60.21 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 465 AKQARKNPSHIALAQRDRQ--YSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQ 542
Cdd:PRK08315 23 DRTAARYPDREALVYRDQGlrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 543 PRERQQHIIQIAGLRTIVT-----QADYQHRLASVFSG-AIVLAGHLLSSN---------------------AQAVALPT 595
Cdd:PRK08315 103 RLSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPElATCEPGQLQSARlpelrrviflgdekhpgmlnfDELLALGR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 596 AESREgQIAYVM------------FTSGSTGLPKGVeigasALDH-------FTAAARQRYGlrAEDRVLQFAPFN--Fd 654
Cdd:PRK08315 183 AVDDA-ELAARQatldpddpiniqYTSGTTGFPKGA-----TLTHrnilnngYFIGEAMKLT--EEDRLCIPVPLYhcF- 253
|
250
....*....|....*..
gi 499404633 655 ASIEEVFATLTSGATLV 671
Cdd:PRK08315 254 GMVLGNLACVTHGATMV 270
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
956-1036 |
4.63e-09 |
|
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: 54.18 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 956 DAPTQALASETENRVSAIWQQILGVSG---IQSRDNFFELGGQSLQTIQIVNRLAAEFSVSIKVSDVFDHPQLSDFCRYL 1032
Cdd:smart00823 3 ALPPAERRRLLLDLVREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
|
....
gi 499404633 1033 DDRL 1036
Cdd:smart00823 83 AAEL 86
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
482-959 |
1.14e-08 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 59.19 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVY-------------VPLDPEQPRErqq 548
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHsvvfggfashslaARIDDAKPVL--- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 549 hIIQI-AGLR--TIVtqaDYQHRLASvfsgAIVLAGH----LLSSNAQAVALPTAESRE--------------------- 600
Cdd:PRK10524 160 -IVSAdAGSRggKVV---PYKPLLDE----AIALAQHkprhVLLVDRGLAPMARVAGRDvdyatlraqhlgarvpvewle 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 601 -GQIAYVMFTSGSTGLPKGVE--IG------ASALDH-FTAAARQRYglraedrvlqfapfnFDAS----------IeeV 660
Cdd:PRK10524 232 sNEPSYILYTSGTTGKPKGVQrdTGgyavalATSMDTiFGGKAGETF---------------FCASdigwvvghsyI--V 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 661 FATLTSGATLVlrtdeMLESIPT---------FVEQVdaQAITLLDLPTA------FWNEWvvgLKTGTLtmpSALRAII 725
Cdd:PRK10524 295 YAPLLAGMATI-----MYEGLPTrpdagiwwrIVEKY--KVNRMFSAPTAirvlkkQDPAL---LRKHDL---SSLRALF 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 726 IGGEAVyPEQLVQWqrhAPDTLR--LINTYGPTETtvvatSCDLQTQPADVAQLPI-----GLPLAGVNALVL--AAGDr 796
Cdd:PRK10524 362 LAGEPL-DEPTASW---ISEALGvpVIDNYWQTET-----GWPILAIARGVEDRPTrlgspGVPMYGYNVKLLneVTGE- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 797 PAAEGE---LVLLGPtLAAGYIGT--------EHTAFTLLavgDRHLpaYRTGD-RVRLEKGHLLYLGRMDNEFKISGYR 864
Cdd:PRK10524 432 PCGPNEkgvLVIEGP-LPPGCMQTvwgdddrfVKTYWSLF---GRQV--YSTFDwGIRDADGYYFILGRTDDVINVAGHR 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 865 IQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-----EIDARALK--------QRLSSVLPPAMIptdyR 931
Cdd:PRK10524 506 LGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSdsladREARLALEkeimalvdSQLGAVARPARV----W 581
|
570 580 590
....*....|....*....|....*....|..
gi 499404633 932 AFHQLPKTGSNKVDRKRL--LAEYHD--DAPT 959
Cdd:PRK10524 582 FVSALPKTRSGKLLRRAIqaIAEGRDpgDLTT 613
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
3-328 |
1.32e-08 |
|
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: 58.48 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCG-LWLGHALNDDKATFNTaECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVevaGEHAEQPeIGFVASQLPV 81
Cdd:cd19547 3 PLAPMQEGmLFRGLFWPDSDAYFNQ-NVLELVGGTDEDVLREAWRRVADRYEILRTGFT---WRDRAEP-LQYVRDDLAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 82 PIGVLPIVELLPapmTDEEQTIRQWARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQI 160
Cdd:cd19547 78 PWALLDWSGEDP---DRRAELLERLLADDRAAGLSLADCPLYRLTLVrLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 161 YTALTAGQSAPVAEFGPFSAVLEEERQRDASGQtaQARDFWLETLNAMpEPASFSEKKAPIAARFLRQSCDMPADLWQPL 240
Cdd:cd19547 155 YEELAHGREPQLSPCRPYRDYVRWIRARTAQSE--ESERFWREYLRDL-TPSPFSTAPADREGEFDTVVHEFPEQLTRLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 241 SALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNR---IGSASLMVpSMQMNIVPLCIQVDEQANFVALAQQVA 317
Cdd:cd19547 232 NEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppeLEGSEHMV-GIFINTIPLRIRLDPDQTVTGLLETIH 310
|
330
....*....|.
gi 499404633 318 RTKRTLRRHQH 328
Cdd:cd19547 311 RDLATTAAHGH 321
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
485-945 |
1.64e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.82 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLgLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGavYVPLdpeqprerqqhII------------- 551
Cdd:PRK06814 660 TYRKLL-TGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAG--RVPA-----------MInfsagianilsac 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 QIAGLRTIVTQADY--QHRLASV---------------FSGAIVLAGHLLSSNAQAVALPTAESREGQ-IAYVMFTSGST 613
Cdd:PRK06814 726 KAAQVKTVLTSRAFieKARLGPLiealefgiriiyledVRAQIGLADKIKGLLAGRFPLVYFCNRDPDdPAVILFTSGSE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 614 GLPKGVeigasALDH-------FTAAARQRYGlrAEDRVLQFAPfnfdasieeVFAT--LTSGATLvlrtdEMLESIPTF 684
Cdd:PRK06814 806 GTPKGV-----VLSHrnllanrAQVAARIDFS--PEDKVFNALP---------VFHSfgLTGGLVL-----PLLSGVKVF 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 685 V-----------EQVDAQAITLLdlptafwnewvvgLKTGTLTMPSA----------LRAIIIGGEAVYPEQLVQW-QRH 742
Cdd:PRK06814 865 LypsplhyriipELIYDTNATIL-------------FGTDTFLNGYAryahpydfrsLRYVFAGAEKVKEETRQTWmEKF 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 743 ApdtLRLINTYGPTETT-VVATSCDLQTQPADVAQLPIGL-----PLAGVNalvlaagdrpaAEGELVLLGPTLAAGYIG 816
Cdd:PRK06814 932 G---IRILEGYGVTETApVIALNTPMHNKAGTVGRLLPGIeyrlePVPGID-----------EGGRLFVRGPNVMLGYLR 997
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 817 TE-HTAFTLLAVGdrhlpAYRTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAhlLAQ---PEVDEACVQgivYP 891
Cdd:PRK06814 998 AEnPGVLEPPADG-----WYDTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEE--LAAelwPDALHAAVS---IP 1067
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404633 892 NGVR--RLVAFVatkEGEIDARA--LKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVD 945
Cdd:PRK06814 1068 DARKgeRIILLT---TASDATRAafLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
482-885 |
2.40e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 58.07 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVT 561
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 562 QADYQHRLASVFSGAIVLAGHLLSSNAQAVALPTAESREG-----------QIAYVMFTSGSTGLPKGVeigasALDHFT 630
Cdd:PLN02330 134 NDTNYGKVKGLGLPVIVLGEEKIEGAVNWKELLEAADRAGdtsdneeilqtDLCALPFSSGTTGISKGV-----MLTHRN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 631 AAAR---QRYGLRAED----RVLQFAPFNFDASIEEV-FATLTSGATLV------LRT--DEMLESIPTFVEQVDAQAIT 694
Cdd:PLN02330 209 LVANlcsSLFSVGPEMigqvVTLGLIPFFHIYGITGIcCATLRNKGKVVvmsrfeLRTflNALITQEVSFAPIVPPIILN 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 695 LLDLPTAfwNEW-VVGLKtgtltmpsaLRAIIIGGEAVYPEQLVQWQRHAPDtLRLINTYGPTE-TTVVATSCDLQTQPA 772
Cdd:PLN02330 289 LVKNPIV--EEFdLSKLK---------LQAIMTAAAPLAPELLTAFEAKFPG-VQVQEAYGLTEhSCITLTHGDPEKGHG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 773 DVAQLPIGLPLAGV--------NALVLAAGdrpaAEGELVLLGPTLAAGYI-GTEHTAFTLLAVGDRHlpayrTGDRVRL 843
Cdd:PLN02330 357 IAKKNSVGFILPNLevkfidpdTGRSLPKN----TPGELCVRSQCVMQGYYnNKEETDRTIDEDGWLH-----TGDIGYI 427
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 499404633 844 EK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACV 885
Cdd:PLN02330 428 DDdGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
483-955 |
2.52e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 57.79 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 483 QYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHII----------- 551
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVnhaedryvlfd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 552 --------QIAG----LRTIVTQADYQHRLASvfSGAIVLAGHLLSSNAQAVALPTAEsrEGQIAYVMFTSGSTGLPKGV 619
Cdd:PRK07008 119 ltflplvdALAPqcpnVKGWVAMTDAAHLPAG--STPLLCYETLVGAQDGDYDWPRFD--ENQASSLCYTSGTTGNPKGA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 620 EIG--ASALDHFTAAARQRYGLRAEDRVLQFAP-FNFDASIEEVFATLTsGATLVL---RTD-----EMLESiptfvEQV 688
Cdd:PRK07008 195 LYShrSTVLHAYGAALPDAMGLSARDAVLPVVPmFHVNAWGLPYSAPLT-GAKLVLpgpDLDgkslyELIEA-----ERV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 689 DAQAitllDLPTAfWNEWVVGLKTGTLTMpSALRAIIIGGEAVYPEQLVQWQRHApdTLRLINTYGPTETTVVATSCDL- 767
Cdd:PRK07008 269 TFSA----GVPTV-WLGLLNHMREAGLRF-STLRRTVIGGSACPPAMIRTFEDEY--GVEVIHAWGMTEMSPLGTLCKLk 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 768 --QTQPADVAQLPI----GLPLAGVN-ALVLAAG-DRP---AAEGELVLLGPTLAAGYIGTEHTAFTllavgDRHLPayr 836
Cdd:PRK07008 341 wkHSQLPLDEQRKLlekqGRVIYGVDmKIVGDDGrELPwdgKAFGDLQVRGPWVIDRYFRGDASPLV-----DGWFP--- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 837 TGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEG-EIDARALK 914
Cdd:PRK07008 413 TGDVATIDAdGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGaEVTREELL 492
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 499404633 915 QRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHD 955
Cdd:PRK07008 493 AFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRD 533
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
482-672 |
2.84e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 57.88 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 482 RQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPE-QPR---ERQQHI---IQIA 554
Cdd:PRK03584 113 RELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDfGVQgvlDRFGQIepkVLIA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 555 ------GLRTIVTQADYQHRLASVFS-GAIVL-----AGHLLSSNAQAVALP--TAESREGQIA----------YVMFTS 610
Cdd:PRK03584 193 vdgyryGGKAFDRRAKVAELRAALPSlEHVVVvpylgPAAAAAALPGALLWEdfLAPAEAAELEfepvpfdhplWILYSS 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499404633 611 GSTGLPKGVEIGASA--LDHFTAAARQrYGLRAEDRVLQFAP-----FNFDASieevfaTLTSGATLVL 672
Cdd:PRK03584 273 GTTGLPKCIVHGHGGilLEHLKELGLH-CDLGPGDRFFWYTTcgwmmWNWLVS------GLLVGATLVL 334
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
431-945 |
4.87e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 57.03 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 431 SGELLGRWLREERelalITSREPEPFVEPVLTAIAKQARKNP--SHIALaqrdRQYSYQQLLGLSGQAAAALhERGVKPG 508
Cdd:PRK08043 185 AGEMLHQIMMEAR----MAVRPRETLYEALLSAQYRYGAGKPciEDVNF----TPDSYRKLLKKTLFVGRIL-EKYSVEG 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 509 ERIGIMLnrsPETIISLLAVMqcGAVY---VP--LDPEQPRERQQHIIQIAGLRTIVTQADYQHR---------LASV-- 572
Cdd:PRK08043 256 ERIGLML---PNATISAAVIF--GASLrrrIPamMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKgklwhlpeqLTQVrw 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 573 -----FSGAIVLA------GHLLSSNAQAVALPTAESregqiAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRA 641
Cdd:PRK08043 331 vyledLKDDVTTAdklwifAHLLMPRLAQVKQQPEDA-----ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTP 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 642 EDRVLQFAPF--NFDASIEeVFATLTSGATLVLRTDEM-LESIPtfvEQVDAQAITLLDLPTAFWNEWvvglktGTLTMP 718
Cdd:PRK08043 406 NDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSPLhYRIVP---ELVYDRNCTVLFGTSTFLGNY------ARFANP 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 719 ---SALRAIIIGGEAVYPEQLVQWQrhapDT--LRLINTYGPTETT-VVATSCDLQTQPADVAQLpiglpLAGVNALVLA 792
Cdd:PRK08043 476 ydfARLRYVVAGAEKLQESTKQLWQ----DKfgLRILEGYGVTECApVVSINVPMAAKPGTVGRI-----LPGMDARLLS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 793 AgdrPAAE--GELVLLGPTLAAGYIGTEH-------TAFTllAVGDRHLPAYRTGDRVRL-EKGHLLYLGRMDNEFKISG 862
Cdd:PRK08043 547 V---PGIEqgGRLQLKGPNIMNGYLRVEKpgvlevpTAEN--ARGEMERGWYDTGDIVRFdEQGFVQIQGRAKRFAKIAG 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 863 YRIQPGEVEA-HLLAQPEVDEACVqgiVYPNGVR--RLVAFvaTKEGEIDARAL-KQRLSSVLPPAMIPTDYRAFHQLPK 938
Cdd:PRK08043 622 EMVSLEMVEQlALGVSPDKQHATA---IKSDASKgeALVLF--TTDSELTREKLqQYAREHGVPELAVPRDIRYLKQLPL 696
|
....*..
gi 499404633 939 TGSNKVD 945
Cdd:PRK08043 697 LGSGKPD 703
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
495-946 |
5.99e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 56.54 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 495 QAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPR-------ERQQHIIQIAGLRTIVTQADYQh 567
Cdd:PRK07768 41 RIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRtdlavwaEDTLRVIGMIGAKAVVVGEPFL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 568 RLASVFSGAIVLAGHLLSSNAQAVALPTaESREGQIAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRYGLRAE-DRVL 646
Cdd:PRK07768 120 AAAPVLEEKGIRVLTVADLLAADPIDPV-ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 647 QFAPFNFDASIEEVFAT-LTSGATLVLRT-DEMLESIPTFVEQVDAQAITLLDLP----TAFWNEWVVGLKTGTLTMpSA 720
Cdd:PRK07768 199 SWLPLFHDMGMVGFLTVpMYFGAELVKVTpMDFLRDPLLWAELISKYRGTMTAAPnfayALLARRLRRQAKPGAFDL-SS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 721 LRAIIIGGEAVYPEQ----LVQWQRHAPDTLRLINTYGPTETTVVAT-------------SCDL--------QTQPADVA 775
Cdd:PRK07768 278 LRFALNGAEPIDPADvedlLDAGARFGLRPEAILPAYGMAEATLAVSfspcgaglvvdevDADLlaalrravPATKGNTR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 776 QLP-IGLPLAGVNALVLAAGDRPAAE---GELVLLGPTLAAGYIGTehtaftllavgDRHLPA------YRTGDRVRL-E 844
Cdd:PRK07768 358 RLAtLGPPLPGLEVRVVDEDGQVLPPrgvGVIELRGESVTPGYLTM-----------DGFIPAqdadgwLDTGDLGYLtE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 845 KGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRR----LVAFVATKEGEIDARALKQRLSS- 919
Cdd:PRK07768 427 EGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSRegfaVAVESNAFEDPAEVRRIRHQVAHe 506
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499404633 920 -------------VLPPAMIptdyrafhqlPKTGSNKVDR 946
Cdd:PRK07768 507 vvaevgvrprnvvVLGPGSI----------PKTPSGKLRR 536
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
518-961 |
6.34e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 56.36 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 518 SPETIISLLAVMQCGAVYVPL----DPEQPRERqqhiIQIAGLRTIVTQaDYQHRLASVFSgaivLAGHLLSSN-AQAVA 592
Cdd:PLN03051 4 TVDAVIIYLAIVLAGCVVVSVadsfSAKEIATR----LDISGAKGVFTQ-DVVLRGGRALP----LYSKVVEAApAKAIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 593 LPTAES------REGQIAY------------------------------VMFTSGSTGLPKGVEIGASALDHFTAAARQR 636
Cdd:PLN03051 75 LPAAGEpvavplREQDLSWcdflgvaaaqgsvggneyspvyapvesvtnILFSSGTTGEPKAIPWTHLSPLRCASDGWAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 637 YGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVLRTDEMLEsiPTFVEQVDAQAITLLDLPTAFWNEWvvgLKTGTLT 716
Cdd:PLN03051 155 MDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPLG--RGFGKFVQDAGVTVLGLVPSIVKAW---RHTGAFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 717 MP----SALRAIIIGGEAVYPEQlVQWQRHAPDTLRLINTY-GPTE-TTVVATSCDLQTQ-PADVAQLPIGLPLAGVNAL 789
Cdd:PLN03051 230 MEgldwSKLRVFASTGEASAVDD-VLWLSSVRGYYKPVIEYcGGTElASGYISSTLLQPQaPGAFSTASLGTRFVLLNDN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 790 VLAAGDRPAAEGELVLLGPTLAAG--YIGTEHTAFTLLAV---GDRHLPAYRTGDRV-RLEKGHLLYLGRMDNEFKISGY 863
Cdd:PLN03051 309 GVPYPDDQPCVGEVALAPPMLGASdrLLNADHDKVYYKGMpmyGSKGMPLRRHGDIMkRTPGGYFCVQGRADDTMNLGGI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 864 RIQPGEVE-AHLLAQPEVDEACVQGIVYPNG-VRRLVAFVAT---KEGEIDAR--ALKQRLSSVLPPAMIP----TDYRA 932
Cdd:PLN03051 389 KTSSVEIErACDRAVAGIAETAAVGVAPPDGgPELLVIFLVLgeeKKGFDQARpeALQKKFQEAIQTNLNPlfkvSRVKI 468
|
490 500
....*....|....*....|....*....
gi 499404633 933 FHQLPKTGSNKVDRKRLLAEYHDDAPTQA 961
Cdd:PLN03051 469 VPELPRNASNKLLRRVLRDQLKKELSGRS 497
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
496-960 |
1.11e-07 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 55.83 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 496 AAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDP-EQPRErQQHIIQIAGLRTIVTQADYQHRLAS-VF 573
Cdd:PRK08974 62 AAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPlYTPRE-LEHQLNDSGAKAIVIVSNFAHTLEKvVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 574 SGAI---VLA--GHLLSSNAQAVA---------------LPTAES--------REGQ----------IAYVMFTSGSTGL 615
Cdd:PRK08974 141 KTPVkhvILTrmGDQLSTAKGTLVnfvvkyikrlvpkyhLPDAISfrsalhkgRRMQyvkpelvpedLAFLQYTGGTTGV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 616 PKGveigaSALDHFTAAARqryglraedrVLQ----FAPFNFDAS--------IEEVFAtLTS--------GATLVLRTD 675
Cdd:PRK08974 221 AKG-----AMLTHRNMLAN----------LEQakaaYGPLLHPGKelvvtalpLYHIFA-LTVncllfielGGQNLLITN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 676 EmlESIPTFVEQVDAQAITLLDLPTAFWNEWVVGLKTGTLTMpSALRAIIIGGEAVypEQLV--QWQRHApdTLRLINTY 753
Cdd:PRK08974 285 P--RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDF-SSLKLSVGGGMAV--QQAVaeRWVKLT--GQYLLEGY 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 754 GPTETTVVATSCdlqtqPADVAQL--PIGLPLAGVNALVL--AAGDRPAAE-GELVLLGPTLAAGYIG-TEHTAFTL--- 824
Cdd:PRK08974 358 GLTECSPLVSVN-----PYDLDYYsgSIGLPVPSTEIKLVddDGNEVPPGEpGELWVKGPQVMLGYWQrPEATDEVIkdg 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 825 -LAvgdrhlpayrTGDRVRL-EKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIvyPNGVR-RLV-AF 900
Cdd:PRK08974 433 wLA----------TGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV--PSEVSgEAVkIF 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 901 VATKEGEIDARALKQRLSSVLPPAMIPTDYRAFHQLPKTGSNKVDRKRLLAEYHDDAPTQ 960
Cdd:PRK08974 501 VVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 560
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
3-210 |
1.55e-07 |
|
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: 55.12 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEhaeqpeigfvASQLPVP 82
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGG----------PYQVVLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 IGVLPiVELLPAPMTDEEQTIRqwARDEISLPLDLLNGLPCRFALL-CGEKRDFLYSCVHHIALDGFGTTMLFQRIAQIY 161
Cdd:cd19540 73 AAEAR-PDLTVVDVTEDELAAR--LAEAARRGFDLTAELPLRARLFrLGPDEHVLVLVVHHIAADGWSMAPLARDLATAY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404633 162 TALTAGQsAPvaEFGP-------FS----AVLEEERQRD--ASGQTaqarDFWLETLNAMPE 210
Cdd:cd19540 150 AARRAGR-AP--DWAPlpvqyadYAlwqrELLGDEDDPDslAARQL----AYWRETLAGLPE 204
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
480-674 |
2.27e-07 |
|
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: 54.60 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 480 RDRQYSYQQLLGLSGQAAAALH-ERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRT 558
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 559 IVTQADYQHRLASVF-------------SGAIVLAG--HLLSSNAQAVALPTAESREGQI-----AYVMFTSGSTGLPKg 618
Cdd:cd05938 82 LVVAPELQEAVEEVLpalradgvsvwylSHTSNTEGviSLLDKVDAASDEPVPASLRAHVtikspALYIYTSGTTGLPK- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404633 619 veigASALDHFTAAARQRY----GLRAEDRVLQFAP-FNFDASIEEVFATLTSGATLVLRT 674
Cdd:cd05938 161 ----AARISHLRVLQCSGFlslcGVTADDVIYITLPlYHSSGFLLGIGGCIELGATCVLKP 217
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
601-921 |
9.59e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.46 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 601 GQIAYVMFTSGSTGLPKGVEIGASALDH--------FTAAarqryGLRAEDRVlQFAP--------FNFDASIEEVfatl 664
Cdd:COG1541 83 EEIVRIHASSGTTGKPTVVGYTRKDLDRwaelfarsLRAA-----GVRPGDRV-QNAFgyglftggLGLHYGAERL---- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 665 tsGATLV----LRTDEMLESIPTFveQVDA------QAITLLDlptafwnewvVGLKTGTLTMPSALRAIIIGGEAVyPE 734
Cdd:COG1541 153 --GATVIpaggGNTERQLRLMQDF--GPTVlvgtpsYLLYLAE----------VAEEEGIDPRDLSLKKGIFGGEPW-SE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 735 QLVQW--QRHApdtLRLINTYGPTETTV-VATSCDLQT--------------QPADVAQLPIGlplagvnalvlaagdrp 797
Cdd:COG1541 218 EMRKEieERWG---IKAYDIYGLTEVGPgVAYECEAQDglhiwedhflveiiDPETGEPVPEG----------------- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 798 aAEGELVL--LGPTlaagyigtehtAFTLLavgdRhlpaYRTGDRVRLEKG----------HLLYLGRMDNEFKISGYRI 865
Cdd:COG1541 278 -EEGELVVttLTKE-----------AMPLI----R----YRTGDLTRLLPEpcpcgrthprIGRILGRADDMLIIRGVNV 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 866 QPGEVEAHLLAQPEVdEACVQGIVYPNGVR-RLVAFVATKEG---EIDARALKQRLSSVL 921
Cdd:COG1541 338 FPSQIEEVLLRIPEV-GPEYQIVVDREGGLdELTVRVELAPGaslEALAEAIAAALKAVL 396
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
3-334 |
1.98e-06 |
|
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: 51.71 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 3 PLSVAQCGLWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGEhAEQPEIGFVASQlpvp 82
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGD-VHQRILDADAAR---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 83 igvlpiVELLPAPMTDEEQTIRqwARDEISLPLDLLNGLPCR---FALlcGEKRDFLYSCVHHIALDGFGTTMLFQRIAQ 159
Cdd:cd19546 81 ------PELPVVPATEEELPAL--LADRAAHLFDLTRETPWRctlFAL--SDTEHVLLLVVHRIAADDESLDVLVRDLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 160 IYTALTAGQS---APVA-EFGPFsAVLEEERQRDASGQTAQARD---FWLETLNAMPEPAS--FSEKKAPIAARFLRQ-S 229
Cdd:cd19546 151 AYGARREGRAperAPLPlQFADY-ALWERELLAGEDDRDSLIGDqiaYWRDALAGAPDELElpTDRPRPVLPSRRAGAvP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 230 CDMPADLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGSASLmVPSMQMNIVPLCIQVDEQAN- 308
Cdd:cd19546 230 LRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEGDL-EGMVGPFARPLALRTDLSGDp 308
|
330 340
....*....|....*....|....*..
gi 499404633 309 -FVALAQQVARTKRTLRRHQHYRYEHL 334
Cdd:cd19546 309 tFRELLGRVREAVREARRHQDVPFERL 335
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
835-949 |
2.36e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 51.82 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 835 YRTGDRVRLEK-GHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGEIDARAL 913
Cdd:PLN02654 515 YFSGDGCSRDKdGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEEL 594
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499404633 914 KQRLSSVLPPAM----IPTDYRAFHQLPKTGSNKVDRKRL 949
Cdd:PLN02654 595 RKSLILTVRNQIgafaAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
118-427 |
5.61e-06 |
|
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: 49.99 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 118 LNGLPCRFALLCGEKRD-FLYSCVHHIALDGFGTTMLFQRIAQIYtalTAGQSAPVAEFGPFSAVLeeeRQRDasgqTAQ 196
Cdd:cd19545 97 LGGPLVRLALVEDPDTErYFVWTIHHALYDGWSLPLILRQVLAAY---QGEPVPQPPPFSRFVKYL---RQLD----DEA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 197 ARDFW---LETLNAMPEPASFSEKKAPIAARFLRQSCDMPADLWQP--LSALCegnKISWpdlflAMLATHLklvSGSDR 271
Cdd:cd19545 167 AAEFWrsyLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGvtLATVL---RAAW-----ALVLSRY---TGSDD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 272 LTFGMMVMNRigsaSLMVPS-MQM-----NIVPLCIQVDEQANFVALAQQVARTKRTLRRHQHYRYEHLRRdLNRVGGEQ 345
Cdd:cd19545 236 VVFGVTLSGR----NAPVPGiEQIvgptiATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRR-LGPDARAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 346 RLFGPLINImpfdHPLNYGSLSSSTLNLSAGPVED--------LTIEIHFKPDGtpvLDFDAN--PACYSAEALASLQET 415
Cdd:cd19545 311 CNFQTLLVV----QPALPSSTSESLELGIEEESEDledfssygLTLECQLSGSG---LRVRARydSSVISEEQVERLLDQ 383
|
330
....*....|..
gi 499404633 416 LFTLLQRWLAQP 427
Cdd:cd19545 384 FEHVLQQLASAP 395
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
468-626 |
7.94e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 49.84 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 468 ARKNPSHIALAQRDRQYS---------YQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL 538
Cdd:PLN02861 53 VKKYPNNQMLGRRQVTDSkvgpyvwltYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 DPEQPRERQQHIIQIAGLRTIVTQadyQHRLASVFS---------GAIVLAGHLLSS---------------------NA 588
Cdd:PLN02861 133 YDTLGANAVEFIINHAEVSIAFVQ---ESKISSILSclpkcssnlKTIVSFGDVSSEqkeeaeelgvscfsweefslmGS 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 499404633 589 QAVALPtaESREGQIAYVMFTSGSTGLPKGVEIGASAL 626
Cdd:PLN02861 210 LDCELP--PKQKTDICTIMYTSGTTGEPKGVILTNRAI 245
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
143-347 |
9.10e-06 |
|
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: 49.41 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 143 IALDGFGTTMLFQRIAQIYTalTAGQSAPVAEFGpFSAVLEEERQRDASgQTAQARDFWLETLNAMPEPASFSEKKAP-- 220
Cdd:cd19535 135 LVADALSLQILLRELAALYE--DPGEPLPPLELS-FRDYLLAEQALRET-AYERARAYWQERLPTLPPAPQLPLAKDPee 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 221 -IAARFLRQSCDMPADLWQPLSALCEGNKISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNRIGsaslMVPSM-QM---- 294
Cdd:cd19535 211 iKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLP----LHPDVnDVvgdf 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499404633 295 -NIVPLCIQVDEQANFVALAQQVartKRTLRR-HQHYRY---EHLRRDLNRVGGEQRL 347
Cdd:cd19535 287 tSLLLLEVDGSEGQSFLERARRL---QQQLWEdLDHSSYsgvVVVRRLLRRRGGQPVL 341
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
603-881 |
9.79e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 49.73 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 603 IAYVMFTSGSTGLPKGVEIGASALDHFTAAARQRY-GLRAEDRVLQFAPFN--FDASIEEVFATL--------------- 664
Cdd:PLN02387 252 IAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAhiLELAAESVMAAVgaaigygspltltdt 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 665 -------TSGATLVLRTDEMLeSIPTFVE--------QVDAQ---AITLLDLPTA-------------------FWNEWV 707
Cdd:PLN02387 332 snkikkgTKGDASALKPTLMT-AVPAILDrvrdgvrkKVDAKgglAKKLFDIAYKrrlaaiegswfgawgleklLWDALV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 708 vgLKTGTLTMPSALRAIIIGGEAVypeqlvqwqrhAPDTLRLINT---------YGPTETTVVATScdlqTQPADVAQLP 778
Cdd:PLN02387 411 --FKKIRAVLGGRIRFMLSGGAPL-----------SGDTQRFINIclgapigqgYGLTETCAGATF----SEWDDTSVGR 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 779 IG--LPLAGVNALVLAAG-----DRPAAEGELVLLGPTLAAGYIGTEHTAFTLLAVGDRHLPAYRTGDRVRL-EKGHLLY 850
Cdd:PLN02387 474 VGppLPCCYVKLVSWEEGgylisDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDERGMRWFYTGDIGQFhPDGCLEI 553
|
330 340 350
....*....|....*....|....*....|..
gi 499404633 851 LGRMDNEFKIS-GYRIQPGEVEAHLLAQPEVD 881
Cdd:PLN02387 554 IDRKKDIVKLQhGEYVSLGKVEAALSVSPYVD 585
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
753-945 |
1.00e-05 |
|
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: 48.84 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 753 YGPTETTVVATSCDLQTQPADVAQLPIglPLAGVNALVLAAGDRPAAE-GELVLLGPTLAAGY-----IGTEHTAFTLla 826
Cdd:cd17636 143 YGQTEVMGLATFAALGGGAIGGAGRPS--PLVQVRILDEDGREVPDGEvGEIVARGPTVMAGYwnrpeVNARRTRGGW-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 827 vgdrhlpaYRTGD--RvRLEKGHLLYLG---RMdneFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFV 901
Cdd:cd17636 219 --------HHTNDlgR-REPDGSLSFVGpktRM---IKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIV 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499404633 902 ATKEG-EIDARAL----KQRLSSVLPPAMIptdyrAF-HQLPKTGSNKVD 945
Cdd:cd17636 287 VLKPGaSVTEAELiehcRARIASYKKPKSV-----EFaDALPRTAGGADD 331
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
461-619 |
1.03e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 49.56 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 461 LTAIAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPL-- 538
Cdd:PRK08162 21 LSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLnt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 539 ---------------------DPEQPRERQQHIIQIAGLRTIVTQADYQHRLASVFSGAIVLAGHLLSSNAQAVALPTAE 597
Cdd:PRK08162 101 rldaasiafmlrhgeakvlivDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAFLASGDPDFAWTLPAD 180
|
170 180
....*....|....*....|..
gi 499404633 598 srEGQIAYVMFTSGSTGLPKGV 619
Cdd:PRK08162 181 --EWDAIALNYTSGTTGNPKGV 200
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
485-672 |
3.37e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 47.76 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 485 SYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQPRERQQHIIQIAGLRTIVTQAD 564
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 565 Y--------------QHRLASVFSGAIVLAGHLLSSNAQAVALPTAESREGQIayVMFTSGSTGLPKGV-----EIGASA 625
Cdd:PRK13391 106 KldvarallkqcpgvRHRLVLDGDGELEGFVGYAEAVAGLPATPIADESLGTD--MLYSSGTTGRPKGIkrplpEQPPDT 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499404633 626 LDHFTAAARQRYGLRAEDRVLQFAPFNFDASIEEVFATLTSGATLVL 672
Cdd:PRK13391 184 PLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIV 230
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
835-946 |
2.92e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 44.73 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 835 YRTGD-RVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPEVDEACVQGIVYPNGVRRLVAFVATKEGE----ID 909
Cdd:PTZ00237 494 YNSGDlGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQsnqsID 573
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 499404633 910 ARALKQRLSSVlppamIPTDYRAF---------HQLPKTGSNKVDR 946
Cdd:PTZ00237 574 LNKLKNEINNI-----ITQDIESLavlrkiiivNQLPKTKTGKIPR 614
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
801-949 |
9.22e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 43.08 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 801 GELVLLGPTLAAGYIGTEHTAFTLLAVGdrhlpAYRTGD-RVRLEKGHLLYLGRMDNEFKISGYRIQPGEVEAHLLAQPE 879
Cdd:PLN03102 393 GEIVIKGSSIMKGYLKNPKATSEAFKHG-----WLNTGDvGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPK 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 880 VDEACVQGIVYPNGVRRLVAFVATKEGEIDARALKQRLSSV-----------LPPAMIPTDYRAFHQLPKTGSNKVDRKR 948
Cdd:PLN03102 468 VLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPK 547
|
.
gi 499404633 949 L 949
Cdd:PLN03102 548 L 548
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
11-281 |
1.96e-03 |
|
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: 41.79 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 11 LWLGHALNDDKATFNTAECIAFDGKVDIDAMLSAIRQAVMECECLYCQFVEVAGehaeqpeiGFVASQLPVPigvlPIVE 90
Cdd:cd19537 11 WWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDG--------GLRRSYSSSP----PRVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 91 LLpapmtdeeQTIRQWArdEISLPLDLLNGLPCRFALlcgeKRDFLYSCVHHIALDgfGTTM--LFQRIAQIYTALTAGQ 168
Cdd:cd19537 79 RV--------DTLDVWK--EINRPFDLEREDPIRVFI----SPDTLLVVMSHIICD--LTTLqlLLREVSAAYNGKLLPP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 169 SAPVaefgPFSAVLeeeRQRDASgqtAQARDFWLETLNAMPePASFSEKKAPIAARFLRQSCDMPADLWQPLSALCEGNK 248
Cdd:cd19537 143 VRRE----YLDSTA---WSRPAS---PEDLDFWSEYLSGLP-LLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSG 211
|
250 260 270
....*....|....*....|....*....|...
gi 499404633 249 ISWPDLFLAMLATHLKLVSGSDRLTFGMMVMNR 281
Cdd:cd19537 212 ITLHQLALAAVALALQDLSDRTDIVLGAPYLNR 244
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
464-561 |
2.54e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 42.01 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404633 464 IAKQARKNPSHIALAQRDRQYSYQQLLGLSGQAAAALHERGVKPGERIGIMLNRSPETIISLLAVMQCGAVYVPLDPEQP 543
Cdd:PRK07868 453 IAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPDTD 532
|
90
....*....|....*...
gi 499404633 544 RERQqhiIQIAGLRTIVT 561
Cdd:PRK07868 533 LAAA---VRLGGVTEIIT 547
|
|
| |
