|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
33-538 |
4.11e-159 |
|
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: 461.14 E-value: 4.11e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEklhyklsaslldslklvismdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKL 192
Cdd:cd05914 86 SD-----------------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 193 LPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPMFTK 272
Cdd:cd05914 125 VLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 273 TWITQFLYSISFIRRaLHKVAGKKLCQTFGGNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVK 352
Cdd:cd05914 205 KKFKFKLAKKINNRK-IRKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 353 WQSTGPKLPDIEMKILNPNHKKI-GEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMV 431
Cdd:cd05914 284 LGSAGKVIDGVEVRIDSPDPATGeGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 432 GANGENIYPEEIEATINEHDMVLESLVVNTKGKLVAMVHFNYEqieklhtFNEEAEVNMTQRVEEVKKELMEYVNSRVNK 511
Cdd:cd05914 364 LSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPD-------FLDVKALKQRNIIDAIKWEVRDKVNQKVPN 436
|
490 500
....*....|....*....|....*..
gi 1309054211 512 SSKILEILEQSSPFEKTATQKIKRYLY 538
Cdd:cd05914 437 YKKISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
9-535 |
5.97e-131 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 394.08 E-value: 5.97e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFSliNKE-----KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSS 83
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALR--EKEdgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 84 RVVVPILPDFTAFEIVNVIEHSESSVVIVSEKLHYKLSASLLD---SLKLVISMD-----------TLEVIKSAGEQDYT 149
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDelpSLRHIVVLDprglrddprllSLDELLALGREVAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 150 LNEL------PRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILpLSR 223
Cdd:COG1022 170 PAELearraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 224 GAQVVYlhgAPTPSLLLPALTQVRPTIMLSVPLIVEKIYkNKIR-PMFTKTWITQFLY------------------SISF 284
Cdd:COG1022 249 GATVAF---AESPDTLAEDLREVKPTFMLAVPRVWEKVY-AGIQaKAEEAGGLKRKLFrwalavgrryararlagkSPSL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 285 IRRALHKVAGK----KLCQTFGGNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKL 360
Cdd:COG1022 325 LLRLKHALADKlvfsKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 361 PDIEMKILNPnhkkiGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYP 440
Cdd:COG1022 405 PGVEVKIAED-----GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 441 EEIEATINEHDMVLESLVVNTKGK-LVAMVHFNYEQIEKL-----HTFNEEAEVNMTQRV-EEVKKELMEyVNSRVNKSS 513
Cdd:COG1022 480 QPIENALKASPLIEQAVVVGDGRPfLAALIVPDFEALGEWaeengLPYTSYAELAQDPEVrALIQEEVDR-ANAGLSRAE 558
|
570 580
....*....|....*....|....*....
gi 1309054211 514 KI--LEILEQssPF-----EKTATQKIKR 535
Cdd:COG1022 559 QIkrFRLLPK--EFtiengELTPTLKLKR 585
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
35-535 |
1.94e-121 |
|
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: 364.61 E-value: 1.94e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 klhyklsaslldslklvismdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLP 194
Cdd:cd05907 86 -----------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 195 IFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTpslLLPALTQVRPTIMLSVPLIVEKIYkNKIRPMftktw 274
Cdd:cd05907 125 ATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAET---LLDDLSEVRPTVFLAVPRVWEKVY-AAIKVK----- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 275 itqflySISFIRRALHKVAgkklcqtFGGNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQ 354
Cdd:cd05907 196 ------AVPGLKRKLFDLA-------VGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 355 STGPKLPDIEMKIlnpnhKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGAN 434
Cdd:cd05907 263 TVGKPLPGVEVRI-----ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 435 GENIYPEEIEATINEHDMVLESLVV-NTKGKLVAMVHFNYEQIEKLHTFNEEAEVNMT--QRVEEVKKELMEYV---NSR 508
Cdd:cd05907 338 GKNISPEPIENALKASPLISQAVVIgDGRPFLVALIVPDPEALEAWAEEHGIAYTDVAelAANPAVRAEIEAAVeaaNAR 417
|
490 500 510
....*....|....*....|....*....|..
gi 1309054211 509 VNKSSKI--LEILEQ---SSPFEKTATQKIKR 535
Cdd:cd05907 418 LSRYEQIkkFLLLPEpftIENGELTPTLKLKR 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
25-431 |
2.13e-101 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 311.94 E-value: 2.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 25 TAFSLINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEH 104
Cdd:pfam00501 12 TALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 105 SESSVVIVSEKLHYKLSASLLDSLKLVISM-----------DTLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASK 173
Cdd:pfam00501 92 SGAKVLITDDALKLEELLEALGKLEVVKLVlvldrdpvlkeEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 174 GVMLTHRNLV----TQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPT--PSLLLPALTQVR 247
Cdd:pfam00501 172 GVMLTHRNLVanvlSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAldPAALLELIERYK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 248 PTIMLSVPLIVEKIyknkirpmftktwitqflysisfirralhkVAGKKLCQTFGGNLRFFGIGGSKLD-GVVEKFLADA 326
Cdd:pfam00501 252 VTVLYGVPTLLNML------------------------------LEAGAPKRALLSSLRLVLSGGAPLPpELARRFRELF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 327 GFPYGIGYGLTETSPLLAGAIPGKVKWQ---STGPKLPDIEMKILNPNHKK------IGEIVVKGPNVMSGYYKDPVTTA 397
Cdd:pfam00501 302 GGALVNGYGLTETTGVVTTPLPLDEDLRslgSVGRPLPGTEVKIVDDETGEpvppgePGELCVRGPGVMKGYLNDPELTA 381
|
410 420 430
....*....|....*....|....*....|....
gi 1309054211 398 SCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMV 431
Cdd:pfam00501 382 EAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
10-536 |
2.95e-97 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 302.50 E-value: 2.95e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 10 LADIYSRSLVDFSEQTAFSlINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPI 89
Cdd:COG0318 1 LADLLRRAAARHPDRPALV-FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 90 LPDFTAFEIVNVIEHSESSVVIVseklhyklsaslldslklvismdtleviksageqdytlnelprpedlASIIYTSGTS 169
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT-----------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 170 GASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPT 249
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLV-LLPRFDPERVLELIERERVT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 250 IMLSVPlivekiyknkirpmftkTWITQFLYSISFIRRALHkvagkklcqtfggNLRFFGIGGSKLD-GVVEKFLADAGF 328
Cdd:COG0318 192 VLFGVP-----------------TMLARLLRHPEFARYDLS-------------SLRLVVSGGAPLPpELLERFEERFGV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 329 PYGIGYGLTETSPLLAGAI--PGKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFt 401
Cdd:COG0318 242 RIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVDEDGRelppgEVGEIVVRGPNVMKGYWNDPEATAEAF- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 402 EDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV----NTKG-KLVAMVhfnyeQI 476
Cdd:COG0318 321 RDGWLRTGDLGRLDEDGYLYIVGRKKDMII-SGGENVYPAEVEEVLAAHPGVAEAAVVgvpdEKWGeRVVAFV-----VL 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 477 EKLHTFNEEaevnmtqrveevkkELMEYVNSRVNKsSKILEILEQSSPFEKTATQKIKRY 536
Cdd:COG0318 395 RPGAELDAE--------------ELRAFLRERLAR-YKVPRRVEFVDELPRTASGKIDRR 439
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
33-536 |
9.36e-89 |
|
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: 280.78 E-value: 9.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEklhyklsaslldslklvismdtleviksageqdytlnelpRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKL 192
Cdd:cd17640 84 EN----------------------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 193 LPIFREDVFLSILPLSHAYECSLGLILpLSRGAQVVYlhgaPTPSLLLPALTQVRPTIMLSVPLIVEKIYKNkirpmftk 272
Cdd:cd17640 124 VPPQPGDRFLSILPIWHSYERSAEYFI-FACGCSQAY----TSIRTLKDDLKRVKPHYIVSVPRLWESLYSG-------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 273 twITQFLYSISFIRRALHKVAgkklcqTFGGNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVK 352
Cdd:cd17640 191 --IQKQVSKSSPIKQFLFLFF------LSGGIFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 353 WQSTGPKLPDIEMKILNPNHKKI------GEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRK 426
Cdd:cd17640 263 RGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 427 DNMMVGANGENIYPEEIEATINEHDMVLESLVVNTKGK-LVAMVHFNYEQIEK-LHTFNEEAEVNMTQRVEEVK------ 498
Cdd:cd17640 343 KDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKrLGALIVPNFEELEKwAKESGVKLANDRSQLLASKKvlklyk 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1309054211 499 KELMEYVNSR--VNKSSKILEILEQSSPFEK----TATQKIKRY 536
Cdd:cd17640 423 NEIKDEISNRpgFKSFEQIAPFALLEEPFIEngemTQTMKIKRN 466
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
10-459 |
1.18e-83 |
|
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: 267.51 E-value: 1.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 10 LADIYSRSLVDFSEQTAFSLINKeKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPI 89
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGR-KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 90 LPDFTAFEIVNVIEHSESSVVIVSEKLhyklsASLLdslklvismdtleviksAGEQDYTLNELPRPEDLASIIYTSGTS 169
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSF-----TDLL-----------------AAGAPLGERVALTPEDVAVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 170 GASKGVMLTHRNLVTQNYMANKLLPIFRE--DVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVR 247
Cdd:cd05936 138 GVPKGAMLTHRNLVANALQIKAWLEDLLEgdDVVLAALPLFHVFGLTVALLLPLALGATIV-LIPRFRPIGVLKEIRKHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 248 PTIMLSVPLIVEKIYKNkirPMFTKTWITQFLYSISfirralhkvagkklcqtfggnlrffgiGGSKLD-GVVEKFLADA 326
Cdd:cd05936 217 VTIFPGVPTMYIALLNA---PEFKKRDFSSLRLCIS---------------------------GGAPLPvEVAERFEELT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 327 GFPYGIGYGLTETSPLLAG-AIPGKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCF 400
Cdd:cd05936 267 GVPIVEGYGLTETSPVVAVnPLDGPRKPGSIGIPLPGTEVKIVDDDGEelppgEVGELWVRGPQVMKGYWNRPEETAEAF 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309054211 401 TeDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05936 347 V-DGWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREVEEVLYEHPAVAEAAVV 403
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
8-459 |
8.41e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 261.66 E-value: 8.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 8 LSLADIYSRSLVDFSEQTAFSlINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVV 87
Cdd:PRK06187 6 LTIGRILRHGARKHPDKEAVY-FDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 88 PI---LPdftAFEIVNVIEHSESSVVIVSEKL--HYKLSASLLDSLKLVISMDTLEViKSAGEQDYTLNEL--------P 154
Cdd:PRK06187 85 PInirLK---PEEIAYILNDAEDRVVLVDSEFvpLLAAILPQLPTVRTVIVEGDGPA-APLAPEVGEYEELlaaasdtfD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 155 RPE----DLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYEcsLGL-ILPLSRGAQVVY 229
Cdd:PRK06187 161 FPDidenDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHA--WGLpYLALMAGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 230 LHGAPtPSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPmftKTWITqflysisfirralhkvagkklcqtfggNLRFFG 309
Cdd:PRK06187 239 PRRFD-PENLLDLIETERVTFFFAVPTIWQMLLKAPRAY---FVDFS---------------------------SLRLVI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 310 IGGSKL-DGVVEKFLADAGFPYGIGYGLTETSPLLAGA-----IPGKVKWQ-STGPKLPDIEMKILN-------PNHKKI 375
Cdd:PRK06187 288 YGGAALpPALLREFKEKFGIDLVQGYGMTETSPVVSVLppedqLPGQWTKRrSAGRPLPGVEARIVDddgdelpPDGGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 376 GEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMM-VGanGENIYPEEIEATINEHDMVL 454
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYITDRIKDVIiSG--GENIYPRELEDALYGHPAVA 444
|
....*
gi 1309054211 455 ESLVV 459
Cdd:PRK06187 445 EVAVI 449
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
35-535 |
1.21e-75 |
|
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: 249.05 E-value: 1.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVK--KGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHyklsaslldslklVISMDTLEVIksaGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQ----NYM 188
Cdd:cd05927 86 DAGVK-------------VYSLEEFEKL---GKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNvagvFKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 189 ANKLLPIFREDVFLSILPLSHAYEcSLGLILPLSRGAQVVYLHGAPTpsLLLPALTQVRPTIMLSVPLIVEKIYKNKIRP 268
Cdd:cd05927 150 LEILNKINPTDVYISYLPLAHIFE-RVVEALFLYHGAKIGFYSGDIR--LLLDDIKALKPTVFPGVPRVLNRIYDKIFNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 269 MFTKTWITQFLYSISFIRRALH-------------KVAGKKLCQTFGGNLRFFGIGGSKLDGVVEKFL-ADAGFPYGIGY 334
Cdd:cd05927 227 VQAKGPLKRKLFNFALNYKLAElrsgvvraspfwdKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLrVALGCPVLEGY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 335 GLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKI-----LNPNHKKI---GEIVVKGPNVMSGYYKDPVTTASCFTEDGWF 406
Cdd:cd05927 307 GQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLvdvpeMNYDAKDPnprGEVCIRGPNVFSGYYKDPEKTAEALDEDGWL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 407 RTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDMVLESLVV--NTKGKLVAMVHFNYEQIEKLHTFN- 483
Cdd:cd05927 387 HTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYgdSLKSFLVAIVVPDPDVLKEWAASKg 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309054211 484 -EEAEVNMTQRVEEVKKELMEYVNsRVNKSSKiLEILEQ-------SSPFEK-----TATQKIKR 535
Cdd:cd05927 467 gGTGSFEELCKNPEVKKAILEDLV-RLGKENG-LKGFEQvkaihlePEPFSVengllTPTFKLKR 529
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
31-459 |
1.32e-74 |
|
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: 244.43 E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 31 NKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVV 110
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 IVSEKLHYKLSASL--LDSLKLVISMDT-----------LEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVML 177
Cdd:cd05911 87 FTDPDGLEKVKEAAkeLGPKDKIIVLDDkpdgvlsiedlLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 178 THRNLVTQNYMANKLLP--IFREDVFLSILPLSHAYECSLGLILPLsRGAqVVYLHGAPTPSLLLPALTQVRPTIMLSVP 255
Cdd:cd05911 167 SHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLL-NGA-TVIIMPKFDSELFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 256 LIVEKIYKNkirPMFTKtwitqflYSISfirralhkvagkklcqtfggNLRFFGIGGSKLDG-VVEKFLADAGFPY-GIG 333
Cdd:cd05911 245 PIAAALAKS---PLLDK-------YDLS--------------------SLRVILSGGAPLSKeLQELLAKRFPNATiKQG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 334 YGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKKI------GEIVVKGPNVMSGYYKDPVTTASCFTEDGWFR 407
Cdd:cd05911 295 YGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSlgpnepGEICVRGPQVMKGYYNNPEATKETFDEDGWLH 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1309054211 408 TKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05911 375 TGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAVLLEHPGVADAAVI 425
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
33-459 |
7.14e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 243.27 E-value: 7.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK07656 29 QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKL--HYKLSASLLDSLKLVIS------------MDTLEVIKSAGEQDYTLNELpRPEDLASIIYTSGTSGASKGVMLT 178
Cdd:PRK07656 109 LGLFlgVDYSATTRLPALEHVVIceteeddphtekMKTFTDFLAAGDPAERAPEV-DPDDVADILFTSGTTGRPKGAMLT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 179 HRNLvTQNYMA-NKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLhgaPT--PSLLLPALTQVRPTIMLSVP 255
Cdd:PRK07656 188 HRQL-LSNAADwAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPL---PVfdPDEVFRLIETERITVLPGPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 256 liveKIYknkirpmftktwitQFLYsiSFIRRALHKVAgkklcqtfggNLRFFGIGGSKLDGV-VEKFlaDAGFPYGI-- 332
Cdd:PRK07656 264 ----TMY--------------NSLL--QHPDRSAEDLS----------SLRLAVTGAASMPVAlLERF--ESELGVDIvl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 333 -GYGLTETSPLL--------AGAIPGkvkwqSTGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTAS 398
Cdd:PRK07656 312 tGYGLSEASGVTtfnrldddRKTVAG-----TIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYYDDPEATAA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309054211 399 CFTEDGWFRTKDLGYIDKNGNLYIKGRKDNM-MVGanGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07656 387 AIDADGWLHTGDLGRLDEEGYLYIVDRKKDMfIVG--GFNVYPAEVEEVLYEHPAVAEAAVI 446
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
158-534 |
3.50e-72 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 233.33 E-value: 3.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 158 DLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYEcSLGLILPLSRGAQVVyLHGAPTPS 237
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVV-LLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 238 LLLPALTQVRPTIMLSVPLIVEKIYKNkirpmftktwitqflysISFIRRALHkvagkklcqtfggNLRFFGIGGSKLDG 317
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKA-----------------PESAGYDLS-------------SLRALVSGGAPLPP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 318 -VVEKFLADAGFPYGIGYGLTETSPLLAGAIP--GKVKWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGY 389
Cdd:cd04433 129 eLLERFEEAPGIKLVNGYGLTETGGTVATGPPddDARKPGSVGRPVPGVEVRIVDPDGGElppgeIGELVVRGPSVMKGY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 390 YKDPVTTAsCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVVNTKGKlvamv 469
Cdd:cd04433 209 WNNPEATA-AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP----- 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309054211 470 hfnyEQIEKLHTFneeaeVNMTQRVEEVKKELMEYVNSRVNKsSKILEILEQSSPFEKTATQKIK 534
Cdd:cd04433 282 ----EWGERVVAV-----VVLRPGADLDAEELRAHVRERLAP-YKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
35-459 |
1.00e-71 |
|
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: 235.58 E-value: 1.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIvse 114
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 klhyklsaslldslklvismdtleviksageqdytlnelprpEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLP 194
Cdd:cd17631 98 ------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 195 IFREDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKnkiRPMFTKTW 274
Cdd:cd17631 136 LGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVV-ILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQ---HPRFATTD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 275 ITqflysisfirralhkvagkklcqtfggNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKV--K 352
Cdd:cd17631 212 LS---------------------------SLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHrrK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 353 WQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKD 427
Cdd:cd17631 265 LGSAGRPVFFVEVRIVDPDGREvppgeVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKK 343
|
410 420 430
....*....|....*....|....*....|..
gi 1309054211 428 NMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17631 344 DMII-SGGENVYPAEVEDVLYEHPAVAEVAVI 374
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
35-535 |
1.69e-62 |
|
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: 212.94 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHY-------KLSASLLD------SLKLVISMDTLEVIKSAGEQDYTLnELPRPEDLASIIYTSGTSGASKGVMLTHRN 181
Cdd:cd05926 95 GELGpasraasKLGLAILElaldvgVLIRAPSAESLSNLLADKKNAKSE-GVPLPDDLALILHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 182 LVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGApTPSLLLPALTQVRPT----------IM 251
Cdd:cd05926 174 LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRF-SASTFWPDVRDYNATwytavptihqIL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 252 LSVPLIVEKIYKNKIRpmftktwitqflysisFIRR---ALHKVAGKKLCQTFGGnlrffgiggskldGVVEkfladagf 328
Cdd:cd05926 253 LNRPEPNPESPPPKLR----------------FIRScsaSLPPAVLEALEATFGA-------------PVLE-------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 329 pygiGYGLTETSPLLAGA--IPGKVKWQSTGPklPD-IEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCF 400
Cdd:cd05926 296 ----AYGMTEAAHQMTSNplPPGPRKPGSVGK--PVgVEVRILDEDGEilppgVVGEICLRGPNVTRGYLNNPEANAEAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 401 TEDGWFRTKDLGYIDKNGNLYIKGRKDNMmVGANGENIYPEEIEATINEHDMVLESLVVntkgklvAMVHFNY-EQIEKL 479
Cdd:cd05926 370 FKDGWFRTGDLGYLDADGYLFLTGRIKEL-INRGGEKISPLEVDGVLLSHPAVLEAVAF-------GVPDEKYgEEVAAA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 480 HTFNEEAEVNMTQRVEEVKKELMEYvnsRVNKssKILEILEqsspFEKTATQKIKR 535
Cdd:cd05926 442 VVLREGASVTEEELRAFCRKHLAAF---KVPK--KVYFVDE----LPKTATGKIQR 488
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
33-535 |
4.37e-61 |
|
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: 209.25 E-value: 4.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSASLL-DSLKLVISMdtlevIKSAGEQDYTLNEL------------PRPEDLASIIYTSGTSGASKGVMLTH 179
Cdd:cd05932 85 GKLDDWKAMAPGVpEGLISISLP-----PPSAANCQYQWDDLiaqhppleerptRFPEQLATLIYTSGTTGQPKGVMLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 180 RNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTpslLLPALTQVRPTIMLSVPLIVE 259
Cdd:cd05932 160 GSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDT---FVEDVQRARPTLFFSVPRLWT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 260 KIYKNKIRPMFTKTwiTQFLYSI----SFIRRALHKVAGKKLCqtfggnlRFFGIGGSKLDGVVEKFLADAGFPYGIGYG 335
Cdd:cd05932 237 KFQQGVQDKIPQQK--LNLLLKIpvvnSLVKRKVLKGLGLDQC-------RLAGCGSAPVPPALLEWYRSLGLNILEAYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 336 LTETSPLLAGAIPGKVKWQSTGPKLPDIEMKIlnpnhKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYID 415
Cdd:cd05932 308 MTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI-----SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 416 KNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDMVlESLVVNTKG--KLVAMVHFNYEQieklhtfNEEAEVNMTQR 493
Cdd:cd05932 383 ADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRV-EMVCVIGSGlpAPLALVVLSEEA-------RLRADAFARAE 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1309054211 494 VEEVKKELMEYVNSRVNKSSKILEILEQSSPFE-----KTATQKIKR 535
Cdd:cd05932 455 LEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSidngiLTPTLKIKR 501
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
35-459 |
9.95e-61 |
|
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: 208.24 E-value: 9.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLSASLLdslkLVISMDTLEVI---KSAGEQDYTLNELPRPE----DLASIIYTSGTSGASKGVMLTHRNLVT--Q 185
Cdd:cd05904 113 ELAEKLASLAL----PVVLLDSAEFDslsFSDLLFEADEAEPPVVVikqdDVAALLYSSGTTGRSKGVMLTHRNLIAmvA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 186 NYMANKLLPIFREDVFLSILPLSHAYecSLGLIL--PLSRGAQVVYLHGAPTPSlLLPALTQVRPTIMLSVPLIVEKIYK 263
Cdd:cd05904 189 QFVAGEGSNSDSEDVFLCVLPMFHIY--GLSSFAlgLLRLGATVVVMPRFDLEE-LLAAIERYKVTHLPVVPPIVLALVK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 264 NKIrpmftktwitqflySISFIRRALHKVagkklcqtfggnlrffGIGGSKLD-GVVEKFLADagFP---YGIGYGLTET 339
Cdd:cd05904 266 SPI--------------VDKYDLSSLRQI----------------MSGAAPLGkELIEAFRAK--FPnvdLGQGYGMTES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 340 SPLLA---GAIPGKVKWQSTGPKLPDIEMKILNPN------HKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKD 410
Cdd:cd05904 314 TGVVAmcfAPEKDRAKYGSVGRLVPNVEAKIVDPEtgeslpPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1309054211 411 LGYIDKNGNLYIKGR-KDnmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05904 394 LCYIDEDGYLFIVDRlKE--LIKYKGFQVAPAELEALLLSHPEILDAAVI 441
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
36-459 |
3.08e-60 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 205.38 E-value: 3.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSessvvivseK 115
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDL---------D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 116 LHYKLSASLLDslKLVISMDTLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPI 195
Cdd:TIGR01923 72 VQLLLTDSLLE--EKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 196 FREDVFLSILPLSHAyeCSLGLILPLSRGAQVVYLHGAptpslllpaltqvrptimlsvplivekiyKNKIRPMFTKTWI 275
Cdd:TIGR01923 150 TEDDNWLLSLPLYHI--SGLSILFRWLIEGATLRIVDK-----------------------------FNQLLEMIANERV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 276 TQflysISFIRRALHKVAGKKLCQTfggNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTET-SPLLAGAIPGKVKWQ 354
Cdd:TIGR01923 199 TH----ISLVPTQLNRLLDEGGHNE---NLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETcSQVTTATPEMLHARP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 355 STGPKLPDIEMKILNPNHKKIGEIVVKGPNVMSGYYKD-PVTTAscFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgA 433
Cdd:TIGR01923 272 DVGRPLAGREIKIKVDNKEGHGEIMVKGANLMKGYLYQgELTPA--FEQQGWFNTGDIGELDGEGFLYVLGRRDDLII-S 348
|
410 420
....*....|....*....|....*.
gi 1309054211 434 NGENIYPEEIEATINEHDMVLESLVV 459
Cdd:TIGR01923 349 GGENIYPEEIETVLYQHPGIQEAVVV 374
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
35-535 |
1.27e-59 |
|
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: 205.53 E-value: 1.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVpilpdfTAFE------IVNVIEHSESS 108
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIV------TVYAtlgedaLIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 109 VVIVSEKlhyklsaslldslklvismdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYM 188
Cdd:cd17639 80 AIFTDGK----------------------------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 189 ANKLLPIF--REDVFLSILPLSHAYECSLGLILpLSRGAQVVYlhgaPTPSLLLPA--------LTQVRPTIMLSVPLIV 258
Cdd:cd17639 120 LGDRVPELlgPDDRYLAYLPLAHIFELAAENVC-LYRGGTIGY----GSPRTLTDKskrgckgdLTEFKPTLMVGVPAIW 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 259 EKIYKN---KIRPMFTktwITQFLYSISFIRR-----------ALHKVAGKKLCQTFGGNLRFFGIGGSKLDGVVEKFLA 324
Cdd:cd17639 195 DTIRKGvlaKLNPMGG---LKRTLFWTAYQSKlkalkegpgtpLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFLN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 325 DAGFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILN-PNHKKI-------GEIVVKGPNVMSGYYKDPVTT 396
Cdd:cd17639 272 IVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDwEEGGYStdkppprGEILIRGPNVFKGYYKNPEKT 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 397 ASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDMVLE--SLVVNTKGKLVAMVHFNYE 474
Cdd:cd17639 352 KEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNicVYADPDKSYPVAIVVPNEK 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309054211 475 QIEKLHTFNE------EAEVNMTQRVEEVKKELMEYvnSRVNKSSKIlEIL-------EQSSPfEK---TATQKIKR 535
Cdd:cd17639 432 HLTKLAEKHGvinsewEELCEDKKLQKAVLKSLAET--ARAAGLEKF-EIPqgvvlldEEWTP-ENglvTAAQKLKR 504
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
9-459 |
1.25e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 201.77 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFSLINKEKlTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVP 88
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATT-TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 89 ILPDFTAFEIVNVIEHSESSVVIVSEK-------------LHYKLSASLLDS--------LKL----------------- 130
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIVWDKvaptverlrrttpLETIVSVNMIAAmpllqrlaLRLpipalrkaraaltgpap 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 131 -VISMDTLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFRED--VFLSILPL 207
Cdd:PRK05605 192 gTVPWETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGpeRVLAALPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 208 SHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKN-KIRPMftktwitqflySISFIR 286
Cdd:PRK05605 272 FHAYGLTLCLTLAVSIGGELV-LLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaEERGV-----------DLSGVR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 287 RALHkvagkklcqtfggnlrffgiGGSKLD-GVVEKFLADAGFPYGIGYGLTETSPLLAG------AIPGKVkwqstGPK 359
Cdd:PRK05605 340 NAFS--------------------GAMALPvSTVELWEKLTGGLLVEGYGLTETSPIIVGnpmsddRRPGYV-----GVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 360 LPDIEMKILNPNHK-------KIGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVg 432
Cdd:PRK05605 395 FPDTEVRIVDPEDPdetmpdgEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELII- 472
|
490 500
....*....|....*....|....*..
gi 1309054211 433 ANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK05605 473 TGGFNVYPAEVEEVLREHPGVEDAAVV 499
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
33-459 |
1.80e-55 |
|
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: 192.50 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILN-KHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVI 111
Cdd:cd05941 10 DSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 vseklhyklsaslldslklvismdtleviksageqdytlnelprpeDLASIIYTSGTSGASKGVMLTHRNLVTQnymANK 191
Cdd:cd05941 90 ----------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAAN---VRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 192 LLPIFR---EDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIyknkirp 268
Cdd:cd05941 121 LVDAWRwteDDVLLHVLPLHHVHGLVNALLCPLFAGASVE-FLPKFDPKEVAISRLMPSITVFMGVPTIYTRL------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 269 mfTKTWITQFLYSISFIRRALHKvagkklcqtfggnLRFFGIGGSKLD-GVVEKFLADAGFPYGIGYGLTETS-----PL 342
Cdd:cd05941 193 --LQYYEAHFTDPQFARAAAAER-------------LRLMVSGSAALPvPTLEEWEAITGHTLLERYGMTEIGmalsnPL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 343 LAGAIPGKVkwqstGPKLPDIEMKILNPN------HKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDK 416
Cdd:cd05941 258 DGERRPGTV-----GMPLPGVQARIVDEEtgeplpRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDE 332
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1309054211 417 NGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05941 333 DGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVI 375
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
35-469 |
4.87e-55 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 196.09 E-value: 4.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPIL----PDFTAFeIVNvieHSESSVV 110
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYdtlgPDAVKF-IVN---HAEVAAI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 IVS-EKLHYKLSA-SLLDSLKLV------------------ISMDTLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSG 170
Cdd:PLN02736 155 FCVpQTLNTLLSClSEIPSVRLIvvvggadeplpslpsgtgVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 171 ASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYEcslglilplsRGAQVVYLHGAPTPSL-------LLPAL 243
Cdd:PLN02736 235 TPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYE----------RVNQIVMLHYGVAVGFyqgdnlkLMDDL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 244 TQVRPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFLYSISFI--RRALHKvaGK------------KLCQTFGGNLRFFG 309
Cdd:PLN02736 305 AALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNakKQALEN--GKnpspmwdrlvfnKIKAKLGGRVRFMS 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 310 IGGSKLDGVVEKFLADA-GFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILN-----------PNHKkiGE 377
Cdd:PLN02736 383 SGASPLSPDVMEFLRICfGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemnytsedqPYPR--GE 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 378 IVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDMVLESL 457
Cdd:PLN02736 461 ICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCF 540
|
490
....*....|....
gi 1309054211 458 VV--NTKGKLVAMV 469
Cdd:PLN02736 541 VYgdSLNSSLVAVV 554
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
36-466 |
1.24e-54 |
|
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: 189.81 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVsek 115
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 116 lhyklsaslldslklvismdtleviksageqdytlnelprpeDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPI 195
Cdd:cd05934 82 ------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 196 FREDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPmftktwi 275
Cdd:cd05934 120 GEDDVYLTVLPLFHINAQAVSVLAALSVGATLV-LLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSP------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 276 tqflysisfiRRALHKVagkKLCqtfggnlrfFGIGGSKLDgvVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQS 355
Cdd:cd05934 192 ----------DDRAHRL---RAA---------YGAPNPPEL--HEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGS 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 356 TGPKLPDIEMKILNPNHKK-----IGEIVVK---GPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKD 427
Cdd:cd05934 248 IGRPAPGYEVRIVDDDGQElpagePGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKK 326
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1309054211 428 NMM-VGanGENIYPEEIEATINEHDMVLESLVVNTKGKLV 466
Cdd:cd05934 327 DMIrRR--GENISSAEVERAILRHPAVREAAVVAVPDEVG 364
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
35-461 |
2.42e-53 |
|
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: 186.53 E-value: 2.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLhyklsaslldslklvismdtleviksageqdytlnelprpEDLASIIYTSGTSGASKGVMLTHRNLvtqnyMANKLLP 194
Cdd:cd05935 82 EL----------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-----AANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 195 IF-----REDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPlivekiyknkirpm 269
Cdd:cd05935 117 AVwtgltPSDVILACLPLFHVTGFVGSLNTAVYVGGTYV-LMARWDRETALELIEKYKVTFWTNIP-------------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 ftkTWITQFLYSISFIRRALHKvagkklcqtfggnLRFFGIGGSKL-DGVVEKFLADAGFPYGIGYGLTETSPLLAGAIP 348
Cdd:cd05935 182 ---TMLVDLLATPEFKTRDLSS-------------LKVLTGGGAPMpPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 349 GKVKWQSTGPKLPDIEMKI--------LNPNhkKIGEIVVKGPNVMSGYYKDPVTTASCFTEDG---WFRTKDLGYIDKN 417
Cdd:cd05935 246 LRPKLQCLGIP*FGVDARVidietgreLPPN--EVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEE 323
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1309054211 418 GNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNT 461
Cdd:cd05935 324 GYFFFVDRVKR-MINVSGFKVWPAEVEAKLYKHPAI*EVCVISV 366
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
33-478 |
1.86e-52 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 187.63 E-value: 1.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SE-----KLhYKLsASLLDSLKLVISMD-------------TLEVIKSAGEQ---------DYTLNELpRPEDLASIIYT 165
Cdd:cd17641 90 EDeeqvdKL-LEI-ADRIPSVRYVIYCDprgmrkyddprliSFEDVVALGRAldrrdpglyEREVAAG-KGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 166 SGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVvylHGAPTPSLLLPALTQ 245
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV---NFPEEPETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 246 VRPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFLYSI--SFIRRAL--------------------HKVAGKKLCQTFG- 302
Cdd:cd17641 244 IGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELgmKLGLRALdrgkrgrpvslwlrlaswlaDALLFRPLRDRLGf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 303 GNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTEtsplLAGAI----PGKVKWQSTGPKLPDIEMKILNpnhkkIGEI 378
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTE----LAGAYtvhrDGDVDPDTVGVPFPGTEVRIDE-----VGEI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 379 VVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDMVLESLV 458
Cdd:cd17641 395 LVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVV 474
|
490 500
....*....|....*....|.
gi 1309054211 459 V-NTKGKLVAMVHFNYEQIEK 478
Cdd:cd17641 475 LgAGRPYLTAFICIDYAIVGK 495
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
33-456 |
1.06e-51 |
|
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: 184.79 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVP--ILPDFTAFE-----IVNVIEHS 105
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPltVPPTYDEPNarlrkLRHIWQLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 106 ESSVVIVSEKLHYKLSASLLDSLKLVISMDTLEvIKSAGEQDYTLNElPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQ 185
Cdd:cd05906 118 GSPVVLTDAELVAEFAGLETLSGLPGIRVLSIE-ELLDTAADHDLPQ-SRPDDLALLMLTSGSTGFPKAVPLTHRNILAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 186 NYMANKLLPIFREDVFLSILPLSHA---YECSlglILPLSRGAQVVYlhgAPTPSLLlpaltqVRPTIMLsvplivEKIY 262
Cdd:cd05906 196 SAGKIQHNGLTPQDVFLNWVPLDHVgglVELH---LRAVYLGCQQVH---VPTEEIL------ADPLRWL------DLID 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 263 KNKIrpmfTKTWITQFLYSIsfIRRALHKVAGKK--LcqtfgGNLRFFGIGGSKLDGVVEKFLADAGFPYGI-------G 333
Cdd:cd05906 258 RYRV----TITWAPNFAFAL--LNDLLEEIEDGTwdL-----SSLRYLVNAGEAVVAKTIRRLLRLLEPYGLppdairpA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 334 YGLTETS-------PLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFT 401
Cdd:cd05906 327 FGMTETCsgviysrSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQllpegEVGRLQVRGPVVTKGYYNNPEANAEAFT 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 402 EDGWFRTKDLGYIDkNGNLYIKGR-KDNMMVgaNGENIYPEEIEATINEHDMVLES 456
Cdd:cd05906 407 EDGWFRTGDLGFLD-NGNLTITGRtKDTIIV--NGVNYYSHEIEAAVEEVPGVEPS 459
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
33-535 |
6.07e-51 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 183.71 E-value: 6.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 -SEKLHYKLSA--SLLDSLKLVI--------------SMDTLEVI--KSAGEQDYTLNELPRPEDLASIIYTSGTSGASK 173
Cdd:cd05933 87 eNQKQLQKILQiqDKLPHLKAIIqykeplkekepnlySWDEFMELgrSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 174 GVMLTHRNLVTQNYMANKLL----PIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVY-----LHGAptpslLLPALT 244
Cdd:cd05933 167 GVMLSHDNITWTAKAASQHMdlrpATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFaqpdaLKGT-----LVKTLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 245 QVRPTIMLSVPLIVEKIY-KNKI---------RPMFT----------KTWITQFLYSISFIRRALHKVAgKKLCQTFG-G 303
Cdd:cd05933 242 EVRPTAFMGVPRVWEKIQeKMKAvgaksgtlkRKIASwakgvgletnLKLMGGESPSPLFYRLAKKLVF-KKVRKALGlD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 304 NLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKKIGEIVVKGP 383
Cdd:cd05933 321 RCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 384 NVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEH-DMVLESLVVNTK 462
Cdd:cd05933 401 HVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNAMLIGDK 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 463 GKLVAMvhfnyeqiekLHTFNEEAEVNMTQRVEEVKKELMEYVNSRVNKSSKILEILEQSSP-FEKTATQKIKR 535
Cdd:cd05933 481 RKFLSM----------LLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPkVYEAIEEGIKR 544
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
36-459 |
1.78e-50 |
|
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: 180.90 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEK 115
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 116 LHYKLSASL--LDSLKLVISMDTlevikSAGEQDYTLNELPRPEDL------------------ASIIYTSGTSGASKGV 175
Cdd:cd12119 107 FLPLLEAIAprLPTVEHVVVMTD-----DAAMPEPAGVGVLAYEELlaaespeydwpdfdentaAAICYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 176 MLTHRNLVTQNYMANK--LLPIFREDVFLSILPLSHAYECSLGLILPLSrGAQVVYLHGAPTPSLLLPALTQVRPTIMLS 253
Cdd:cd12119 182 VYSHRSLVLHAMAALLtdGLGLSESDVVLPVVPMFHVNAWGLPYAAAMV-GAKLVLPGPYLDPASLAELIEREGVTFAAG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 254 VPLIvekiyknkirpmftktWItQFLYSISFIRRALHKvagkklcqtfggnLRFFGIGGSKL-DGVVEKFlADAGFPYGI 332
Cdd:cd12119 261 VPTV----------------WQ-GLLDHLEANGRDLSS-------------LRRVVIGGSAVpRSLIEAF-EERGVRVIH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 333 GYGLTETSPLLAGAIPGKV-----------KWQSTGPKLPDIEMKILNPN-------HKKIGEIVVKGPNVMSGYYKDPV 394
Cdd:cd12119 310 AWGMTETSPLGTVARPPSEhsnlsedeqlaLRAKQGRPVPGVELRIVDDDgrelpwdGKAVGELQVRGPWVTKSYYKNDE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 395 TTAScFTEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd12119 390 ESEA-LTEDGWLRTGDVATIDEDGYLTITDRsKDVIKSG--GEWISSVELENAIMAHPAVAEAAVI 452
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
24-461 |
3.07e-49 |
|
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: 175.73 E-value: 3.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 24 QTAFsLINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIE 103
Cdd:cd05919 1 KTAF-YAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 104 HSESSVVIVSEklhyklsaslldslklvismdtleviksageqdytlnelprpEDLASIIYTSGTSGASKGVMLTHRNLV 183
Cdd:cd05919 80 DCEARLVVTSA------------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 184 -TQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLLLPALTQVRPTIMLSVPliveKIY 262
Cdd:cd05919 118 lFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVP----TFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 263 KNKIRpmftktwitqflySISFIRRALHkvagkklcqtfggNLRFFGIGGSKLD-GVVEKFLADAGFPYGIGYGLTETSP 341
Cdd:cd05919 194 ANLLD-------------SCAGSPDALR-------------SLRLCVSAGEALPrGLGERWMEHFGGPILDGIGATEVGH 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 342 LLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDK 416
Cdd:cd05919 248 IFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIppgeeGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDA 326
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1309054211 417 NGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVVNT 461
Cdd:cd05919 327 DGWYTHAGRADDMLK-VGGQWVSPVEVESLIIQHPAVAEAAVVAV 370
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
36-535 |
3.09e-49 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 180.40 E-value: 3.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEK 115
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 116 LHYKL------SASLLDSLKLVISMDTLEVIKSA--GEQDYTLNEL-------------PRPEDLASIIYTSGTSGASKG 174
Cdd:PLN02430 158 KIKELlepdckSAKRLKAIVSFTSVTEEESDKASqiGVKTYSWIDFlhmgkenpsetnpPKPLDICTIMYTSGTSGDPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 175 VMLTHRNLVTQNYMANKLLPIFR-----EDVFLSILPLSHayecslglILP-------LSRGAQVVYLHGapTPSLLLPA 242
Cdd:PLN02430 238 VVLTHEAVATFVRGVDLFMEQFEdkmthDDVYLSFLPLAH--------ILDrmieeyfFRKGASVGYYHG--DLNALRDD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 243 LTQVRPTIMLSVPLIVEKIYK------NKIRPMFTKTWITQFLYSISFIRRAL-HK--------VAGKKLCQTFGGNLRF 307
Cdd:PLN02430 308 LMELKPTLLAGVPRVFERIHEgiqkalQELNPRRRLIFNALYKYKLAWMNRGYsHKkaspmadfLAFRKVKAKLGGRLRL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 308 FGIGGSKLDGVVEKFLADAGFPYGI-GYGLTETSPLLAGAIP------GKVKWQSTGPKL-----PDIEMKILNPNHKki 375
Cdd:PLN02430 388 LISGGAPLSTEIEEFLRVTSCAFVVqGYGLTETLGPTTLGFPdemcmlGTVGAPAVYNELrleevPEMGYDPLGEPPR-- 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 376 GEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDMVLE 455
Cdd:PLN02430 466 GEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVED 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 456 SLVV--NTKGKLVAMVHFNYEQIEKL-----HTFNEEAEVNMTQRVEEVKKELMEYVN-SRVNKSSKILEILEQSSPFEK 527
Cdd:PLN02430 545 IWVYgdSFKSMLVAVVVPNEENTNKWakdngFTGSFEELCSLPELKEHILSELKSTAEkNKLRGFEYIKGVILETKPFDV 624
|
570
....*....|...
gi 1309054211 528 -----TATQKIKR 535
Cdd:PLN02430 625 erdlvTATLKKRR 637
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
5-459 |
3.15e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 178.43 E-value: 3.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 5 VLGLSLADIYSRSLVDFSEQTAFSLINKE-KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSS 83
Cdd:PRK12583 15 LLTQTIGDAFDATVARFPDREALVVRHQAlRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 84 RVVVPILPDFTAFEIVNVIEHSESSVVI--------------------VSEKLHYKLSASLLDSLKLVISMD-------- 135
Cdd:PRK12583 95 AILVNINPAYRASELEYALGQSGVRWVIcadafktsdyhamlqellpgLAEGQPGALACERLPELRGVVSLApapppgfl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 136 TLEVIKSAGE--QDYTLNELP---RPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHA 210
Cdd:PRK12583 175 AWHELQARGEtvSREALAERQaslDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 211 YECSLGLILPLSRGAQVVYLHGAPTPSLLLPALTQVRPTIMLSVPlivekiyknkirpmftktwiTQFLYSISFIRRALH 290
Cdd:PRK12583 255 FGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVP--------------------TMFIAELDHPQRGNF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 291 KVAgkklcqtfggNLRFfGI--GGSKLDGVVEKFLADAGFP-YGIGYGLTETSPLL---AGAIPGKVKWQSTGPKLPDIE 364
Cdd:PRK12583 315 DLS----------SLRT-GImaGAPCPIEVMRRVMDEMHMAeVQIAYGMTETSPVSlqtTAADDLERRVETVGRTQPHLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 365 MKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIY 439
Cdd:PRK12583 384 VKVVDPDGAtvprgEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMII-RGGENIY 462
|
490 500
....*....|....*....|
gi 1309054211 440 PEEIEATINEHDMVLESLVV 459
Cdd:PRK12583 463 PREIEEFLFTHPAVADVQVF 482
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
34-459 |
2.38e-48 |
|
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: 172.53 E-value: 2.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVvivs 113
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 114 eklhyklsaslldslklvismdtleviksageqdytlnelprpEDLASIIYTSGTSGASKGVMLTHRNlVTQNYMANKL- 192
Cdd:cd05912 77 -------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGN-HWWSAIGSALn 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 193 LPIFREDVFLSILPLSHAYECSL---GLILPLSrgaqvVYLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKnkirpm 269
Cdd:cd05912 113 LGLTEDDNWLCALPLFHISGLSIlmrSVIYGMT-----VYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE------ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 ftktwitqflysisfirralhkvagkKLCQTFGGNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIP- 348
Cdd:cd05912 182 --------------------------ILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPe 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 349 -GKVKWQSTGPKLPDIEMKILNPNHKK--IGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGR 425
Cdd:cd05912 236 dALNKIGSAGKPLFPVELKIEDDGQPPyeVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDR 314
|
410 420 430
....*....|....*....|....*....|....
gi 1309054211 426 KDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05912 315 RSDLII-SGGENIYPAEIEEVLLSHPAIKEAGVV 347
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
32-537 |
3.12e-48 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 175.69 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 32 KEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITtssR---VVVPILPDFTAFEIVNVIEHSESS 108
Cdd:COG0365 37 ERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACA---RigaVHSPVFPGFGAEALADRIEDAEAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 109 VVIVSEKLHY---------KLSASL--LDSLKLVISMD-TLEVIKSAGEQDYtlNEL-------PRPEDLAS-----IIY 164
Cdd:COG0365 114 VLITADGGLRggkvidlkeKVDEALeeLPSLEHVIVVGrTGADVPMEGDLDW--DELlaaasaeFEPEPTDAddplfILY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 165 TSGTSGASKGVMLTHRNLVTQNYMANKLlpIF---REDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPT---PSL 238
Cdd:COG0365 192 TSGTTGKPKGVVHTHGGYLVHAATTAKY--VLdlkPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDfpdPGR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 239 LLPALTQVRPTIMLSVPlivekiyknkirpmftkTWItqflysisfirRALHKVAGKKLCQTFGGNLRFFGIGGSKLDG- 317
Cdd:COG0365 270 LWELIEKYGVTVFFTAP-----------------TAI-----------RALMKAGDEPLKKYDLSSLRLLGSAGEPLNPe 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 318 VVEKFLADAGFPYGIGYGLTETSPLLAGAIPG-KVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKG--PNVMSGY 389
Cdd:COG0365 322 VWEWWYEAVGVPIVDGWGQTETGGIFISNLPGlPVKPGSMGKPVPGYDVAVVDEDGNpvppgEEGELVIKGpwPGMFRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 390 YKDPVTTASCF--TEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV----NTKG 463
Cdd:COG0365 402 WNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVIN-VSGHRIGTAEIESALVSHPAVAEAAVVgvpdEIRG 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309054211 464 -KLVAMVhfnyeqieklhTFNEEAEVNmtqrvEEVKKELMEYVNSRVnksSKIL---EILEQSS-PfeKTATQKIKRYL 537
Cdd:COG0365 481 qVVKAFV-----------VLKPGVEPS-----DELAKELQAHVREEL---GPYAyprEIEFVDElP--KTRSGKIMRRL 538
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
21-535 |
3.94e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 175.61 E-value: 3.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 21 FSEQTAFSLINKEkLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVN 100
Cdd:PRK06710 37 YPEKKALHFLGKD-ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 101 VIEHSESSVVIV-------------SEKLHYKLSASLLDSL----------------KLVISMDTLEVI----KSAGEQD 147
Cdd:PRK06710 116 QLHDSGAKVILCldlvfprvtnvqsATKIEHVIVTRIADFLpfpknllypfvqkkqsNLVVKVSESETIhlwnSVEKEVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 148 YTLNELPRPE-DLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLL--PIFREDVFLSILPLSHAYECSLGLILPLSRG 224
Cdd:PRK06710 196 TGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLynCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 225 AQVVYLHGAPTpSLLLPALTQVRPTIMLSVPLIVEKIYKNkirPMFTKtwitqflYSISFIRRALHKVAGKKLcqtfggn 304
Cdd:PRK06710 276 YKMVLIPKFDM-KMVFEAIKKHKVTLFPGAPTIYIALLNS---PLLKE-------YDISSIRACISGSAPLPV------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 305 lrffgiggskldGVVEKFLADAGFPYGIGYGLTETSP------LLAGAIPGK--VKWQSTGPKLPDIEM-KILNPNhkKI 375
Cdd:PRK06710 338 ------------EVQEKFETVTGGKLVEGYGLTESSPvthsnfLWEKRVPGSigVPWPDTEAMIMSLETgEALPPG--EI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 376 GEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLE 455
Cdd:PRK06710 404 GEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEEVLYEHEKVQE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 456 SLVVNTKGKlvamvhFNYEQIEKLHTFNEEAEVNMTQRVEEVKKELMEYvnsrvnkssKILEILEQSSPFEKTATQKIKR 535
Cdd:PRK06710 482 VVTIGVPDP------YRGETVKAFVVLKEGTECSEEELNQFARKYLAAY---------KVPKVYEFRDELPKTTVGKILR 546
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
35-459 |
5.04e-48 |
|
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: 172.57 E-value: 5.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILgnnMPNW---AVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVI 111
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQ---LPNWwefAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VSEKLhyklsaslldslklvismdtleviksaGEQDYtlneLPRPEDLASIIYTSGTSGASKGVMLTHRNLV--TQNYMA 189
Cdd:cd05903 79 VPERF---------------------------RQFDP----AAMPDAVALLLFTSGTTGEPKGVMHSHNTLSasIRQYAE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 190 NklLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVplivekiyknkirpm 269
Cdd:cd05903 128 R--LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVV-LQDIWDPDKALALMREHGVTFMMGA--------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 ftktwiTQFLYSISfirRALHKvAGKKLCQtfggnLRFFGIGGSKLDGVVEKFLADAGFPYGIG-YGLTETSPLLAGAIP 348
Cdd:cd05903 190 ------TPFLTDLL---NAVEE-AGEPLSR-----LRTFVCGGATVPRSLARRAAELLGAKVCSaYGSTECPGAVTSITP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 349 GKV--KWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTAScFTEDGWFRTKDLGYIDKNGNLY 421
Cdd:cd05903 255 APEdrRLYTDGRPLPGVEIKVVDDTGATlapgvEGELLSRGPSVFLGYLDRPDLTAD-AAPEGWFRTGDLARLDEDGYLR 333
|
410 420 430
....*....|....*....|....*....|....*...
gi 1309054211 422 IKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05903 334 ITGRSKDIII-RGGENIPVLEVEDLLLGHPGVIEAAVV 370
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
31-459 |
6.11e-48 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 173.51 E-value: 6.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 31 NKEKLTYREFGDSVEHLTEIL-NKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSV 109
Cdd:PRK06839 24 EEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 110 VIVSEKLhyklsASLLDSLKLVISMDTLEVIKS-AGEQDYTLNEL-PRPEDLASII-YTSGTSGASKGVMLTHRNLVTqN 186
Cdd:PRK06839 104 LFVEKTF-----QNMALSMQKVSYVQRVISITSlKEIEDRKIDNFvEKNESASFIIcYTSGTTGKPKGAVLTQENMFW-N 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 187 YMANKL-LPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIyknk 265
Cdd:PRK06839 178 ALNNTFaIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVII-VPRKFEPTKALSMIEKHKVTVVMGVPTIHQAL---- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 266 irpmftktwitqfLYSISFIRRALHKVagkklcqtfggnlRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETSP--LL 343
Cdd:PRK06839 253 -------------INCSKFETTNLQSV-------------RWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPtvFM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 344 AGAIPGKVKWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNG 418
Cdd:PRK06839 307 LSEEDARRKVGSIGKPVLFCDYELIDENKNKvevgeVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1309054211 419 NLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK06839 386 FVYIVGRKKEMII-SGGENIYPLEVEQVINKLSDVYEVAVV 425
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
156-459 |
6.16e-48 |
|
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: 169.77 E-value: 6.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 156 PEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPiFREDVFLSI-LPLSHAYECSLGLILPLSRGAQVVYLHGAP 234
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLG-LTEQDRLCIpVPLFHCFGSVLGVLACLTHGATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 235 TPSLLLPALTQVRPTIMLSVPLIVEKIYKnkiRPMFTKtwitqflYSISFIRRALhkvagkklcqtfggnlrffgIGGSK 314
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFIAELE---HPDFDK-------FDLSSLRTGI--------------------MAGAP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 315 -----LDGVVEKF-LADagfpYGIGYGLTETSPLLAGAIPG---KVKWQSTGPKLPDIEMKILNPNHKKI------GEIV 379
Cdd:cd05917 130 cppelMKRVIEVMnMKD----VTIAYGMTETSPVSTQTRTDdsiEKRVNTVGRIMPHTEAKIVDPEGGIVppvgvpGELC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 380 VKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDnmMVGANGENIYPEEIEATINEHDMVLESLV 458
Cdd:cd05917 206 IRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRiKD--MIIRGGENIYPREIEEFLHTHPKVSDVQV 283
|
.
gi 1309054211 459 V 459
Cdd:cd05917 284 V 284
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
35-462 |
2.91e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 172.84 E-value: 2.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEIL-NKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVS 113
Cdd:PRK08314 36 ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 114 EKLHYKLsASLLDSLKL--VIS---MDTL----------------EVIKSAGEQDYTLNE------LPRP-----EDLAS 161
Cdd:PRK08314 116 SELAPKV-APAVGNLRLrhVIVaqySDYLpaepeiavpawlraepPLQALAPGGVVAWKEalaaglAPPPhtagpDDLAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 162 IIYTSGTSGASKGVMLTHRNLvtqnyMANKLLPIF-----REDVFLSILPLSHAYECSLGLILPLSRGAQVVYLhgaptP 236
Cdd:PRK08314 195 LPYTSGTTGVPKGCMHTHRTV-----MANAVGSVLwsnstPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLM-----P 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 237 ----SLLLPALTQVRPTIMLSVPlivekiyknkirpmftkTWITQFLYSISFIRRALHKvagkklcqtfggnLRFFGIGG 312
Cdd:PRK08314 265 rwdrEAAARLIERYRVTHWTNIP-----------------TMVVDFLASPGLAERDLSS-------------LRYIGGGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 313 SKL-DGVVEKFLADAGFPYGIGYGLTET-SPLLAGAiPGKVKWQSTGPKLPDIEMKILNPN------HKKIGEIVVKGPN 384
Cdd:PRK08314 315 AAMpEAVAERLKELTGLDYVEGYGLTETmAQTHSNP-PDRPKLQCLGIPTFGVDARVIDPEtleelpPGEVGEIVVHGPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 385 VMSGYYKDPVTTASCFTE-DG--WFRTKDLGYIDKNGNLYIKGR-KdnMMVGANGENIYPEEIEATINEHDMVLESLVVN 460
Cdd:PRK08314 394 VFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGYFFITDRlK--RMINASGFKVWPAEVENLLYKHPAIQEACVIA 471
|
..
gi 1309054211 461 TK 462
Cdd:PRK08314 472 TP 473
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
35-537 |
8.54e-47 |
|
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: 170.63 E-value: 8.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLSASLLDSLKLVISMDtleVIKSAGEQDYTL---NELP-----------RPEDLASIIYTSGTSGASKGVMLTHR 180
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLI---VSGGAGPEAGALllaELVAaeaeqlkpaatHADDPAFWLYSSGSTGRPKGVVHLHA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 181 NL-VTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLLLPALTQVRPTIMLSVPlive 259
Cdd:cd05959 187 DIyWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRPTVFFGVP---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 260 KIYKNKIR-PMFTKtwitqflYSISFIRRALHkvAGKKLCQTFGGNLR-FFGIggSKLDGVvekfladagfpygigyGLT 337
Cdd:cd05959 263 TLYAAMLAaPNLPS-------RDLSSLRLCVS--AGEALPAEVGERWKaRFGL--DILDGI----------------GST 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 338 ETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLG 412
Cdd:cd05959 316 EMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGdvadgEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 413 YIDKNGNLYIKGRKDNMMvGANGENIYPEEIEATINEHDMVLESLVVNTKG-----KLVAMVHFNYEqieklhtfneeae 487
Cdd:cd05959 395 VRDDDGFYTYAGRADDML-KVSGIWVSPFEVESALVQHPAVLEAAVVGVEDedgltKPKAFVVLRPG------------- 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1309054211 488 vnmTQRVEEVKKELMEYVNSRVnKSSKILEILEQSSPFEKTATQKIKRYL 537
Cdd:cd05959 461 ---YEDSEALEEELKEFVKDRL-APYKYPRWIVFVDELPKTATGKIQRFK 506
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
9-537 |
8.91e-47 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 171.47 E-value: 8.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFSLINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAIlgnNMPNWA---VSYFAITTSSRV 85
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAF---QLPGWCeftIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 86 VVPILPDFTAFEIVNVIEHSESSVVI----------------VSEKLHYKLSASLLDSLKLVISMDTLEVIKSAGEqdyT 149
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKMFFaptlfkqtrpvdlilpLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYE---P 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 150 LNELP--RPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQV 227
Cdd:PRK06087 178 LTTAIttHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 228 VyLHGAPTPSLLLPALTQVRPTIMLSVplivekiyknkirpmftktwiTQFLYSI-SFIRRALHKVAgkklcqtfggNLR 306
Cdd:PRK06087 258 V-LLDIFTPDACLALLEQQRCTCMLGA---------------------TPFIYDLlNLLEKQPADLS----------ALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 307 FFGIGGSkldgVVEKFLADAGFPYGIG----YGLTETSPL----LAGAIPGKVKWqsTGPKLPDIEMKILNPNHKKI--- 375
Cdd:PRK06087 306 FFLCGGT----TIPKKVARECQQRGIKllsvYGSTESSPHavvnLDDPLSRFMHT--DGYAAAGVEIKVVDEARKTLppg 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 376 --GEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMV 453
Cdd:PRK06087 380 ceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIV-RGGENISSREVEDILLQHPKI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 454 LESLVVNTKGKLVAmvhfnyeqiEKLHTFNEEAEVNMTQRVEEVKKELMEyvnSRVNKsSKILEILEQSSPFEKTATQKI 533
Cdd:PRK06087 459 HDACVVAMPDERLG---------ERSCAYVVLKAPHHSLTLEEVVAFFSR---KRVAK-YKYPEHIVVIDKLPRTASGKI 525
|
....
gi 1309054211 534 KRYL 537
Cdd:PRK06087 526 QKFL 529
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
23-459 |
1.78e-46 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 169.37 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 23 EQTAFSlINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVI 102
Cdd:PRK03640 17 DRTAIE-FEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 103 EHSESSVVIVSEklhyklsaSLLDSLKLVISMDTLEVIKSAgEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNl 182
Cdd:PRK03640 96 DDAEVKCLITDD--------DFEAKLIPGISVKFAELMNGP-KEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGN- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 183 vtqNY---MANKL-LPIFREDVFLSILPLSHAYECSL---GLILPLSrgaqvVYLHGAPTPSLLLPALTQVRPTIMLSVP 255
Cdd:PRK03640 166 ---HWwsaVGSALnLGLTEDDCWLAAVPIFHISGLSIlmrSVIYGMR-----VVLVEKFDAEKINKLLQTGGVTIISVVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 256 LIVEKIYKnkirpmftktwitqflysisfirrALHKvagkklcQTFGGNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYG 335
Cdd:PRK03640 238 TMLQRLLE------------------------RLGE-------GTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 336 LTETSPLLAgAIPGK---VKWQSTGPKLPDIEMKI------LNPNhkKIGEIVVKGPNVMSGYYKDPVTTASCFtEDGWF 406
Cdd:PRK03640 287 MTETASQIV-TLSPEdalTKLGSAGKPLFPCELKIekdgvvVPPF--EEGEIVVKGPNVTKGYLNREDATRETF-QDGWF 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1309054211 407 RTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK03640 363 KTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLLSHPGVAEAGVV 414
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
34-425 |
3.81e-46 |
|
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: 168.66 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKhGVKKGEKVAILGNNMPNWAVSYFAITTSSRVvvPILPDFTAF--EIVNVIEHSESSVVI 111
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAGlrELRACIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VSEKLHYKLSASLLDSLKLVISMDTLEVIK---SAGE-----------QDYTLNELPR----PEDLASIIYTSGTSGASK 173
Cdd:cd05909 84 TSKQFIEKLKLHHLFDVEYDARIVYLEDLRakiSKADkckaflagkfpPKWLLRIFGVapvqPDDPAVILFTSGSEGLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 174 GVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYlhgAPTPslllpaltqvrptimLS 253
Cdd:cd05909 164 GVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF---HPNP---------------LD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 254 VPLIVEKIYKNKIRPMF-TKTWITQFLysisfirRALHKvagkklcQTFGGnLRFFGIGGSKL-DGVVEKFLADAGFPYG 331
Cdd:cd05909 226 YKKIPELIYDKKATILLgTPTFLRGYA-------RAAHP-------EDFSS-LRLVVAGAEKLkDTLRQEFQEKFGIRIL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 332 IGYGLTETSPLLAGAIPGKVKWQST-GPKLPDIEMKILNPNHK---KIGE---IVVKGPNVMSGYYKDPVTTaSCFTEDG 404
Cdd:cd05909 291 EGYGTTECSPVISVNTPQSPNKEGTvGRPLPGMEVKIVSVETHeevPIGEgglLLVRGPNVMLGYLNEPELT-SFAFGDG 369
|
410 420
....*....|....*....|.
gi 1309054211 405 WFRTKDLGYIDKNGNLYIKGR 425
Cdd:cd05909 370 WYDTGDIGKIDGEGFLTITGR 390
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
36-478 |
6.47e-46 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 170.97 E-value: 6.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEK 115
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 116 LHYKLSASLLDS---LKLVISM-----------DTLEVIKSAGEQDYTLNE-----LP--RPEDLASIIYTSGTSGASKG 174
Cdd:PLN02614 161 KISELFKTCPNSteyMKTVVSFggvsreqkeeaETFGLVIYAWDEFLKLGEgkqydLPikKKSDICTIMYTSGTTGDPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 175 VMLTHRNLVT-----QNYMANKLLPIFREDVFLSILPLSHAYECSLGLILpLSRGAQVVYLHGapTPSLLLPALTQVRPT 249
Cdd:PLN02614 241 VMISNESIVTliagvIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECF-IQHGAAIGFWRG--DVKLLIEDLGELKPT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 250 IMLSVPLIVEKIYKNKIRPM----FTKTWI--TQFLYSISFIRRALHKVAGKKLC---------QTFGGNLRFFGIGGSK 314
Cdd:PLN02614 318 IFCAVPRVLDRVYSGLQKKLsdggFLKKFVfdSAFSYKFGNMKKGQSHVEASPLCdklvfnkvkQGLGGNVRIILSGAAP 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 315 LDGVVEKFLADAGFPYGI-GYGLTETSPLLAGAIPGKVKWQST-GPKLPDIEMK---ILNPNHKKI-----GEIVVKGPN 384
Cdd:PLN02614 398 LASHVESFLRVVACCHVLqGYGLTESCAGTFVSLPDELDMLGTvGPPVPNVDIRlesVPEMEYDALastprGEICIRGKT 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 385 VMSGYYKDPVTTASCFTeDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDmVLESLVV---NT 461
Cdd:PLN02614 478 LFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQ-AVDSVWVygnSF 555
|
490
....*....|....*..
gi 1309054211 462 KGKLVAMVHFNYEQIEK 478
Cdd:PLN02614 556 ESFLVAIANPNQQILER 572
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
35-459 |
9.82e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 163.06 E-value: 9.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLH---Y-----------------KLSASLLDSLKLVISMDTL---------EVIKSAGEQ-DYTLNELPR---PEDLAS 161
Cdd:PRK08315 124 GFKdsdYvamlyelapelatcepgQLQSARLPELRRVIFLGDEkhpgmlnfdELLALGRAVdDAELAARQAtldPDDPIN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 162 IIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPiFREDVFLSI-LPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLLL 240
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILNNGYFIGEAMK-LTEEDRLCIpVPLYHCFGMVLGNLACVTHGATMVYPGEGFDPLATL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 241 PALTQVRPTIMLSVP--LIVEKIYknkirPMFTKtwitqflYSISFIRralhkvagkklcqTfggnlrffGI-GGSK--- 314
Cdd:PRK08315 283 AAVEEERCTALYGVPtmFIAELDH-----PDFAR-------FDLSSLR-------------T--------GImAGSPcpi 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 315 --LDGVVEKF-LADAGfpygIGYGLTETSPllagaipgkVKWQS------------TGPKLPDIEMKILNPNHKKI---- 375
Cdd:PRK08315 330 evMKRVIDKMhMSEVT----IAYGMTETSP---------VSTQTrtddplekrvttVGRALPHLEVKIVDPETGETvprg 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 376 --GEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDnmMVGANGENIYPEEIEATINEHDM 452
Cdd:PRK08315 397 eqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRiKD--MIIRGGENIYPREIEEFLYTHPK 474
|
....*..
gi 1309054211 453 VLESLVV 459
Cdd:PRK08315 475 IQDVQVV 481
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1-459 |
1.14e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 162.41 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 1 MISEVLGLSLADIYSRSLVDFSEQTAfsLINKEK-LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAI 79
Cdd:PRK08316 4 RSTRARRQTIGDILRRSARRYPDKTA--LVFGDRsWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 80 TTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEKLhyklsASLLDSLKLVISMDTLEVIKSAGEQDY----------- 148
Cdd:PRK08316 82 ARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPAL-----APTAEAALALLPVDTLILSLVLGGREApggwldfadwa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 149 ------TLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQnYMANKL-LPIFREDVFLSILPLSHAYECSLGLILPL 221
Cdd:PRK08316 157 eagsvaEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAE-YVSCIVaGDMSADDIPLHALPLYHCAQLDVFLGPYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 222 SRGAQVVYLhGAPTPSLLLPALTQVRPTIMLSVPLIvekiyknkirpmftktWITqFLYSISFIRRALhkvagkklcqtf 301
Cdd:PRK08316 236 YVGATNVIL-DAPDPELILRTIEAERITSFFAPPTV----------------WIS-LLRHPDFDTRDL------------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 302 gGNLRFFGIGGSKLDGVVEKFLADAgFPyGIG----YGLTETSPLLAGAIPG--KVKWQSTGPKLPDIEMKILNPNHKKI 375
Cdd:PRK08316 286 -SSLRKGYYGASIMPVEVLKELRER-LP-GLRfyncYGQTEIAPLATVLGPEehLRRPGSAGRPVLNVETRVVDDDGNDV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 376 -----GEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGR-KDnmMVGANGENIYPEEIEATINE 449
Cdd:PRK08316 363 apgevGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRkKD--MIKTGGENVASREVEEALYT 439
|
490
....*....|
gi 1309054211 450 HDMVLESLVV 459
Cdd:PRK08316 440 HPAVAEVAVI 449
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
8-462 |
4.69e-43 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 160.92 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 8 LSLADIYSRSLVDFSEQTAfsLINK---EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSR 84
Cdd:PLN02246 23 LPLHDYCFERLSEFSDRPC--LIDGatgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 85 VVVPILPDFTAFEIVNVIEHSESSVVIVSeklhyklsASLLDSLKLVISMDTLEVIKSAGEQDYTL----------NELP 154
Cdd:PLN02246 101 VTTTANPFYTPAEIAKQAKASGAKLIITQ--------SCYVDKLKGLAEDDGVTVVTIDDPPEGCLhfseltqadeNELP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 155 ----RPEDLASIIYTSGTSGASKGVMLTHRNLVT----QNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQ 226
Cdd:PLN02246 173 eveiSPDDVVALPYSSGTTGLPKGVMLTHKGLVTsvaqQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 227 VVYLHGAPTPsLLLPALTQVRPTIMLSVPLIVEKIYKNkirPMFTKtwitqflYSISFIRRALHKVA--GKKLCQTFGgn 304
Cdd:PLN02246 253 ILIMPKFEIG-ALLELIQRHKVTIAPFVPPIVLAIAKS---PVVEK-------YDLSSIRMVLSGAAplGKELEDAFR-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 305 lrffgiggSKLDGVVekfladagfpYGIGYGLTETSPLLAGAI-----PGKVKWQSTGPKLPDIEMKILNPN------HK 373
Cdd:PLN02246 320 --------AKLPNAV----------LGQGYGMTEAGPVLAMCLafakePFPVKSGSCGTVVRNAELKIVDPEtgaslpRN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 374 KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDnmMVGANGENIYPEEIEATINEHDM 452
Cdd:PLN02246 382 QPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRlKE--LIKYKGFQVAPAELEALLISHPS 459
|
490
....*....|
gi 1309054211 453 VLESLVVNTK 462
Cdd:PLN02246 460 IADAAVVPMK 469
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
20-515 |
5.08e-43 |
|
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: 160.77 E-value: 5.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 20 DFSEQTAFS-LINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEI 98
Cdd:cd17642 29 SVPGTIAFTdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNEREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 99 VNVIEHSESSVVIVSEKLHYKLS--ASLLDSLKLVISMDTLEVIK---------------SAGEQDYTLNELPRPEDLAS 161
Cdd:cd17642 109 DHSLNISKPTIVFCSKKGLQKVLnvQKKLKIIKTIIILDSKEDYKgyqclytfitqnlppGFNEYDFKPPSFDRDEQVAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 162 IIYTSGTSGASKGVMLTHRNLVTQnyMANKLLPIF-----REDVFLSILPLSHAYECsLGLILPLSRGAQVVYLHGApTP 236
Cdd:cd17642 189 IMNSSGSTGLPKGVQLTHKNIVAR--FSHARDPIFgnqiiPDTAILTVIPFHHGFGM-FTTLGYLICGFRVVLMYKF-EE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 237 SLLLPALTQVRPTIMLSVPLIVEKIYKNkirPMFTKtwitqflYSISfirrALHKVA--GKKLCQTFGgnlrffgiggsk 314
Cdd:cd17642 265 ELFLRSLQDYKVQSALLVPTLFAFFAKS---TLVDK-------YDLS----NLHEIAsgGAPLSKEVG------------ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 315 lDGVVEKFladaGFPyGI--GYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKKI------GEIVVKGPNVM 386
Cdd:cd17642 319 -EAVAKRF----KLP-GIrqGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTlgpnerGELCVKGPMIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 387 SGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV----NTK 462
Cdd:cd17642 393 KGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQHPKIFDAGVAgipdEDA 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1309054211 463 GKLVAMVhfnyeqieklhtFNEEAEVNMTQrveevkKELMEYVNSRVNKSSKI 515
Cdd:cd17642 472 GELPAAV------------VVLEAGKTMTE------KEVMDYVASQVSTAKRL 506
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
33-454 |
5.95e-43 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 160.87 E-value: 5.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGvKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFE---IVNVIEHSESSV 109
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 110 VIVSEKLHYKLSASLLDSLKL----VISMDTLEViksaGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQ 185
Cdd:cd05931 102 VLTTAAALAAVRAFAASRPAAgtprLLVVDLLPD----TSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLAN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 186 NYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLhgAPT-----PSLLLPALTQVRPTIMlSVPlivek 260
Cdd:cd05931 178 VRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM--SPAaflrrPLRWLRLISRYRATIS-AAP----- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 261 iykNkirpmftktwitqFLYSIsfirrALHKVAGKKLCQTFGGNLRFFGIGG-----SKLDGVVEKFlADAGF------P 329
Cdd:cd05931 250 ---N-------------FAYDL-----CVRRVRDEDLEGLDLSSWRVALNGAepvrpATLRRFAEAF-APFGFrpeafrP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 330 ygiGYGLTETSPLLAGAIPGK--------------------------VKWQSTGPKLPDIEMKILNPNHKK------IGE 377
Cdd:cd05931 308 ---SYGLAEATLFVSGGPPGTgpvvlrvdrdalagravavaaddpaaRELVSCGRPLPDQEVRIVDPETGRelpdgeVGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 378 IVVKGPNVMSGYYKDPVTTASCF------TEDGWFRTKDLGYIDKnGNLYIKGRKDNMMVgANGENIYPEEIEATINEHD 451
Cdd:cd05931 385 IWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLHD-GELYITGRLKDLII-VRGRNHYPQDIEATAEEAH 462
|
...
gi 1309054211 452 MVL 454
Cdd:cd05931 463 PAL 465
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
33-535 |
1.49e-42 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 161.82 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PLN02387 105 EWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSA--SLLDSLKLVISMD-------------------TLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGA 171
Cdd:PLN02387 185 DSKQLKKLIDisSQLETVKRVIYMDdegvdsdsslsgssnwtvsSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 172 SKGVMLTHRNLVTQNYMANKLLP-IFREDVFLSILPLSHAYECSLGLILpLSRGAQVVYlhGAPtpsLLLP--------- 241
Cdd:PLN02387 265 PKGVMMTHGNIVATVAGVMTVVPkLGKNDVYLAYLPLAHILELAAESVM-AAVGAAIGY--GSP---LTLTdtsnkikkg 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 242 ---ALTQVRPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFLYSISFIRR------------ALHKV-----AGKKLCQTF 301
Cdd:PLN02387 339 tkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRlaaiegswfgawGLEKLlwdalVFKKIRAVL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 302 GGNLRFFGIGGSKLDGVVEKFLADA-GFPYGIGYGLTETSpllAGAIPGkvKWQST-----GPKLPDIEMKILN------ 369
Cdd:PLN02387 419 GGRIRFMLSGGAPLSGDTQRFINIClGAPIGQGYGLTETC---AGATFS--EWDDTsvgrvGPPLPCCYVKLVSweeggy 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 370 -----PNHKkiGEIVVKGPNVMSGYYKDPVTTASCFTEDG----WFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYP 440
Cdd:PLN02387 494 lisdkPMPR--GEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSL 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 441 EEIEATINEHDMVlESLVVNT---KGKLVAMVHFNYEQIEKLH-----TFNEEAEV-NMTQRVEEVKKELMEYV-NSRVN 510
Cdd:PLN02387 572 GKVEAALSVSPYV-DNIMVHAdpfHSYCVALVVPSQQALEKWAkkagiDYSNFAELcEKEEAVKEVQQSLSKAAkAARLE 650
|
570 580 590
....*....|....*....|....*....|.
gi 1309054211 511 KS---SKILEILEQSSPfEK---TATQKIKR 535
Cdd:PLN02387 651 KFeipAKIKLLPEPWTP-ESglvTAALKLKR 680
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
35-459 |
3.20e-42 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 158.12 E-value: 3.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLSAslLDSLKLVISMDTL------EVIKSAGEQDYTLNELPR-PEDLASIIYTSGTSGASKGVMLTHRNLVTqNY 187
Cdd:PRK07514 109 ANFAWLSK--IAAAAGAPHVETLdadgtgSLLEAAAAAPDDFETVPRgADDLAAILYTSGTTGRSKGAMLSHGNLLS-NA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 188 MANKLLPIFRE-DVFLSILPLSHAYecslGLILplsrGAQVVYLHGAPTpsLLLPAL--TQV-----RPTIMLSVPlive 259
Cdd:PRK07514 186 LTLVDYWRFTPdDVLIHALPIFHTH----GLFV----ATNVALLAGASM--IFLPKFdpDAVlalmpRATVMMGVP---- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 260 kiyknkirpmftkTWITQFLYSISFIRRALhkvagkklcqtfgGNLRFFgIGGSK--LDGVVEKFLADAGFPYGIGYGLT 337
Cdd:PRK07514 252 -------------TFYTRLLQEPRLTREAA-------------AHMRLF-ISGSAplLAETHREFQERTGHAILERYGMT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 338 ET-----SPLLAGAIPGKVkwqstGPKLPDIEMKILNPNHKK------IGEIVVKGPNVMSGYYKDPVTTASCFTEDGWF 406
Cdd:PRK07514 305 ETnmntsNPYDGERRAGTV-----GFPLPGVSLRVTDPETGAelppgeIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFF 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 407 RTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07514 380 ITGDLGKIDERGYVHIVGRgKDLIISG--GYNVYPKEVEGEIDELPGVVESAVI 431
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
9-459 |
2.07e-41 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 156.72 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFSLINKEkLTYREFGDSVEHLTEILNKHGVKKGEKVAILgnnMPN---WAVSYFAITTSSRV 85
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKA-ITYGELDELSRALAAWLQSRGLAKGARVAIM---MPNvlqYPVAIAAVLRAGYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 86 VVPILPDFTAFEIVNVIEHSESSVVIVSEKLHYKLSASLLD-SLKLVI--SMDTLEVIK--------------------- 141
Cdd:PRK07059 100 VVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKtAVKHVVvaSMGDLLGFKghivnfvvrrvkkmvpawslp 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 142 ---------SAGEQdYTLNELP-RPEDLASIIYTSGTSGASKGVMLTHRNLVTqNYMANK--LLPIFRED------VFLS 203
Cdd:PRK07059 180 ghvrfndalAEGAR-QTFKPVKlGPDDVAFLQYTGGTTGVSKGATLLHRNIVA-NVLQMEawLQPAFEKKprpdqlNFVC 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 204 ILPLSHAYECSLGLILPLSRGAQvvylhgaptpSLLLPaltqvRPtimLSVPLIVEKIYKNKIRpMF--TKTWITQFLYS 281
Cdd:PRK07059 258 ALPLYHIFALTVCGLLGMRTGGR----------NILIP-----NP---RDIPGFIKELKKYQVH-IFpaVNTLYNALLNN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 282 ISFirralHKVAGKKLCQTFGGnlrffgiGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQST-GPKL 360
Cdd:PRK07059 319 PDF-----DKLDFSKLIVANGG-------GMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTiGLPL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 361 PDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANG 435
Cdd:PRK07059 387 PSTEVSIRDDDGNdlplgEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMIL-VSG 465
|
490 500
....*....|....*....|....
gi 1309054211 436 ENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07059 466 FNVYPNEIEEVVASHPGVLEVAAV 489
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
36-458 |
5.69e-41 |
|
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: 152.42 E-value: 5.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNK-HGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLhyklsASLLDSLKLVISMDTLEVIKSAGEQDY--TLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVtqNYMA--N 190
Cdd:TIGR01733 81 AL-----ASRLAGLVLPVILLDPLELAALDDAPAppPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLV--NLLAwlA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 KLLPIFREDVFLSILPLSH---AYEcslgLILPLSRGAQVVYL---HGAPTPSLLLPALTQVRPTIMLSVPlivekiykn 264
Cdd:TIGR01733 154 RRYGLDPDDRVLQFASLSFdasVEE----IFGALLAGATLVVPpedEERDDAALLAALIAEHPVTVLNLTP--------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 265 kirpmftkTWITQFLYSISFIRRALHKVAgkklcqtfggnlrffgIGGSKLD-GVVEKFLADAGFPYGI-GYGLTETS-- 340
Cdd:TIGR01733 221 --------SLLALLAAALPPALASLRLVI----------------LGGEALTpALVDRWRARGPGARLInLYGPTETTvw 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 341 ---PLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFTEDG-------- 404
Cdd:TIGR01733 277 staTLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPvpvgvVGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgar 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 405 WFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLV 458
Cdd:TIGR01733 357 LYRTGDLVRYLPDGNLEFLGRIDD-QVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
158-459 |
1.10e-40 |
|
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: 149.79 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 158 DLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHayecsLGLILPLSR----GAQVVYLHGA 233
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYH-----VGGLAILVRsllaGAELVLLERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 234 PtpsLLLPALTQVRPTIMLSVPlivekiyknkirpmftktwiTQflysisfIRRALHKVAGKKLCQTFGGNLrffgIGGS 313
Cdd:cd17630 76 Q---ALAEDLAPPGVTHVSLVP--------------------TQ-------LQRLLDSGQGPAALKSLRAVL----LGGA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 314 KLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPnhkkiGEIVVKGPNVMSGYYKDP 393
Cdd:cd17630 122 PIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----GEIWVGGASLAMGYLRGQ 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 394 VTTAscFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17630 197 LVPE--FNEDGWFTTKDLGELHADGRLTVLGRADNMII-SGGENIQPEEIEAALAAHPAVRDAFVV 259
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
44-459 |
5.25e-40 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 151.05 E-value: 5.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 44 VEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSS----RVVVPILPDFTAFEIVNVIEHSESSVVIVSEKLHYK 119
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 120 LSASLLDS--LKLVISMDTLeviksAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFR 197
Cdd:cd05922 83 LRDALPASpdPGTVLDADGI-----RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 198 EDVFLSILPLSHAYECSLgLILPLSRGAQVVYLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPMFTKTwitq 277
Cdd:cd05922 158 DDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPS---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 278 flysisfirralhkvagkklcqtfggnLRFFGIGGSKLDGVVEKFLADAgFPYG---IGYGLTETSPLLAGAIPGKV--K 352
Cdd:cd05922 233 ---------------------------LRYLTQAGGRLPQETIARLREL-LPGAqvyVMYGQTEATRRMTYLPPERIleK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 353 WQSTGPKLPDIEMKILNPN-----HKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKD 427
Cdd:cd05922 285 PGSIGLAIPGGEFEILDDDgtptpPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRD 364
|
410 420 430
....*....|....*....|....*....|..
gi 1309054211 428 NmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05922 365 R-MIKLFGNRISPTEIEAAARSIGLIIEAAAV 395
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
34-537 |
5.39e-40 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 152.65 E-value: 5.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVS 113
Cdd:PLN02860 32 RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 114 EKLHY---KLSASLLDSLKLVISMD--------------TLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVM 176
Cdd:PLN02860 112 ETCSSwyeELQNDRLPSLMWQVFLEspsssvfiflnsflTTEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 177 LTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILpLSRGAQVVYLhgaPT--PSLLLPALTQVRPTIMLSV 254
Cdd:PLN02860 192 ISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAM-LMVGACHVLL---PKfdAKAALQAIKQHNVTSMITV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 255 PLIVEKIyknkIRPMFTK-TWitqflYSISFIRRALHkvagkklcqtfGGNlrffGIGGSKLDGVVEKFLADAGFPygiG 333
Cdd:PLN02860 268 PAMMADL----ISLTRKSmTW-----KVFPSVRKILN-----------GGG----SLSSRLLPDAKKLFPNAKLFS---A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 334 YGLTET---------------SPLLAGAIPGKVKWQSTGPK--------LPDIEMKILNPNHKKIGEIVVKGPNVMSGYY 390
Cdd:PLN02860 321 YGMTEAcssltfmtlhdptleSPKQTLQTVNQTKSSSVHQPqgvcvgkpAPHVELKIGLDESSRVGRILTRGPHVMLGYW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 391 KDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNT-KGKLVAMV 469
Cdd:PLN02860 401 GQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSND-RIKTGGENVYPEEVEAVLSQHPGVASVVVVGVpDSRLTEMV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 470 ------HFNYEQIEKLHtfnEEAEVNMTQRVEEVKKELMEYVNSRVnKSSKILEILEQssPFEKTATQKIKRYL 537
Cdd:PLN02860 480 vacvrlRDGWIWSDNEK---ENAKKNLTLSSETLRHHCREKNLSRF-KIPKLFVQWRK--PFPLTTTGKIRRDE 547
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
26-459 |
2.21e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 149.96 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 26 AFSLINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHS 105
Cdd:PRK09088 14 AVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 106 ESSVvIVSEKLHYKLSASLLDSLKLVISMDTLEVIKSAgeqdytlnelPRPEDLASII-YTSGTSGASKGVMLTHRNLVT 184
Cdd:PRK09088 94 EPRL-LLGDDAVAAGRTDVEDLAAFIASADALEPADTP----------SIPPERVSLIlFTSGTSGQPKGVMLSERNLQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 185 QNYMANKLLPIFREDVFLSILPLSHAyecsLGLIlplsrgaqvvylhgaptpslllpalTQVRPTIMLSVPLIVEkiykN 264
Cdd:PRK09088 163 TAHNFGVLGRVDAHSSFLCDAPMFHI----IGLI-------------------------TSVRPVLAVGGSILVS----N 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 265 KIRPMFTKTWITQFLYSISfirralHKVAGKKLCQTFGGNLRFFGIGGSKLDGVV--------EKFLA--DAGFPYGIGY 334
Cdd:PRK09088 210 GFEPKRTLGRLGDPALGIT------HYFCVPQMAQAFRAQPGFDAAALRHLTALFtggaphaaEDILGwlDDGIPMVDGF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 335 GLTETS-----PLLAGAIPGKVKwqSTGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFTEDG 404
Cdd:PRK09088 284 GMSEAGtvfgmSVDCDVIRAKAG--AAGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDG 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1309054211 405 WFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK09088 362 WFRTGDIARRDADGFFWVVDRKKDMFI-SGGENVYPAEIEAVLADHPGIRECAVV 415
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
9-501 |
2.18e-38 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 148.10 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFSLINKeKLTYREFGDSVEHLTE-ILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVV 87
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGK-TITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 88 PILPDFTAFEIVNVIEHSESSVVIVSEKLHYKLSASLLDS-LKLVISM---DTLEVIKSAGEQ-----------DYTLNE 152
Cdd:PRK08751 105 NVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTpVKQVITTglgDMLGFPKAALVNfvvkyvkklvpEYRING 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 153 LPR-------------------PEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMA-------NKLLPifREDVFLSILP 206
Cdd:PRK08751 185 AIRfrealalgrkhsmptlqiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqwlagtGKLEE--GCEVVITALP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 207 LSHAYECSL-GLILPLSRGAQVVYLHGAPTPSLLlPALTQVRPTIMLSVPLIVEKIYKNkirPMFTKtwitqflysISFi 285
Cdd:PRK08751 263 LYHIFALTAnGLVFMKIGGCNHLISNPRDMPGFV-KELKKTRFTAFTGVNTLFNGLLNT---PGFDQ---------IDF- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 286 rralhkvagKKLCQTFGGnlrffgiGGSKLDGVVEKFLADAGFPYGIGYGLTETSPllaGAIPGKVKWQ----STGPKLP 361
Cdd:PRK08751 329 ---------SSLKMTLGG-------GMAVQRSVAERWKQVTGLTLVEAYGLTETSP---AACINPLTLKeyngSIGLPIP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 362 DIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGE 436
Cdd:PRK08751 390 STDACIKDDAGTvlaigEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMIL-VSGF 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309054211 437 NIYPEEIEATINEHDMVLESLVVNT----KGKLVAMVHFNYEQIEKLHTFNEEAEVNMTQ----RVEEVKKEL 501
Cdd:PRK08751 469 NVYPNEIEDVIAMMPGVLEVAAVGVpdekSGEIVKVVIVKKDPALTAEDVKAHARANLTGykqpRIIEFRKEL 541
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
35-454 |
2.42e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 149.36 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLsASLLDSLKL----VISMDTL-EVIKSAGEQDY-----------TLNELPRP-----EDLASIIYTSGTSGASK 173
Cdd:PTZ00216 202 KNVPNL-LRLMKSGGMpnttIIYLDSLpASVDTEGCRLVawtdvvakghsAGSHHPLNipennDDLALIMYTSGTTGDPK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 174 GVMLTHRNLV----TQNYMANKLLPIFRED-VFLSILPLSHAYECSLGLILpLSRGAQVVYlhgaPTPSLLLPA------ 242
Cdd:PTZ00216 281 GVMHTHGSLTagilALEDRLNDLIGPPEEDeTYCSYLPLAHIMEFGVTNIF-LARGALIGF----GSPRTLTDTfarphg 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 243 -LTQVRPTIMLSVPLIVEKIYKN---KI-------RPMFTKTWITQFlysisfirRALHKvaGK-----------KLCQT 300
Cdd:PTZ00216 356 dLTEFRPVFLIGVPRIFDTIKKAveaKLppvgslkRRVFDHAYQSRL--------RALKE--GKdtpywnekvfsAPRAV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 301 FGGNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYGLTETspLLAGAI--PGKVKWQSTGPKLPDIEMKILNPNHKK---- 374
Cdd:PTZ00216 426 LGGRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTET--VCCGGIqrTGDLEPNAVGQLLKGVEMKLLDTEEYKhtdt 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 375 ---IGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHD 451
Cdd:PTZ00216 504 pepRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNE 583
|
...
gi 1309054211 452 MVL 454
Cdd:PTZ00216 584 LVV 586
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
33-459 |
2.50e-38 |
|
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: 146.13 E-value: 2.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd05930 11 QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SeklhyklsaslldslklvismdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLVtqNYMAN-- 190
Cdd:cd05930 91 D------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLV--NLLLWmq 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 KLLPIFREDVFLSILPLS---HAYEcslgLILPLSRGAQVVYL--HGAPTPSLLLPALTQVRPTIMLSVPlivekiyknk 265
Cdd:cd05930 127 EAYPLTPGDRVLQFTSFSfdvSVWE----IFGALLAGATLVVLpeEVRKDPEALADLLAEEGITVLHLTP---------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 266 irpmftkTWITQFLYSISFIRRAlhkvagkklcqtfggNLRFFGIGGSKLDG-VVEKFlADAGFPYGI--GYGLTETS-- 340
Cdd:cd05930 193 -------SLLRLLLQELELAALP---------------SLRLVLVGGEALPPdLVRRW-RELLPGARLvnLYGPTEATvd 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 341 ---------PLLAGAIP-GKvkwqstgPkLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGW 405
Cdd:cd05930 250 atyyrvppdDEEDGRVPiGR-------P-IPNTRVYVLDENLRpvppgVPGELYIGGAGLARGYLNRPELTAERFVPNPF 321
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 406 F------RTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05930 322 GpgermyRTGDLVRWLPDGNLEFLGRIDD-QVKIRGYRIELGEIEAALLAHPGVREAAVV 380
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
35-446 |
4.69e-38 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 148.45 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KlhyKLSASL------------------------LDSLKLVISMDTLEVIKSAGEQDYtlnELPRPE--DLASIIYTSGT 168
Cdd:PLN02861 158 S---KISSILsclpkcssnlktivsfgdvsseqkEEAEELGVSCFSWEEFSLMGSLDC---ELPPKQktDICTIMYTSGT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 169 SGASKGVMLTHRNLVTQNYMANKLL-----PIFREDVFLSILPLSHAYECSLGlILPLSRGAQVVYLHGapTPSLLLPAL 243
Cdd:PLN02861 232 TGEPKGVILTNRAIIAEVLSTDHLLkvtdrVATEEDSYFSYLPLAHVYDQVIE-TYCISKGASIGFWQG--DIRYLMEDV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 244 TQVRPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFL------YSISFIRRALH---------KVAGKKLCQTFGGNLRFF 308
Cdd:PLN02861 309 QALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLfdfaynYKLGNLRKGLKqeeasprldRLVFDKIKEGLGGRVRLL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 309 GIGGSKLDGVVEKFL-ADAGFPYGIGYGLTETSPLLAGAIPGKVKWQST-GPKLPDIEMKILN-P-------NHKKIGEI 378
Cdd:PLN02861 389 LSGAAPLPRHVEEFLrVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTvGVPMTTIEARLESvPemgydalSDVPRGEI 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309054211 379 VVKGPNVMSGYYKDPVTTASCFTeDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEAT 446
Cdd:PLN02861 469 CLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENT 535
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
23-459 |
1.09e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 146.08 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 23 EQTAFSLINKEkLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVI 102
Cdd:PRK07786 32 DAPALRFLGNT-TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 103 EHSESSVVIVSEKLHyKLSASLLDslkLVISMDTLEVIKSAGEQD-YTLNELPR-----------PEDLASII-YTSGTS 169
Cdd:PRK07786 111 SDCGAHVVVTEAALA-PVATAVRD---IVPLLSTVVVAGGSSDDSvLGYEDLLAeagpahapvdiPNDSPALImYTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 170 GASKGVMLTHRNLVTQNYMANKLLPIFRE-DVFLSILPLSHAyeCSLGLILP-LSRGAQ-VVYLHGAPTPSLLLPALTQV 246
Cdd:PRK07786 187 GRPKGAVLTHANLTGQAMTCLRTNGADINsDVGFVGVPLFHI--AGIGSMLPgLLLGAPtVIYPLGAFDPGQLLDVLEAE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 247 RPTIMLSVPLIVEKIYknkirpmftktwitqflysisfirrALHKVAGKKLcqtfggNLRFFGIGGSKLDGVVEKFLADA 326
Cdd:PRK07786 265 KVTGIFLVPAQWQAVC-------------------------AEQQARPRDL------ALRVLSWGAAPASDTLLRQMAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 327 gFPYGI---GYGLTETSP---LLAG--AIPgkvKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDP 393
Cdd:PRK07786 314 -FPEAQilaAFGQTEMSPvtcMLLGedAIR---KLGSVGKVIPTVAARVVDENMNdvpvgEVGEIVYRAPTLMSGYWNNP 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 394 VTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07786 390 EATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMII-SGGENIYCAEVENVLASHPDIVEVAVI 453
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
23-505 |
6.12e-37 |
|
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: 142.00 E-value: 6.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 23 EQTAFsLINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVI 102
Cdd:cd05945 6 DRPAV-VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 103 EHSESSVVIVSeklhyklsaslldslklvismdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNL 182
Cdd:cd05945 85 DAAKPALLIAD------------------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 183 VTQNYMANKLLPIFREDVFLSILPLShaYECSLGLILP-LSRGAQVVYLHGAPT--PSLLLPALTQVRPTIMLSVPlive 259
Cdd:cd05945 123 VSFTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDLYPaLASGATLVPVPRDATadPKQLFRFLAEHGITVWVSTP---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 260 kiyknkirpmftktwitqflysiSFIRRALHKvagKKLCQTFGGNLRFFGIGGSKLDGVVEKFLADAgFP----YGIgYG 335
Cdd:cd05945 197 -----------------------SFAAMCLLS---PTFTPESLPSLRHFLFCGEVLPHKTARALQQR-FPdariYNT-YG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 336 LTETS-PLLAGAIPGKVKWQST----GPKLPDIEMKILNPN-----HKKIGEIVVKGPNVMSGYYKDPVTTAS-CFTEDG 404
Cdd:cd05945 249 PTEATvAVTYIEVTPEVLDGYDrlpiGYAKPGAKLVILDEDgrpvpPGEKGELVISGPSVSKGYLNNPEKTAAaFFPDEG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 405 --WFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV-----NTKGKLVAMVhfnyeqie 477
Cdd:cd05945 329 qrAYRTGDLVRLEADGLLFYRGRLDF-QVKLNGYRIELEEIEAALRQVPGVKEAVVVpkykgEKVTELIAFV-------- 399
|
490 500
....*....|....*....|....*....
gi 1309054211 478 klhTFNEEAEVNMTQRV-EEVKKELMEYV 505
Cdd:cd05945 400 ---VPKPGAEAGLTKAIkAELAERLPPYM 425
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
9-459 |
7.07e-37 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 143.66 E-value: 7.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFslINK-EKLTYREFGDSVEHLTEIL-NKHGVKKGEKVAILgnnMPN---WAVSYFAITTSS 83
Cdd:PRK08974 24 SLVDMFEQAVARYADQPAF--INMgEVMTFRKLEERSRAFAAYLqNGLGLKKGDRVALM---MPNllqYPIALFGILRAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 84 RVVVPILPDFTAFEIvnviEHS-----ESSVVIVS------EKL-------HYKLSaSLLDSL----------------K 129
Cdd:PRK08974 99 MIVVNVNPLYTPREL----EHQlndsgAKAIVIVSnfahtlEKVvfktpvkHVILT-RMGDQLstakgtlvnfvvkyikR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 130 LV--------ISMDtlEVIKSAGEQDYTLNELPRpEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKL-LPIFREDV 200
Cdd:PRK08974 174 LVpkyhlpdaISFR--SALHKGRRMQYVKPELVP-EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAyGPLLHPGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 201 FLSI--LPLSHAYECSLGLILPLSRGAQvvylhgaptpSLLLpalTQVRptimlSVPLIVEKIYKNKirpmFT-----KT 273
Cdd:PRK08974 251 ELVVtaLPLYHIFALTVNCLLFIELGGQ----------NLLI---TNPR-----DIPGFVKELKKYP----FTaitgvNT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 274 WITQFLYSISFirralHKVAGKKLCQTFGGnlrffgiGGSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKW 353
Cdd:PRK08974 309 LFNALLNNEEF-----QELDFSSLKLSVGG-------GMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 354 Q-STGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKD 427
Cdd:PRK08974 377 SgSIGLPVPSTEIKLVDDDGNevppgEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKK 455
|
490 500 510
....*....|....*....|....*....|..
gi 1309054211 428 NMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK08974 456 DMIL-VSGFNVYPNEIEDVVMLHPKVLEVAAV 486
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
16-459 |
1.48e-35 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 138.97 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 16 RSLVDFSEQTafSLINKE-KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFT 94
Cdd:cd12118 12 RAAAVYPDRT--SIVYGDrRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 95 AFEIVNVIEHSESSVVIVSEKLHYKlsaSLLDSLKlvismDTLEVIKSAGEQD-YTLNelprpedlasiiYTSGTSGASK 173
Cdd:cd12118 90 AEEIAFILRHSEAKVLFVDREFEYE---DLLAEGD-----PDFEWIPPADEWDpIALN------------YTSGTTGRPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 174 GVMLTHRNLVTqNYMANKLlpIFRED---VFLSILPLSHayeCSlGLILPLS---RGAQVVylhgaptpslllpALTQVR 247
Cdd:cd12118 150 GVVYHHRGAYL-NALANIL--EWEMKqhpVYLWTLPMFH---CN-GWCFPWTvaaVGGTNV-------------CLRKVD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 248 PtimlsvPLIVEKIYKNKIrpmftktwiTQFLYS---ISFIRRALHKVAGKklcqtFGGNLRFFgIGGSKLDGVVEKFLA 324
Cdd:cd12118 210 A------KAIYDLIEKHKV---------THFCGAptvLNMLANAPPSDARP-----LPHRVHVM-TAGAPPPAAVLAKME 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 325 DAGFPYGIGYGLTETSPLLAGAIpgkvkWQSTGPKLPDIE-----------------MKILNPNH--------KKIGEIV 379
Cdd:cd12118 269 ELGFDVTHVYGLTETYGPATVCA-----WKPEWDELPTEErarlkarqgvryvgleeVDVLDPETmkpvprdgKTIGEIV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 380 VKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMVLESLV 458
Cdd:cd12118 344 FRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRsKDIIISG--GENISSVEVEGVLYKHPAVLEAAV 420
|
.
gi 1309054211 459 V 459
Cdd:cd12118 421 V 421
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
35-535 |
1.51e-35 |
|
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: 137.85 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 klhyklsaslldslklvismdtleviksageqdytlnelprpEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLP 194
Cdd:cd05972 81 ------------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 195 IFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAP-TPSLLLPALTQVRPTIMLSVPLIVekiyknkirpmftKT 273
Cdd:cd05972 119 LRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRfDAERILELLERYGVTSFCGPPTAY-------------RM 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 274 WITQFLYSISFIRralhkvagkklcqtfggnLRFFGIGGSKLD-GVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVK 352
Cdd:cd05972 186 LIKQDLSSYKFSH------------------LRLVVSAGEPLNpEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVK 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 353 WQSTGPKLPDIEMKILNPNHK-----KIGEIVVK-GPNVM-SGYYKDPVTTASCFTEDgWFRTKDLGYIDKNGNLYIKGR 425
Cdd:cd05972 248 PGSMGRPTPGYDVAIIDDDGRelppgEEGDIAIKlPPPGLfLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 426 KDNMMVgANGENIYPEEIEATINEHDMVLESLVvntkgklVAMVHFNYEQIEKlhtfneeAEVNMTQ---RVEEVKKELM 502
Cdd:cd05972 327 ADDIIK-SSGYRIGPFEVESALLEHPAVAEAAV-------VGSPDPVRGEVVK-------AFVVLTSgyePSEELAEELQ 391
|
490 500 510
....*....|....*....|....*....|...
gi 1309054211 503 EYVNSRVnKSSKILEILEQSSPFEKTATQKIKR 535
Cdd:cd05972 392 GHVKKVL-APYKYPREIEFVEELPKTISGKIRR 423
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
21-462 |
1.95e-35 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 139.05 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 21 FSEQTAfsLINKE------KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFT 94
Cdd:PRK08008 20 YGHKTA--LIFESsggvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 95 AFEIVNVIEHSESSVVIVSEKL----------------HYKLSASLLDSLKLVISMDTLEviksaGEQDYTLNELP--RP 156
Cdd:PRK08008 98 REESAWILQNSQASLLVTSAQFypmyrqiqqedatplrHICLTRVALPADDGVSSFTQLK-----AQQPATLCYAPplST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 157 EDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAyECSLGLILP-LSRGAQVVYLHGApT 235
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHI-DCQCTAAMAaFSAGATFVLLEKY-S 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 236 PSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFLYSisfirraLHKVAGKKL--CQTFGgnLRFFGiggs 313
Cdd:PRK08008 251 ARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFY-------LNLSDQEKDafEERFG--VRLLT---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 314 kldgvvekfladagfpygiGYGLTETSPLLAGAIPG-KVKWQSTG-------PKLPDIEMKILNPNhkKIGEIVVKG--- 382
Cdd:PRK08008 318 -------------------SYGMTETIVGIIGDRPGdKRRWPSIGrpgfcyeAEIRDDHNRPLPAG--EIGEICIKGvpg 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 383 PNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTK 462
Cdd:PRK08008 377 KTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCN-MIKRGGENVSCVELENIIATHPKIQDIVVVGIK 455
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
33-459 |
1.76e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 133.09 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSaslLDSLKLVISMDTLEVIK--SAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMAN 190
Cdd:PRK06145 106 DEEFDAIVA---LETPKIVIDAAAQADSRrlAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 KLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAqVVYLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYknkirpmf 270
Cdd:PRK06145 183 IALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGG-TLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVL-------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 271 tkTWITQFLYSISFIRRAlhkVAGKKlcQTFGGNLRFFGiggskldgvvEKFladAGFPYGIGYGLTET----SPLLAGA 346
Cdd:PRK06145 254 --TVPDRDRFDLDSLAWC---IGGGE--KTPESRIRDFT----------RVF---TRARYIDAYGLTETcsgdTLMEAGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 347 IPGKVKwqSTGPKLPDIEMKI-------LNPNHKkiGEIVVKGPNVMSGYYKDPVTTASCFTeDGWFRTKDLGYIDKNGN 419
Cdd:PRK06145 314 EIEKIG--STGRALAHVEIRIadgagrwLPPNMK--GEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1309054211 420 LYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK06145 389 LYLTDRKKDMII-SGGENIASSEVERVIYELPEVAEAAVI 427
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
162-459 |
2.30e-33 |
|
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: 129.70 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 162 IIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLLLP 241
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 242 ALTQVrpTIMLSVPlivekiyknkirPMFTKtwITQFLYSISFIRRALHKVAGkklcqtfggnlrffgiggskLDG--VV 319
Cdd:cd17637 85 EEEKV--TLMGSFP------------PILSN--LLDAAEKSGVDLSSLRHVLG--------------------LDApeTI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 320 EKFLADAGFPYGIGYGLTETSPLLAGAiPGKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPV 394
Cdd:cd17637 129 QRFEETTGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDNDRpvpagETGEIVVRGPLVFQGYWNLPE 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 395 TTASCFtEDGWFRTKDLGYIDKNGNLYIKGRK-DNMMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17637 208 LTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVI 272
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
7-459 |
2.49e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 133.19 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 7 GLSLADIYSRSLVDFSEQTAFSLINKEkLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVV 86
Cdd:PRK06188 11 GATYGHLLVSALKRYPDRPALVLGDTR-LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 87 VPILP----DFTAFeivnVIEHSESSVVIVSEKLHYKLSASLL---DSLKLVISMDTLEVIKS-----AGEQDYTLNELP 154
Cdd:PRK06188 90 TALHPlgslDDHAY----VLEDAGISTLIVDPAPFVERALALLarvPSLKHVLTLGPVPDGVDllaaaAKFGPAPLVAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 155 RPEDLASIIYTSGTSGASKGVMLTHRNLVTQN--YMANKLLPifrEDV-FLSILPLSHAyecSLGLILP-LSRGAQVVYL 230
Cdd:PRK06188 166 LPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAqiQLAEWEWP---ADPrFLMCTPLSHA---GGAFFLPtLLRGGTVIVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 231 HGApTPSLLLPALTQVRPTIMLSVPL---------------------------------IVEKIykNKIRPMFTKTW-IT 276
Cdd:PRK06188 240 AKF-DPAEVLRAIEEQRITATFLVPTmiyalldhpdlrtrdlssletvyygaspmspvrLAEAI--ERFGPIFAQYYgQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 277 QFLYSISFIRRALHkvagkklcqtfggnlrffgiggsklDGVVEKFLADAGFPYgigygltetspllagaipgkvkwqst 356
Cdd:PRK06188 317 EAPMVITYLRKRDH-------------------------DPDDPKRLTSCGRPT-------------------------- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 357 gpklPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMV 431
Cdd:PRK06188 346 ----PGLRVALLDEDGREVaqgevGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIV 420
|
490 500
....*....|....*....|....*...
gi 1309054211 432 gANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK06188 421 -TGGFNVFPREVEDVLAEHPAVAQVAVI 447
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
9-455 |
3.20e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 133.35 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFSLINKeKLTYREFGDSVEHLTEILNKH-GVKKGEKVAILGNNMPNWAVSYFAITTSSRVVV 87
Cdd:PRK05677 25 NIQAVLKQSCQRFADKPAFSNLGK-TLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 88 PILPDFTAFEIVN----------------------VIEHSESSVVIVSE--KLHYKLSASLLDSL-----KLVISMDTLE 138
Cdd:PRK05677 104 NTNPLYTAREMEHqfndsgakalvclanmahlaekVLPKTGVKHVIVTEvaDMLPPLKRLLINAVvkhvkKMVPAYHLPQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 139 VIK-----SAGeQDYTLNEL-PRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFRED---VFLSILPLSH 209
Cdd:PRK05677 184 AVKfndalAKG-AGQPVTEAnPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 210 AYECSLGLILPLSRGAQVVYLhgaPTPSLLlpaltqvrptimlsvPLIVEKIYKNKirpmFTktwitqflysiSFIRRAL 289
Cdd:PRK05677 263 IYAFTFHCMAMMLIGNHNILI---SNPRDL---------------PAMVKELGKWK----FS-----------GFVGLNT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 290 HKVAgkkLCQTFG-GNLRFFGI-----GGSKLD-GVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKLPD 362
Cdd:PRK05677 310 LFVA---LCNNEAfRKLDFSALkltlsGGMALQlATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 363 IEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGEN 437
Cdd:PRK05677 387 TLCKVIDDDGNelplgEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMIL-VSGFN 465
|
490
....*....|....*...
gi 1309054211 438 IYPEEIEATINEHDMVLE 455
Cdd:PRK05677 466 VYPNELEDVLAALPGVLQ 483
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
35-469 |
4.76e-33 |
|
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: 131.64 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLSASLLdslklvISMDTLEVIKSAGEQdytLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLP 194
Cdd:cd12116 93 ALPDRLPAGLP------VLLLALAAAAAAPAA---PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 195 IFREDVFLSIlpLSHAYECS-LGLILPLSRGAQVVYlhgAPT-----PSLLLPALTQVRPTIMLSVPlivekiyknkirp 268
Cdd:cd12116 164 LGPGDRLLAV--TTYAFDISlLELLLPLLAGARVVI---APRetqrdPEALARLIEAHSITVMQATP------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 269 mftKTWiTQFLYSISFIRRALHkvagkKLCqtfggnlrffgiGGSKLD-GVVEKFLADAGFPYGIgYGLTETSpLLAGAi 347
Cdd:cd12116 226 ---ATW-RMLLDAGWQGRAGLT-----ALC------------GGEALPpDLAARLLSRVGSLWNL-YGPTETT-IWSTA- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 348 pGKVKWQST----GPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFTEDG-------WFRTKDL 411
Cdd:cd12116 282 -ARVTAAAGpipiGRPLANTQVYVLDAALRPvppgvPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDL 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309054211 412 GYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV----NTKGKLVAMV 469
Cdd:cd12116 361 VRRRADGRLEYLGRADG-QVKIRGHRIELGEIEAALAAHPGVAQAAVVvredGGDRRLVAYV 421
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
33-459 |
8.11e-33 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 132.10 E-value: 8.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAIlgnNMPNW---AVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSV 109
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSC---QLPNWwefTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 110 VIVSEKL----HYKLSASL---LDSLKLVI--------SMDTLeVIKSAGEQDYTLNEL-----PRPEDLASIIYTSGTS 169
Cdd:PRK13295 131 LVVPKTFrgfdHAAMARRLrpeLPALRHVVvvggdgadSFEAL-LITPAWEQEPDAPAIlarlrPGPDDVTQLIYTSGTT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 170 GASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHgAPTPSLLLPALTQVRPT 249
Cdd:PRK13295 210 GEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD-IWDPARAAELIRTEGVT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 250 IMLSVplivekiyknkirpmftktwiTQFLYSISfirRALhKVAGKKLCQtfggnLRFFGIGGSKLDG-VVEKflADAGF 328
Cdd:PRK13295 289 FTMAS---------------------TPFLTDLT---RAV-KESGRPVSS-----LRTFLCAGAPIPGaLVER--ARAAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 329 PYGI--GYGLTETSpLLAGAIPG---KVKWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTAS 398
Cdd:PRK13295 337 GAKIvsAWGMTENG-AVTLTKLDdpdERASTTDGCPLPGVEVRVVDADGAPlpagqIGRLQVRGCSNFGGYLKRPQLNGT 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309054211 399 CFteDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK13295 416 DA--DGWFDTGDLARIDADGYIRISGRsKDVIIRG--GENIPVVEIEALLYRHPAIAQVAIV 473
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
35-459 |
1.30e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 131.70 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLhYKLSASLLDSLKL----VISMD-------TLEV--------IKSAGEQDY----------TLNELPRPEDLASIIYT 165
Cdd:PRK06178 139 QL-APVVEQVRAETSLrhviVTSLAdvlpaepTLPLpdslraprLAAAGAIDLlpalractapVPLPPPALDALAALNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 166 SGTSGASKGVMLTHRNLVtqnYMANKLLPIF----REDVFLSILPLSHAYECSLGLILPLSRGAQVVYLhGAPTPSLLLP 241
Cdd:PRK06178 218 GGTTGMPKGCEHTQRDMV---YTAAAAYAVAvvggEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLL-ARWDAVAFMA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 242 ALTQVRPTIMLsvpLIVEKIYKNKIRPMFTKTWIT--QFLYSISFIrralhkvagKKLCQTFGGNLRffgiggsKLDGVV 319
Cdd:PRK06178 294 AVERYRVTRTV---MLVDNAVELMDHPRFAEYDLSslRQVRVVSFV---------KKLNPDYRQRWR-------ALTGSV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 320 ekfLADAGfpygigYGLTET-------------------SPLLAG-AIPGkvkwqsTGPKLPDIEMKILNPNHKKiGEIV 379
Cdd:PRK06178 355 ---LAEAA------WGMTEThtcdtftagfqdddfdllsQPVFVGlPVPG------TEFKICDFETGELLPLGAE-GEIV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 380 VKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMvGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK06178 419 VRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEML-KVNGMSVFPSEVEALLGQHPAVLGSAVV 496
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
158-459 |
1.58e-32 |
|
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: 127.23 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 158 DLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVylhgaptps 237
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 238 lllpaltqvrPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFLysisfirraLHKVAGKKLCQTfggNLRFFGIGGSKLDG 317
Cdd:cd17638 72 ----------PVAVFDVDAILEAIERERITVLPGPPTLFQSL---------LDHPGRKKFDLS---SLRAAVTGAATVPV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 318 V-VEKFLADAGF-PYGIGYGLTE--TSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPnhkkiGEIVVKGPNVMSGYYKDP 393
Cdd:cd17638 130 ElVRRMRSELGFeTVLTAYGLTEagVATMCRPGDDAETVATTCGRACPGFEVRIADD-----GEVLVRGYNVMQGYLDDP 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 394 VTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17638 205 EATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGALAEHPGVAQVAVI 269
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
35-459 |
6.29e-32 |
|
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: 128.00 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLSaslldslklvismdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLP 194
Cdd:cd05969 81 ELYERTD----------------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 195 IFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLLLPALTQVRPTIMLSVPlivekiykNKIRPMftktw 274
Cdd:cd05969 127 LHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAP--------TAIRML----- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 275 itqflysisfirralhKVAGKKLCQTFGGN-LRFFGIGGSKLDGVVEKFLADA-GFPYGIGYGLTETSPLLAGAIPG-KV 351
Cdd:cd05969 194 ----------------MKEGDELARKYDLSsLRFIHSVGEPLNPEAIRWGMEVfGVPIHDTWWQTETGSIMIANYPCmPI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 352 KWQSTGPKLPDIEMKI-------LNPNHKkiGEIVVKG--PNVMSGYYKDPVTTASCFTeDGWFRTKDLGYIDKNGNLYI 422
Cdd:cd05969 258 KPGSMGKPLPGVKAAVvdengneLPPGTK--GILALKPgwPSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWF 334
|
410 420 430
....*....|....*....|....*....|....*..
gi 1309054211 423 KGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05969 335 VGRADD-IIKTSGHRVGPFEVESALMEHPAVAEAGVI 370
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
156-536 |
6.61e-32 |
|
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: 128.76 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 156 PEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHayecSLGLI----LPLSRGAQVVYLH 231
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTH----DMGLIafhlAPLIAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 232 GA---PTPSLLLPALTQVRPTImLSVPLIVEKIYKNKIRPMFTKTWItqfLYSISFIRRALHKVAgKKLCQTFGGNLRFF 308
Cdd:cd05908 181 TRlfiRRPILWLKKASEHKATI-VSSPNFGYKYFLKTLKPEKANDWD---LSSIRMILNGAEPID-YELCHEFLDHMSKY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 309 GIGGSKL-------DGVVEKFLADAGFPYGI------GYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKK- 374
Cdd:cd05908 256 GLKRNAIlpvyglaEASVGASLPKAQSPFKTitlgrrHVTHGEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKIl 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 375 ----IGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIdKNGNLYIKGR-KDNMMVgaNGENIYPEEIEATINE 449
Cdd:cd05908 336 pdgyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGReKDIIFV--NGQNVYPHDIERIAEE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 450 HDMVLESLVV-----NTKGKLVAMVHFnyeqIEKLHTFNEEAEVnmtqrVEEVKKELMEYVNSRVNKSSKILEIleqssp 524
Cdd:cd05908 413 LEGVELGRVVacgvnNSNTRNEEIFCF----IEHRKSEDDFYPL-----GKKIKKHLNKRGGWQINEVLPIRRI------ 477
|
410
....*....|..
gi 1309054211 525 fEKTATQKIKRY 536
Cdd:cd05908 478 -PKTTSGKVKRY 488
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
10-459 |
1.10e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 128.24 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 10 LADIYSRSLVDFSEQTAFsLINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVP- 88
Cdd:PRK07470 9 LAHFLRQAARRFPDRIAL-VWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 89 ---ILPDftafEIVNVIEHSESSVVIVSEKL--HYKLSASLLDSLKLVISMDTlevikSAGEQDY---TLNELPRPEDLA 160
Cdd:PRK07470 88 nfrQTPD----EVAYLAEASGARAMICHADFpeHAAAVRAASPDLTHVVAIGG-----ARAGLDYealVARHLGARVANA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 161 SI--------IYTSGTSGASKGVMLTHRNL--VTQNYMANkLLP-IFREDVFLSILPLSHAyeCSLGLILPLSRGAQVVY 229
Cdd:PRK07470 159 AVdhddpcwfFFTSGTTGRPKAAVLTHGQMafVITNHLAD-LMPgTTEQDASLVVAPLSHG--AGIHQLCQVARGAATVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 230 LhgaPTPSLLLPALTQV----RPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFLYSISFIRRALHKVA----GKKLCQTF 301
Cdd:PRK07470 236 L---PSERFDPAEVWALverhRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRAlaklGKVLVQYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 302 G-----GNLRFFGIGGSKLDGVVEKFLADAGFPygigygltetspllagaipgkvkwqSTGPKLP--DIEMKILNPNhkK 374
Cdd:PRK07470 313 GlgevtGNITVLPPALHDAEDGPDARIGTCGFE-------------------------RTGMEVQiqDDEGRELPPG--E 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 375 IGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVL 454
Cdd:PRK07470 366 TGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYI-SGGSNVYPREIEEKLLTHPAVS 443
|
....*
gi 1309054211 455 ESLVV 459
Cdd:PRK07470 444 EVAVL 448
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
33-537 |
1.28e-31 |
|
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: 126.82 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEIL-NKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVI 111
Cdd:cd05958 9 REWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VSEKLhyklSASlldslklvismdtleviksageqdytlnelprpEDLASIIYTSGTSGASKGVMLTHRNL--VTQNYMA 189
Cdd:cd05958 89 CAHAL----TAS---------------------------------DDICILAFTSGTTGAPKATMHFHRDPlaSADRYAV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 190 NKLLPifRE-DVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGApTPSLLLPALTQVRPTIMLSVPlivekiyknkirp 268
Cdd:cd05958 132 NVLRL--REdDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA-TPDLLLSAIARYKPTVLFTAP------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 269 mftktwiTQFlysisfirRALhkVAGKKLCQTFGGNLRFFGIGGSKLDGVV-EKFLADAGFPYGIGYGLTETSPLLAGAI 347
Cdd:cd05958 196 -------TAY--------RAM--LAHPDAAGPDLSSLRKCVSAGEALPAALhRAWKEATGIPIIDGIGSTEMFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 348 PGKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPnvmSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYI 422
Cdd:cd05958 259 PGDARPGATGKPVPGYEAKVVDDEGNpvpdgTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRH 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 423 KGRKDNMMVGAnGENIYPEEIEATINEHDMVLESLVVNTKGKLVAMVHFNYEQIEKLHTfneEAEVNMTQRVEEVKKELM 502
Cdd:cd05958 336 QGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI---PGPVLARELQDHAKAHIA 411
|
490 500 510
....*....|....*....|....*....|....*
gi 1309054211 503 EYvnsrvnKSSKILEILEQsspFEKTATQKIKRYL 537
Cdd:cd05958 412 PY------KYPRAIEFVTE---LPRTATGKLQRFA 437
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
152-459 |
1.69e-31 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 128.92 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 152 ELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYL- 230
Cdd:PRK07529 208 RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAt 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 231 -HGAPTPSLL--LPALTQ-VRPTIMLSVPLIVEKIYKnkiRPmftktwitqflysisfirralhkVAGKKLcqtfgGNLR 306
Cdd:PRK07529 288 pQGYRGPGVIanFWKIVErYRINFLSGVPTVYAALLQ---VP-----------------------VDGHDI-----SSLR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 307 FFGIGGSKLD-GVVEKFLADAGFPYGIGYGLTETSPLLAGAIP-GKVKWQSTGPKLPDIEMKILNPNHK----------K 374
Cdd:PRK07529 337 YALCGAAPLPvEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgrylrdcavdE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 375 IGEIVVKGPNVMSGYYkDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMV 453
Cdd:PRK07529 417 VGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRaKDLIIRG--GHNIDPAAIEEALLRHPAV 493
|
....*.
gi 1309054211 454 LESLVV 459
Cdd:PRK07529 494 ALAAAV 499
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
30-425 |
2.03e-31 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 129.70 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 30 INKEKLTYRE--FGDSVehLTEILnKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVvvPILPDFTAfEIVNVI---EH 104
Cdd:PRK06814 654 PVNGPLTYRKllTGAFV--LGRKL-KKNTPPGENVGVMLPNANGAAVTFFALQSAGRV--PAMINFSA-GIANILsacKA 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 105 SESSVVIVS---------EKLHYKLSASL----LDSLKLVIS-MDTLE-VIKSAGEQDYTLNelPRPEDLASIIYTSGTS 169
Cdd:PRK06814 728 AQVKTVLTSrafiekarlGPLIEALEFGIriiyLEDVRAQIGlADKIKgLLAGRFPLVYFCN--RDPDDPAVILFTSGSE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 170 GASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQvVYLHgaPTPslllpaltqvrpt 249
Cdd:PRK06814 806 GTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVK-VFLY--PSP------------- 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 250 imLSVPLIVEKIYKNKIRPMF-TKTWITQF--------LYSisfirralhkvagkklcqtfggnLRFFGIGGSKLDGVVE 320
Cdd:PRK06814 870 --LHYRIIPELIYDTNATILFgTDTFLNGYaryahpydFRS-----------------------LRYVFAGAEKVKEETR 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 321 KFLADAgfpYGI----GYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILN-PNHKKIGEIVVKGPNVMSGYYK---- 391
Cdd:PRK06814 925 QTWMEK---FGIrileGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPvPGIDEGGRLFVRGPNVMLGYLRaenp 1001
|
410 420 430
....*....|....*....|....*....|....*..
gi 1309054211 392 ---DPvttascfTEDGWFRTKDLGYIDKNGNLYIKGR 425
Cdd:PRK06814 1002 gvlEP-------PADGWYDTGDIVTIDEEGFITIKGR 1031
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
35-535 |
3.32e-31 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 126.82 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLS---ASLLDSLKLVISMDTLEVI-KSAGEQDYTLNEL----------PR-PEDLASIIYTSGTSGASKGVMLTH 179
Cdd:TIGR03098 106 ERLDLLHpalPGCHDLRTLIIVGDPAHASeGHPGEEPASWPKLlalgdadpphPViDSDMAAILYTSGSTGRPKGVVLSH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 180 RNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSlGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPLIVE 259
Cdd:TIGR03098 186 RNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFN-QLTTAFYVGATVV-LHDYLLPRDVLKALEKHGITGLAAVPPLWA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 260 KIYKNKIRPMFTKTwitqflysisfirralhkvagkklcqtfggnLRFFGIGGSKLDGVV----EKFLADAG-FPYgigY 334
Cdd:TIGR03098 264 QLAQLDWPESAAPS-------------------------------LRYLTNSGGAMPRATlsrlRSFLPNARlFLM---Y 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 335 GLTET--SPLLAgaiPGKV--KWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGW 405
Cdd:TIGR03098 310 GLTEAfrSTYLP---PEEVdrRPDSIGKAIPNAEVLVLREDGSecapgEEGELVHRGALVAMGYWNDPEKTAERFRPLPP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 406 FRTK-----------DLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKGKLVAmvhfnyE 474
Cdd:TIGR03098 387 FPGElhlpelavwsgDTVRRDEEGFLYFVGRRDE-MIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLG------Q 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054211 475 QIEKLHTFNEEAEVNMTQRVEEVKKELMEYVNSRvnksskileILEQSSPFEKTATQKIKR 535
Cdd:TIGR03098 460 AIVLVVTPPGGEELDRAALLAECRARLPNYMVPA---------LIHVRQALPRNANGKIDR 511
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
12-469 |
6.44e-31 |
|
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: 124.73 E-value: 6.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 12 DIYSRSLVDFSEQTAFSLiNKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILP 91
Cdd:cd17653 1 DAFERIAAAHPDAVAVES-LGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 92 DFTAFEIVNVIEHSESsvvivseklhyklsaslldslKLVISmdtleviksageqdytlneLPRPEDLASIIYTSGTSGA 171
Cdd:cd17653 80 KLPSARIQAILRTSGA---------------------TLLLT-------------------TDSPDDLAYIIFTSGSTGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 172 SKGVMLTHRNLVtqNYMAN-----KLLPIFREDVFLSIlplshAYECSLGLILP-LSRGAQVV-------------YLHG 232
Cdd:cd17653 120 PKGVMVPHRGVL--NYVSQpparlDVGPGSRVAQVLSI-----AFDACIGEIFStLCNGGTLVladpsdpfahvarTVDA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 233 AP-TPSLLlpalTQVRPTIMLSVPLIVekiyknkirpmftktwitqflysisfirralhkVAG----KKLCQTFGGNLRF 307
Cdd:cd17653 193 LMsTPSIL----STLSPQDFPNLKTIF---------------------------------LGGeavpPSLLDRWSPGRRL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 308 FGiggskldgvvekfladagfpygiGYGLTETS--PLLAGAIPGKvkwQST-GPKLPDIEMKILNPNHK-----KIGEIV 379
Cdd:cd17653 236 YN-----------------------AYGPTECTisSTMTELLPGQ---PVTiGKPIPNSTCYILDADLQpvpegVVGEIC 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 380 VKGPNVMSGYYKDPVTTASCFTEDGW------FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMV 453
Cdd:cd17653 290 ISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDN-QVKVRGFRINLEEIEEVVLQSQPE 368
|
490
....*....|....*....
gi 1309054211 454 LES---LVVNtkGKLVAMV 469
Cdd:cd17653 369 VTQaaaIVVN--GRLVAFV 385
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
154-425 |
1.01e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 127.35 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 154 PRPEDLASIIYTSGTSGASKGVMLTHRNLvtqnyMAN-----KLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVV 228
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMLSHHNI-----LSNieqisDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 229 YlHGAPTPSLLLPALT-QVRPTIMLSVPLIVeKIY--KNKIRP-MFTktwitqflysisfirralhkvagkklcqtfggN 304
Cdd:PRK08633 854 Y-HPDPTDALGIAKLVaKHRATILLGTPTFL-RLYlrNKKLHPlMFA--------------------------------S 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 305 LRFFGIGGSKL-----DGVVEKFladagfpyGI----GYGLTETSPLLAGAIP----GKVKWQ------STGPKLPDIEM 365
Cdd:PRK08633 900 LRLVVAGAEKLkpevaDAFEEKF--------GIrileGYGATETSPVASVNLPdvlaADFKRQtgskegSVGMPLPGVAV 971
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309054211 366 KILNPNHKKI------GEIVVKGPNVMSGYYKDPVTTASCFTE---DGWFRTKDLGYIDKNGNLYIKGR 425
Cdd:PRK08633 972 RIVDPETFEElppgedGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
8-537 |
1.06e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 125.86 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 8 LSLADIYSRSLVDFSEQTAF-SLINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVV 86
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFvEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 87 VPILPDFTAFEIVNVIEHSESSVvIVSEKLHYKLSASL------LDSLKLVISMDTLEVIKSAGE-QDYTLNELPRPEDL 159
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKL-IVTNDTNYGKVKGLglpvivLGEEKIEGAVNWKELLEAADRaGDTSDNEEILQTDL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 160 ASIIYTSGTSGASKGVMLTHRNLVTQnyMANKLLPIFREDV----FLSILPLSHAYECSlGLILPLSRGAQVVYLHGAPT 235
Cdd:PLN02330 187 CALPFSSGTTGISKGVMLTHRNLVAN--LCSSLFSVGPEMIgqvvTLGLIPFFHIYGIT-GICCATLRNKGKVVVMSRFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 236 PSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPMFTKTWItqflySISFIRRALHKVAgKKLCQTFGgnlrffgiggSKL 315
Cdd:PLN02330 264 LRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKL-----KLQAIMTAAAPLA-PELLTAFE----------AKF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 316 DGV-VEKfladagfpygiGYGLTETSPL-LAGAIPGK----VKWQSTGPKLPDIEMKILNPNHKKI------GEIVVKGP 383
Cdd:PLN02330 328 PGVqVQE-----------AYGLTEHSCItLTHGDPEKghgiAKKNSVGFILPNLEVKFIDPDTGRSlpkntpGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 384 NVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV---- 459
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKE-LIKYKGFQVAPAELEAILLTHPSVEDAAVVplpd 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309054211 460 NTKGKLVAmvhfnyeqieklhtfneeAEVNMTQRVEEVKKELMEYVNSRVNKSSKIlEILEQSSPFEKTATQKIKRYL 537
Cdd:PLN02330 476 EEAGEIPA------------------ACVVINPKAKESEEDILNFVAANVAHYKKV-RVVQFVDSIPKSLSGKIMRRL 534
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
9-453 |
1.42e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 125.70 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFSLINKeKLTYREFGDSVEHLTEILNKH-GVKKGEKVAIlgnNMPN---WAVSYFAITTSSR 84
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAFSNLGV-TLSYAELERHSAAFAAYLQQHtDLVPGDRIAV---QMPNvlqYPIAVFGALRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 85 VVVPILPDFTAFEIVNVIEHSESSVVI--------VSEKLH-----YKLSASLLDSL----------------KLVISMD 135
Cdd:PRK12492 101 IVVNTNPLYTAREMRHQFKDSGARALVylnmfgklVQEVLPdtgieYLIEAKMGDLLpaakgwlvntvvdkvkKMVPAYH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 136 TLEVI--KSAGEQDYTLNELPRP---EDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLL--------PIFRE--DV 200
Cdd:PRK12492 181 LPQAVpfKQALRQGRGLSLKPVPvglDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLsqlgpdgqPLMKEgqEV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 201 FLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKNkirPMFTKtwitqfly 280
Cdd:PRK12492 261 MIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDH---PGFKD-------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 281 sISFirralhkvagkklcqtfgGNLRFFGIGGSKL-DGVVEKFLADAGFPYGIGYGLTETSPLlAGAIP--GKVKWQSTG 357
Cdd:PRK12492 330 -LDF------------------SALKLTNSGGTALvKATAERWEQLTGCTIVEGYGLTETSPV-ASTNPygELARLGTVG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 358 PKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVg 432
Cdd:PRK12492 390 IPVPGTALKVIDDDGNELplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLII- 468
|
490 500
....*....|....*....|.
gi 1309054211 433 ANGENIYPEEIEATINEHDMV 453
Cdd:PRK12492 469 VSGFNVYPNEIEDVVMAHPKV 489
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
33-459 |
4.76e-30 |
|
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: 125.35 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDF----TAFeivnVIEHSESS 108
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYpaerLAY----MLEDAGAR 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 109 VVIVSEKLHYKLSASLLDslklVISMDTLEViksAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVtqNYM 188
Cdd:COG1020 576 LVLTQSALAARLPELGVP----VLALDALAL---AAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV--NLL 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 189 A--NKLLPIFREDVFLSILPLSH---AYEcslgLILPLSRGAQVVYL--HGAPTPSLLLPALTQVRPTIMLSVPliveki 261
Cdd:COG1020 647 AwmQRRYGLGPGDRVLQFASLSFdasVWE----IFGALLSGATLVLAppEARRDPAALAELLARHRVTVLNLTP------ 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 262 yknkirpmftktwitqflysiSFIRRALHkvAGKKLCQTfggnLRFFGIGGSKLDG-VVEKFLadAGFPYGI---GYGLT 337
Cdd:COG1020 717 ---------------------SLLRALLD--AAPEALPS----LRLVLVGGEALPPeLVRRWR--ARLPGARlvnLYGPT 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 338 ETS-----------PLLAGAIP-GKvkwqstgPkLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCF 400
Cdd:COG1020 768 ETTvdstyyevtppDADGGSVPiGR-------P-IANTRVYVLDAHLQpvpvgVPGELYIGGAGLARGYLNRPELTAERF 839
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 401 -----TEDG--WFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:COG1020 840 vadpfGFPGarLYRTGDLARWLPDGNLEFLGRADD-QVKIRGFRIELGEIEAALLQHPGVREAVVV 904
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
32-451 |
1.49e-28 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 119.72 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 32 KEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPiLPDFTAF--------EIVNVIE 103
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVP-LPLPMGFggresyiaQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 104 HSESSVVIVSEKLHyKLSASLLDSLKLVISMdTLEVIKSAGEQDYTLNElPRPEDLASIIYTSGTSGASKGVMLTHRNLv 183
Cdd:PRK09192 126 SAQPAAIITPDELL-PWVNEATHGNPLLHVL-SHAWFKALPEADVALPR-PTPDDIAYLQYSSGSTRFPRGVIITHRAL- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 184 tqnyMANkLLPIFRE-------DVFLSILPLSHayecSLGLI----LPLSRGAQVVYLhgaPT------PSLLLPALTQV 246
Cdd:PRK09192 202 ----MAN-LRAISHDglkvrpgDRCVSWLPFYH----DMGLVgfllTPVATQLSVDYL---PTrdfarrPLQWLDLISRN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 247 RPTIMlsvplivekiyknkirpmftktwitqflYSISFirralhkvaGKKLC------QTFGG----NLRFFGIGGS--- 313
Cdd:PRK09192 270 RGTIS----------------------------YSPPF---------GYELCarrvnsKDLAEldlsCWRVAGIGADmir 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 314 --KLDGVVEKFlADAGF---PYGIGYGLTET------SPLLAG----------------AIPGKVKWQST------GPKL 360
Cdd:PRK09192 313 pdVLHQFAEAF-APAGFddkAFMPSYGLAEAtlavsfSPLGSGivveevdrdrleyqgkAVAPGAETRRVrtfvncGKAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 361 PDIEMKILNPN-----HKKIGEIVVKGPNVMSGYYKDPVTTASCfTEDGWFRTKDLGYIdKNGNLYIKGRKDNMMVgANG 435
Cdd:PRK09192 392 PGHEIEIRNEAgmplpERVVGHICVRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYL-LDGYLYITGRAKDLII-ING 468
|
490
....*....|....*.
gi 1309054211 436 ENIYPEEIEATINEHD 451
Cdd:PRK09192 469 RNIWPQDIEWIAEQEP 484
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
156-453 |
2.40e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 116.04 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 156 PEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYlhgaPT 235
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVL----AG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 236 PSlllpalTQVRPTIMLSVPLIVEKiyknkirpmftktWITQFLYSISFIRRALHKVAGKKLCqtfgGNLRFFGIGGSKL 315
Cdd:cd05944 77 PA------GYRNPGLFDNFWKLVER-------------YRITSLSTVPTVYAALLQVPVNADI----SSLRFAMSGAAPL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 316 D-GVVEKFLADAGFPYGIGYGLTETSPLLAGAIP-GKVKWQSTGPKLP--DIEMKILNPNHK--------KIGEIVVKGP 383
Cdd:cd05944 134 PvELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPyaRVRIKVLDGVGRllrdcapdEVGEICVAGP 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054211 384 NVMSGYYKDpVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMV 453
Cdd:cd05944 214 GVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRaKDLIIRG--GHNIDPALIEEALLRHPAV 281
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
7-459 |
4.95e-28 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 117.55 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 7 GLSLADIYSRSLVDFSEQTAfsLINKEK-LTYREFGDSVEHLTEILNKHGVKKGEKVAIlgnNMPNWA---VSYFAITts 82
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIA--VVDGERrLSYAELDRRADRLAAGLLALGLRPGDRVVV---QLPNVAefvIVFFALF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 83 sRV-VVPI--LPDFTAFEIVNVIEHSESSVVIVSEKL----HYKLSASLLDSLklvismDTLEVIKSAGEQD--YTLNEL 153
Cdd:COG1021 97 -RAgAIPVfaLPAHRRAEISHFAEQSEAVAYIIPDRHrgfdYRALARELQAEV------PSLRHVLVVGDAGefTSLDAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 154 -----------PRPEDLASIIYTSGTSGASKGVMLTHRNLVtqnYMANKLLPIFR---EDVFLSILPLSHAYE-CSLGLI 218
Cdd:COG1021 170 laapadlseprPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL---YSVRASAEICGldaDTVYLAALPAAHNFPlSSPGVL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 219 LPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPLIVekiyknkirpmftKTWitqfLYSISFIRRALhkvagkklc 298
Cdd:COG1021 247 GVLYAGGTVV-LAPDPSPDTAFPLIERERVTVTALVPPLA-------------LLW----LDAAERSRYDL--------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 299 qtfgGNLRFFGIGGSKLD-----GVVEKFLADAGFPYGIGYGLTETSPLLAgaiPGKVKWQSTG-PKLPDIEMKILNPNH 372
Cdd:COG1021 300 ----SSLRVLQVGGAKLSpelarRVRPALGCTLQQVFGMAEGLVNYTRLDD---PEEVILTTQGrPISPDDEVRIVDEDG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 373 K-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDnmMVGANGENIYPEEIEAT 446
Cdd:COG1021 373 NpvppgEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRaKD--QINRGGEKIAAEEVENL 450
|
490
....*....|...
gi 1309054211 447 INEHDMVLESLVV 459
Cdd:COG1021 451 LLAHPAVHDAAVV 463
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-536 |
6.18e-28 |
|
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: 116.38 E-value: 6.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEklhyklsaslldslklvismdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLVTQN---YMA 189
Cdd:cd05971 85 DG-----------------------------------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLpgvQFP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 190 NKLLPIfREDVFLSilPLSHAYECSLGlilplsrgaqvvylhgaptpSLLLPALtqvrptiMLSVPLIVEKIYKNKIRPM 269
Cdd:cd05971 124 FNLFPR-DGDLYWT--PADWAWIGGLL--------------------DVLLPSL-------YFGVPVLAHRMTKFDPKAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 FT--KTW--ITQFL--YSISFIRRAlhkvagKKLCQTFGGNLRFFGIGGSKLDGVVEKFLADA-GFPYGIGYGLTETSPL 342
Cdd:cd05971 174 LDlmSRYgvTTAFLppTALKMMRQQ------GEQLKHAQVKLRAIATGGESLGEELLGWAREQfGVEVNEFYGQTECNLV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 343 LAG-AIPGKVKWQSTGPKLPDIEMKILNPN-----HKKIGEIVVKGPN--VMSGYYKDPVTTASCFTEDgWFRTKDLGYI 414
Cdd:cd05971 248 IGNcSALFPIKPGSMGKPIPGHRVAIVDDNgtplpPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 415 DKNGNLYIKGRKDNMMVGAnGENIYPEEIEATINEHDMVLESLVVN----TKGKLV-AMVHFNyeqieklhtfneEAEVN 489
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVVGipdpIRGEIVkAFVVLN------------PGETP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1309054211 490 MtqrvEEVKKELMEYVNSRVNKSSKILEIlEQSSPFEKTATQKIKRY 536
Cdd:cd05971 394 S----DALAREIQELVKTRLAAHEYPREI-EFVNELPRTATGKIRRR 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
6-458 |
1.13e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 116.52 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 6 LGLSLADIYSRSLVDFSEQTAFSLI-NKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSR 84
Cdd:PRK05852 14 FGPRIADLVEVAATRLPEAPALVVTaDRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 85 VVVPILPDFTAFEIVNVIEHSESSVVIV--------SEKLHYKLSASLLDSLKLVISMDTLEVIKSAGEQDYTLNELP-- 154
Cdd:PRK05852 94 VVVPLDPALPIAEQRVRSQAAGARVVLIdadgphdrAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPeg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 155 -RPEDlASIIYTSGTSGASKGVMLTHRNLVTQNY---MANKLLPifrEDVFLSILPLSHAYECSLGLILPLSRGAQVvyl 230
Cdd:PRK05852 174 lRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRaiiTGYRLSP---RDATVAVMPLYHGHGLIAALLATLASGGAV--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 231 hgaptpslLLPALTQVRPtimlsvpliveKIYKNKIRPMfTKTWITqflySISFIRRALHKVAGKKLCQTFGGNLRFFGI 310
Cdd:PRK05852 247 --------LLPARGRFSA-----------HTFWDDIKAV-GATWYT----AVPTIHQILLERAATEPSGRKPAALRFIRS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 311 GGSKLDGVVEKFLADA-GFPYGIGYGLTETSPLLA-------------GAIPGKVKwQSTGPklpdiEMKILNPNHK--- 373
Cdd:PRK05852 303 CSAPLTAETAQALQTEfAAPVVCAFGMTEATHQVTttqiegigqtenpVVSTGLVG-RSTGA-----QIRIVGSDGLplp 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 374 --KIGEIVVKGPNVMSGYYKDPVTTASCFTeDGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHD 451
Cdd:PRK05852 377 agAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKE-LINRGGEKISPERVEGVLASHP 454
|
....*..
gi 1309054211 452 MVLESLV 458
Cdd:PRK05852 455 NVMEAAV 461
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
21-482 |
3.54e-27 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 114.20 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 21 FSEQTAFSL---INKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFE 97
Cdd:PRK09029 12 WAQVRPQAIalrLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 98 IvnviehsessvvivsEKL--HYKLS-ASLLDSLKLVISMDTLEVIKSAGEQDYTlnelPRPEDLASIIYTSGTSGASKG 174
Cdd:PRK09029 92 L---------------EELlpSLTLDfALVLEGENTFSALTSLHLQLVEGAHAVA----WQPQRLATMTLTSGSTGLPKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 175 VMLTHrnlvtQNYMAN-----KLLPIFREDVFLSILPLSHAyecS-LGLILP-LSRGAQVVYLHGAPtpslLLPALTQVr 247
Cdd:PRK09029 153 AVHTA-----QAHLASaegvlSLMPFTAQDSWLLSLPLFHV---SgQGIVWRwLYAGATLVVRDKQP----LEQALAGC- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 248 pTIMLSVPLIVEKIYKNKIRPMFTKtwitQFLysisfirralhkvagkklcqtfggnlrffgIGGSkldgVVEKFLADAG 327
Cdd:PRK09029 220 -THASLVPTQLWRLLDNRSEPLSLK----AVL------------------------------LGGA----AIPVELTEQA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 328 FPYGI----GYGLTET-SPLLAGAIPGKvkwQSTGPKLPDIEMKILNpnhkkiGEIVVKGPNVMSGYYKD----PVTTas 398
Cdd:PRK09029 261 EQQGIrcwcGYGLTEMaSTVCAKRADGL---AGVGSPLPGREVKLVD------GEIWLRGASLALGYWRQgqlvPLVN-- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 399 cftEDGWFRTKDLGYIDkNGNLYIKGRKDNMMVGAnGENIYPEEIEATINEHDMVLESLVVNTKGKL-----VAMVHFNY 473
Cdd:PRK09029 330 ---DEGWFATRDRGEWQ-NGELTILGRLDNLFFSG-GEGIQPEEIERVINQHPLVQQVFVVPVADAEfgqrpVAVVESDS 404
|
490
....*....|
gi 1309054211 474 EQ-IEKLHTF 482
Cdd:PRK09029 405 EAaVVNLAEW 414
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
34-425 |
3.76e-27 |
|
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: 115.22 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILP-------DFTafEIVNVIEHSE 106
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPayslmsqDLA--KLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 107 SSVVIVS--EKLHYKLSASLLDSLKLVISMDTLEVIKSAG-----EQDYTLnELPR------PEDLASIIYTSGTSGASK 173
Cdd:cd05921 103 PGLVFAQdaAPFARALAAIFPLGTPLVVSRNAVAGRGAISfaelaATPPTA-AVDAafaavgPDTVAKFLFTSGSTGLPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 174 GVMLTHRNLVTQNYMANKLLPIFRED--VFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLL---LPALTQVRP 248
Cdd:cd05921 182 AVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDGKPMPGGFeetLRNLREISP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 249 TIMLSVPlivekiyknkirpmftKTWitqflysiSFIRRALHKVAGkkLCQTFGGNLRFFGIGGSKL-----DGVVEKFL 323
Cdd:cd05921 262 TVYFNVP----------------AGW--------EMLVAALEKDEA--LRRRFFKRLKLMFYAGAGLsqdvwDRLQALAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 324 ADAG--FPYGIGYGLTETSPLLAG-----AIPGKVkwqstGPKLPDIEMKiLNPNHKKIgEIVVKGPNVMSGYYKDPVTT 396
Cdd:cd05921 316 ATVGerIPMMAGLGATETAPTATFthwptERSGLI-----GLPAPGTELK-LVPSGGKY-EVRVKGPNVTPGYWRQPELT 388
|
410 420 430
....*....|....*....|....*....|...
gi 1309054211 397 ASCFTEDGWFRTKDLGYI----DKNGNLYIKGR 425
Cdd:cd05921 389 AQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGR 421
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-449 |
6.33e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 116.42 E-value: 6.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 6 LGLSLADIYSRSLVDFSEQTAFSLINKEK-----LTYREFGDSVEHLTEILNKHGVKkGEKVAILGNNMPNWAVSYFAIT 80
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPgegvvLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 81 TSSRVVVPILPDFTAFE-----IVNVIEHSESSVVIVSEKLH---YKLSASLLDSLKLVISMDTLEVIKSAGEQDYTLne 152
Cdd:PRK05691 86 YAGVIAVPAYPPESARRhhqerLLSIIADAEPRLLLTVADLRdslLQMEELAAANAPELLCVDTLDPALAEAWQEPAL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 153 lpRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFR--EDVFLSILPLSHayecSLGLIlplsrgaqvvyl 230
Cdd:PRK05691 164 --QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLnpDDVIVSWLPLYH----DMGLI------------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 231 hgaptPSLLLPALTQVrPTIMLSVPLIVEkiyknkiRPMFTKTWITQFLYSIS----FIRRALH-KVAGKKLCQTFGGNL 305
Cdd:PRK05691 226 -----GGLLQPIFSGV-PCVLMSPAYFLE-------RPLRWLEAISEYGGTISggpdFAYRLCSeRVSESALERLDLSRW 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 306 R--FFG---IGGSKLDGVVEKFlADAGF---PYGIGYGLTETSPLLAGAIPGK------VKWQS---------TGPKL-- 360
Cdd:PRK05691 293 RvaYSGsepIRQDSLERFAEKF-AACGFdpdSFFASYGLAEATLFVSGGRRGQgipaleLDAEAlarnraepgTGSVLms 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 361 -----PDIEMKILNPNH------KKIGEIVVKGPNVMSGYYKDPVTTASCFTE-DG--WFRTKDLGYIdKNGNLYIKGRK 426
Cdd:PRK05691 372 cgrsqPGHAVLIVDPQSlevlgdNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFL-RDGELFVTGRL 450
|
490 500
....*....|....*....|...
gi 1309054211 427 DNMMVgANGENIYPEEIEATINE 449
Cdd:PRK05691 451 KDMLI-VRGHNLYPQDIEKTVER 472
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
35-467 |
8.95e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 114.07 E-value: 8.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLSASLLDSlklvISMDTLEVIKSAGEQDYTLNELPRP--------------------------EDLASIIYT-SG 167
Cdd:PRK06164 116 GFKGIDFAAILAA----VPPDALPPLRAIAVVDDAADATPAPapgarvqlfalpdpappaaageraadPDAGALLFTtSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 168 TSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSlGLILPLSRGAQVVYLHGAPTPslllPALTQVR 247
Cdd:PRK06164 192 TTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFS-TLLGALAGGAPLVCEPVFDAA----RTARALR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 248 ptimlsvplivekiyknkirpmftKTWITQFLYSISFIRRaLHKVAGKKlcQTFGgNLRFFGIGG--SKLDGVVEKfLAD 325
Cdd:PRK06164 267 ------------------------RHRVTHTFGNDEMLRR-ILDTAGER--ADFP-SARLFGFASfaPALGELAAL-ARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 326 AGFP-YGIgYGLTETSPLLAG---AIPGKVKWQSTG-PKLPDIEMKILNPN------HKKIGEIVVKGPNVMSGYYKDPV 394
Cdd:PRK06164 318 RGVPlTGL-YGSSEVQALVALqpaTDPVSVRIEGGGrPASPEARVRARDPQdgallpDGESGEIEIRAPSLMRGYLDNPD 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 395 TTASCFTEDGWFRTKDLGYIDKNGNLYIKGRK-DNMMVGanGENIYPEEIEATINEHDMVLESLVV--NTKGKLVA 467
Cdd:PRK06164 397 ATARALTDDGYFRTGDLGYTRGDGQFVYQTRMgDSLRLG--GFLVNPAEIEHALEALPGVAAAQVVgaTRDGKTVP 470
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
154-459 |
1.20e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.78 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 154 PRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLhGA 233
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHT-GR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 234 PTPSLLLPALtQVRPTIMLSVPLIvekiyknkirpmftktWitqflysisfirralHKVAGK-KLCQTFGGnLRFFGIGG 312
Cdd:PRK07787 204 PTPEAYAQAL-SEGGTLYFGVPTV----------------W---------------SRIAADpEAARALRG-ARLLVSGS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 313 SKL-DGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNH-------KKIGEIVVKGPN 384
Cdd:PRK07787 251 AALpVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGgpvphdgETVGELQVRGPT 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309054211 385 VMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07787 331 LFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVV 405
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
156-444 |
1.62e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 113.17 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 156 PEDLASIIYTSGTSGASKGVMLTHRNLVTQNY-MANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYlhgap 234
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGNLYANAEaMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVK----- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 235 tpslllpaltqVRPTIMLSVPLI-VEKIYKNKIrpmfTKTWITQFLYSIsFIRRaLHKVAGKKlcqTFG-GNLRFFGIGG 312
Cdd:PRK07768 226 -----------VTPMDFLRDPLLwAELISKYRG----TMTAAPNFAYAL-LARR-LRRQAKPG---AFDlSSLRFALNGA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 313 SKLD-GVVEKFlADAGFPYGIG-------YGLTET------SPLLAG----------------AIP---GKVKWQST-GP 358
Cdd:PRK07768 286 EPIDpADVEDL-LDAGARFGLRpeailpaYGMAEAtlavsfSPCGAGlvvdevdadllaalrrAVPatkGNTRRLATlGP 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 359 KLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYykdpvTTASCFT----EDGWFRTKDLGYIDKNGNLYIKGRKDNM 429
Cdd:PRK07768 365 PLPGLEVRVVDEDGQvlpprGVGVIELRGESVTPGY-----LTMDGFIpaqdADGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
330
....*....|....*
gi 1309054211 430 MVGAnGENIYPEEIE 444
Cdd:PRK07768 440 IIMA-GRNIYPTDIE 453
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
34-467 |
1.93e-26 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 112.60 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSE-SSVVIV 112
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEmTAAVIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSASLLDSLKLVISMDTLEVIKSAGeqDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQN-YMANK 191
Cdd:cd05923 108 VDAQVMDAIFQSGVRVLALSDLVGLGEPESAG--PLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVlFMSTQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 192 LLPIF-REDVFLSILPLSHAYECSLGLILPLSRGAQVVylhgapTPSLLLPALTqvrptimlsvpliVEKIYKNKIRPMF 270
Cdd:cd05923 186 AGLRHgRHNVVLGLMPLYHVIGFFAVLVAALALDGTYV------VVEEFDPADA-------------LKLIEQERVTSLF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 271 -TKTWITQFLYSISFirralhkvAGKKLcqtfgGNLRFFGIGGSKL-DGVVEKFLADAGFPYGIGYGLTETSPLL----- 343
Cdd:cd05923 247 aTPTHLDALAAAAEF--------AGLKL-----SSLRHVTFAGATMpDAVLERVNQHLPGEKVNIYGTTEAMNSLymrda 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 344 ---AGAIPG---KVKWQSTGPK----LPDIEMkilnpnhkkiGEIVVK--GPNVMSGYYKDPVTTASCFtEDGWFRTKDL 411
Cdd:cd05923 314 rtgTEMRPGffsEVRIVRIGGSpdeaLANGEE----------GELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDV 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 412 GYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVVNTK----GKLVA 467
Cdd:cd05923 383 GYVDPSGDVRILGRVDDMII-SGGENIHPSEIERVLSRHPGVTEVVVIGVAderwGQSVT 441
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
157-449 |
2.55e-26 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 109.66 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 157 EDLASIIYTSGTSGASKGVMLTHRNLVTQ-NYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPT 235
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVpDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 236 PSLLlPALTQVRPTIMLSVPLIVEKI---YKNKIrpmftktwitqflysisfirralhkvagkKLCQTfggnLRFFGIGG 312
Cdd:cd17635 81 KSLF-KILTTNAVTTTCLVPTLLSKLvseLKSAN-----------------------------ATVPS----LRLIGYGG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 313 SK-LDGVVEKFLADAGFPYGIGYGLTETSPLLAgaIP---GKVKWQSTGPKLPDIEMKILNPNHKKI-----GEIVVKGP 383
Cdd:cd17635 127 SRaIAADVRFIEATGLTNTAQVYGLSETGTALC--LPtddDSIEINAVGRPYPGVDVYLAATDGIAGpsasfGTIWIKSP 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309054211 384 NVMSGYYKDPVTTASCFTeDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINE 449
Cdd:cd17635 205 ANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRsSESINCG--GVKIAPDEVERIAEG 268
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
50-535 |
4.50e-26 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 111.86 E-value: 4.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 50 ILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPD------------------FTAFEIVNVIEHSESSVVI 111
Cdd:PLN02574 83 LYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSsslgeikkrvvdcsvglaFTSPENVEKLSPLGVPVIG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VSEKLHYKLSASLLDSLKLVISMDTLEVIKSAGEQDytlnelprpeDLASIIYTSGTSGASKGVMLTHRNLVTQ-----N 186
Cdd:PLN02574 163 VPENYDFDSKRIEFPKFYELIKEDFDFVPKPVIKQD----------DVAAIMYSSGTTGASKGVVLTHRNLIAMvelfvR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 187 YMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTpSLLLPALTQVRPTIMLSVPlivekiyknki 266
Cdd:PLN02574 233 FEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDA-SDMVKVIDRFKVTHFPVVP----------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 267 rPMFTktwitqflysisfirrALHKVAgKKLCQTFGGNLRFFGIGGSKLDG-VVEKFLAdaGFPYG---IGYGLTETSPL 342
Cdd:PLN02574 301 -PILM----------------ALTKKA-KGVCGEVLKSLKQVSCGAAPLSGkFIQDFVQ--TLPHVdfiQGYGMTESTAV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 343 LAGAIPGK--VKWQSTGPKLPDIEMKI--------LNPNHKkiGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLG 412
Cdd:PLN02574 361 GTRGFNTEklSKYSSVGLLAPNMQAKVvdwstgclLPPGNC--GELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 413 YIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKGKLVAMVHFNYEQIEKLHTFNEEAevnmtq 492
Cdd:PLN02574 439 YFDEDGYLYIVDRLKE-IIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA------ 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1309054211 493 rveevkkeLMEYVNSRVNKSSKILE-ILEQSSPfeKTATQKIKR 535
Cdd:PLN02574 512 --------VINYVAKQVAPYKKVRKvVFVQSIP--KSPAGKILR 545
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
33-504 |
6.89e-26 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 111.14 E-value: 6.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPIlpDF-TAFE-IVNVIEHSESSVV 110
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV--DVsSPAErIEMIIEVAKPSLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 IVSEKLhyklsaSLLDSLKLVISMDTLEVIKSAGEqDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVT-QNYMa 189
Cdd:PRK04813 104 IATEEL------PLEILGIPVITLDELKDIFATGN-PYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSfTNWM- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 190 NKLLPIFREDVFLSILPLShaYECSLGLILP-LSRGAQVVYLHGAPT--PSLLLPALTQVRPTIMLSVPlivekiyknki 266
Cdd:PRK04813 176 LEDFALPEGPQFLNQAPYS--FDLSVMDLYPtLASGGTLVALPKDMTanFKQLFETLPQLPINVWVSTP----------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 267 rpmftktwitqflysiSFIRRALhkvagkkLCQTFGG----NLRFFGIGGSKLDGVVEKFLADAgFPYGI---GYGLTE- 338
Cdd:PRK04813 243 ----------------SFADMCL-------LDPSFNEehlpNLTHFLFCGEELPHKTAKKLLER-FPSATiynTYGPTEa 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 339 ---------TSPLLAGAIP---GKVKwqstgpklPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCF- 400
Cdd:PRK04813 299 tvavtsieiTDEMLDQYKRlpiGYAK--------PDSPLLIIDEEGTKLpdgeqGEIVISGPSVSKGYLNNPEKTAEAFf 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 401 TEDGW--FRTKDLGYIDkNGNLYIKGRKDnMMVGANGENIYPEEIEATINEHDMVLESLVV--NTKGK---LVAMVhfny 473
Cdd:PRK04813 371 TFDGQpaYHTGDAGYLE-DGLLFYQGRID-FQIKLNGYRIELEEIEQNLRQSSYVESAVVVpyNKDHKvqyLIAYV---- 444
|
490 500 510
....*....|....*....|....*....|..
gi 1309054211 474 eqIEKLHTFNEEAEvnMTQRV-EEVKKELMEY 504
Cdd:PRK04813 445 --VPKEEDFEREFE--LTKAIkKELKERLMEY 472
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
33-459 |
8.35e-26 |
|
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: 110.09 E-value: 8.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 seklhyklsaslldslklvismdtleviksageqdytlnelpRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKL 192
Cdd:cd17643 91 ------------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 193 LPIFREDVFLsiLPLSHAYECSLGLI-LPLSRGAQVVYL--HGAPTPSLLLPALTQVRPTIMLSVPlivekiyknkirpm 269
Cdd:cd17643 129 FGFNEDDVWT--LFHSYAFDFSVWEIwGALLHGGRLVVVpyEVARSPEDFARLLRDEGVTVLNQTP-------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 ftktwiTQFLYSISFIRRALHKVAgkklcqtfggNLRFFGIGGSKLD-GVVEKFLADAGFPYGI---GYGLTETS----- 340
Cdd:cd17643 193 ------SAFYQLVEAADRDGRDPL----------ALRYVIFGGEALEaAMLRPWAGRFGLDRPQlvnMYGITETTvhvtf 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 341 -PLLAGAIPGKVKwQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFTEDGW-------FR 407
Cdd:cd17643 257 rPLDAADLPAAAA-SPIGRPLPGLRVYVLDADGRPvppgvVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYR 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1309054211 408 TKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17643 336 TGDLARRLPDGELEYLGRADE-QVKIRGFRIELGEIEAALATHPSVRDAAVI 386
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
7-446 |
1.34e-25 |
|
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: 110.62 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 7 GLSLADIYSRSLVDFSEQTAFS-------------------LINKEKLTYREFGDSVEHLTEILN-KHGVKKGEKVAILG 66
Cdd:cd17632 21 GLRLAQIIATVMTGYADRPALGqratelvtdpatgrttlrlLPRFETITYAELWERVGAVAAAHDpEQPVRPGDFVAVLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 67 NNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVS-EKLHYKLSASL--------------------- 124
Cdd:cd17632 101 FTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSaEHLDLAVEAVLeggtpprlvvfdhrpevdahr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 125 --LDS----LKLVISMDTLEVIKSAGEQDYTLNELPRPED----LASIIYTSGTSGASKGVMLTHRnLVTQNYMANKLLP 194
Cdd:cd17632 181 aaLESarerLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPdddpLALLIYTSGSTGTPKGAMYTER-LVATFWLKVSSIQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 195 IFRED--VFLSILPLSHAYEcSLGLILPLSRGAqVVYLHGAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPMftK 272
Cdd:cd17632 260 DIRPPasITLNFMPMSHIAG-RISLYGTLARGG-TAYFAAASDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAEL--D 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 273 TWITQflysiSFIRRALHKVAGKKLCQ-TFGGNLrFFGIGGS-----KLDGVVEKFLadaGFPYGIGYGLTET-SPLLAG 345
Cdd:cd17632 336 RRSVA-----GADAETLAERVKAELRErVLGGRL-LAAVCGSaplsaEMKAFMESLL---DLDLHDGYGSTEAgAVILDG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 346 AIpgkVKWQSTGPKLPDI-EMKILNPN--HKKiGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKD---------LGY 413
Cdd:cd17632 407 VI---VRPPVLDYKLVDVpELGYFRTDrpHPR-GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDvmaelgpdrLVY 482
|
490 500 510
....*....|....*....|....*....|...
gi 1309054211 414 IDkngnlyikgRKDNMMVGANGENIYPEEIEAT 446
Cdd:cd17632 483 VD---------RRNNVLKLSQGEFVTVARLEAV 506
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
33-459 |
1.61e-25 |
|
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: 109.72 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd17655 21 QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLhyklsASLLDSLKLVISMDTlEVIKSAGEQDytLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKL 192
Cdd:cd17655 101 QSHL-----QPPIAFIGLIDLLDE-DTIYHEESEN--LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 193 LPIFREDVFLSILPLShaYECSLGLILP--LSRGAQVVYLHGAPTP-SLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPM 269
Cdd:cd17655 173 IYQGEHLRVALFASIS--FDASVTEIFAslLSGNTLYIVRKETVLDgQALTQYIRQNRITIIDLTPAHLKLLDAADDSEG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 FT-KTWITQflysisfiRRALHKVAGKKLCQTFGGNLRFFGIggskldgvvekfladagfpygigYGLTETS--PLLAGA 346
Cdd:cd17655 251 LSlKHLIVG--------GEALSTELAKKIIELFGTNPTITNA-----------------------YGPTETTvdASIYQY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 347 IPGKVKWQST--GPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFTEDGW------FRTKDLGY 413
Cdd:cd17655 300 EPETDQQVSVpiGKPLGNTRIYILDQYGRPQpvgvaGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLAR 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1309054211 414 IDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17655 380 WLPDGNIEFLGRIDH-QVKIRGYRIELGEIEARLLQHPDIKEAVVI 424
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
34-460 |
1.80e-25 |
|
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: 109.67 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVS 113
Cdd:cd17646 23 TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 114 EKLHYKLSASLLDslklvismDTLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVtqnymaNKLL 193
Cdd:cd17646 103 ADLAARLPAGGDV--------ALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIV------NRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 194 ------PIFREDVFLSILPLS---HAYEcslgLILPLSRGAQVVYL-HGAPT-PSLLLPALTQVRPTIMLSVPlivekiy 262
Cdd:cd17646 169 wmqdeyPLGPGDRVLQKTPLSfdvSVWE----LFWPLVAGARLVVArPGGHRdPAYLAALIREHGVTTCHFVP------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 263 knkirpmftktwitqflysiSFIRRALhKVAGKKLCQTfggnLRFFGIGGSKLDG-VVEKFLADAGFPYGIGYGLTETS- 340
Cdd:cd17646 238 --------------------SMLRVFL-AEPAAGSCAS----LRRVFCSGEALPPeLAARFLALPGAELHNLYGPTEAAi 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 341 -----PLLAGAIPGKVkwqSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFTEDgWF---- 406
Cdd:cd17646 293 dvthwPVRGPAETPSV---PIGRPVPNTRLYVLDDALRPvpvgvPGELYLGGVQLARGYLGRPALTAERFVPD-PFgpgs 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1309054211 407 ---RTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVN 460
Cdd:cd17646 369 rmyRTGDLARWRPDGALEFLGRSDD-QVKIRGFRVEPGEIEAALAAHPAVTHAVVVA 424
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
7-459 |
2.40e-25 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 108.95 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 7 GLSLADIYSRSLVDFSEQTAfsLINKE-KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRV 85
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIA--VVDGDrRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 86 VVPILPDFTAFEIVNVIEHSESSVVIVSEKlhyklsASLLDSLKLVISMdtleviksageqdytLNELPrpeDLASIIYT 165
Cdd:cd05920 92 PVLALPSHRRSELSAFCAHAEAVAYIVPDR------HAGFDHRALAREL---------------AESIP---EVALFLLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 166 SGTSGASKGVMLTHRNLVtqnYMAN---KLLPIFREDVFLSILPLSHAYE-CSLGLILPLSRGAQVVyLHGAPTPSLLLP 241
Cdd:cd05920 148 GGTTGTPKLIPRTHNDYA---YNVRasaEVCGLDQDTVYLAVLPAAHNFPlACPGVLGTLLAGGRVV-LAPDPSPDAAFP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 242 ALTQVRPTIMLSVPLIVekiyknkirpmftKTWitqfLYSISFIRRALhkvagkklcqtfgGNLRFFGIGGSKLDGVVEK 321
Cdd:cd05920 224 LIEREGVTVTALVPALV-------------SLW----LDAAASRRADL-------------SSLRLLQVGGARLSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 322 FLADAGFP-----YGIGYGLTETSPLlagAIPGKVKWQSTG-PKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYY 390
Cdd:cd05920 274 RVPPVLGCtlqqvFGMAEGLLNYTRL---DDPDEVIIHTQGrPMSPDDEIRVVDEEGNpvppgEEGELLTRGPYTIRGYY 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 391 KDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05920 351 RAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRiKDQINRG--GEKIAAEEVENLLLRHPAVHDAAVV 418
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
164-459 |
2.46e-25 |
|
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: 106.72 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 164 YTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYecSL-GLILPLSRGAQVVyLHGAPTPSLLLPA 242
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSL--FLyGAISALYLGGTFI-GQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 243 LTQVRPTIMLSVPLIVEKIYK-----NKIRPMFTktwitqflysisfirralhkvagkklcqtfggnlrffgiGGSKLDG 317
Cdd:cd17633 84 INQYNATVIYLVPTMLQALARtlepeSKIKSIFS---------------------------------------SGQKLFE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 318 VVEKFLAdAGFPYGI---GYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKKIGEIVVKGPNVMSGYykdpv 394
Cdd:cd17633 125 STKKKLK-NIFPKANlieFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGY----- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309054211 395 TTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17633 199 VRGGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMII-IGGINIFPTEIESVLKAIPGIEEAIVV 262
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
33-459 |
4.34e-25 |
|
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: 108.13 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAfEIVNVIEHSESSVVIV 112
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPA-ARREAILADAGARLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSASLLDSLKLVISMDTLEVIKSAGEQDytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLvtqnymANKL 192
Cdd:cd12114 90 TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVA--------PDDLAYVIFTSGSTGTPKGVMISHRAA------LNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 193 LPIFR------EDVFLSILPLSH---AYEcslgLILPLSRGAQVVYL--HGAPTPSLLLPALTQVRPTIMLSVP----LI 257
Cdd:cd12114 156 LDINRrfavgpDDRVLALSSLSFdlsVYD----IFGALSAGATLVLPdeARRRDPAHWAELIERHGVTLWNSVPalleML 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 258 VEKIYKNKIRP------MFTKTWITQFLysisfiRRALHKVAgkklcqtfgGNLRFFGIGGskldgvvekflADAGFPYG 331
Cdd:cd12114 232 LDVLEAAQALLpslrlvLLSGDWIPLDL------PARLRALA---------PDARLISLGG-----------ATEASIWS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 332 IGYGLTETSPLLAgAIPgkvkwqsTGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFTEDG-- 404
Cdd:cd12114 286 IYHPIDEVPPDWR-SIP-------YGRPLANQRYRVLDPRGRDCpdwvpGELWIGGRGVALGYLGDPELTAARFVTHPdg 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1309054211 405 --WFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd12114 358 erLYRTGDLGRYRPDGTLEFLGRRDG-QVKVRGYRIELGEIEAALQAHPGVARAVVV 413
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
9-465 |
4.51e-25 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 108.69 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 9 SLADIYSRSLVDFSEQTAFSlINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVP 88
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLV-FGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 89 ILPDFTAFEIVNVIEHSESSVVIVSEKLHYKLSASLLDSLKL--VISMDtlEVIKSAGEQDYTLNELP-----------R 155
Cdd:PRK06155 101 INTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLpaVWLLD--APASVSVPAGWSTAPLPpldapapaaavQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 156 PEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLgLILPLSRGAQVVYL----- 230
Cdd:PRK06155 179 PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNA-FFQALLAGATYVLEprfsa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 231 ---------HGApTPSLLLPALTqvrpTIMLSVPLIVEKiyknkirpmftktwitqflySISFIRRALhkvagkklcqtf 301
Cdd:PRK06155 258 sgfwpavrrHGA-TVTYLLGAMV----SILLSQPARESD--------------------RAHRVRVAL------------ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 302 ggnlrffGIGGSKldGVVEKFLADAGFPYGIGYGLTETSPLLAGAIPGKvKWQSTGPKLPDIEMKILNPNHKKI-----G 376
Cdd:PRK06155 301 -------GPGVPA--ALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELpdgepG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 377 EIVVKGPN---VMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVgaNGENIYPEEIEATINEHDM 452
Cdd:PRK06155 371 ELLLRADEpfaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRiKDAIRR--RGENISSFEVEQVLLSHPA 447
|
490
....*....|...
gi 1309054211 453 VLESLVVNTKGKL 465
Cdd:PRK06155 448 VAAAAVFPVPSEL 460
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
34-410 |
1.65e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 107.66 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILP-------DFTAFEivNVIEHSE 106
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPayslvsqDFGKLR--HVLELLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 107 SSVVIVSEKLHYK--LSASLLDSLKLVI-----------SMDTLEVIKSAGEQDYTLNELpRPEDLASIIYTSGTSGASK 173
Cdd:PRK08180 147 PGLVFADDGAAFAraLAAVVPADVEVVAvrgavpgraatPFAALLATPPTAAVDAAHAAV-GPDTIAKFLFTSGSTGLPK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 174 GVMLTHRNLVTQNYMANKLLPIFRED--VFLSILPLSHAYECSLGLILPLSRGAQVvYL-HGAPTPSLL---LPALTQVR 247
Cdd:PRK08180 226 AVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGTL-YIdDGKPTPGGFdetLRNLREIS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 248 PTIMLSVPlivekiyknkirpmftKTWitqflysiSFIRRALHKVAGkkLCQTFGGNLRFFGIGGS--------KLDGVV 319
Cdd:PRK08180 305 PTVYFNVP----------------KGW--------EMLVPALERDAA--LRRRFFSRLKLLFYAGAalsqdvwdRLDRVA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 320 EK-------FLAdagfpygiGYGLTETSPLLAgaipgKVKWQSTGP-----KLPDIEMKiLNPNHKKIgEIVVKGPNVMS 387
Cdd:PRK08180 359 EAtcgerirMMT--------GLGMTETAPSAT-----FTTGPLSRAgniglPAPGCEVK-LVPVGGKL-EVRVKGPNVTP 423
|
410 420
....*....|....*....|...
gi 1309054211 388 GYYKDPVTTASCFTEDGWFRTKD 410
Cdd:PRK08180 424 GYWRAPELTAEAFDEEGYYRSGD 446
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
33-505 |
2.52e-24 |
|
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: 106.02 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSasllDSLKLVISMDTLEVIKSAGEQDYTLNElprpEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKL 192
Cdd:cd17656 92 QRHLKSKLS----FNKSTILLEDPSISQEDTSNIDYINNS----DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 193 LPIFREDVFLSILPLSHAYeCSLGLILPLSRGAQvvylhgaptpslllpaLTQVRPTIMLSVPLIVEKIYKNKIRPMFTK 272
Cdd:cd17656 164 TNINFSDKVLQFATCSFDV-CYQEIFSTLLSGGT----------------LYIIREETKRDVEQLFDLVKRHNIEVVFLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 273 TWITQFLYSIsfirralhkvagKKLCQTFGGNLRFFGIGGSKLdgVVEKFLADAGFPYGIG----YGLTETSPLLAGAIP 348
Cdd:cd17656 227 VAFLKFIFSE------------REFINRFPTCVKHIITAGEQL--VITNEFKEMLHEHNVHlhnhYGPSETHVVTTYTIN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 349 GKVKWqstgPKLPDI-------EMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGW------FRTKD 410
Cdd:cd17656 293 PEAEI----PELPPIgkpisntWIYILDQEQQlqpqgIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 411 LGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV---NTKGKLVAMVHFNYEQieklhtfneeaE 487
Cdd:cd17656 369 LARYLPDGNIEFLGRADH-QVKIRGYRIELGEIEAQLLNHPGVSEAVVLdkaDDKGEKYLCAYFVMEQ-----------E 436
|
490
....*....|....*...
gi 1309054211 488 VNMTQRVEEVKKELMEYV 505
Cdd:cd17656 437 LNISQLREYLAKQLPEYM 454
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
33-417 |
3.80e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 106.28 E-value: 3.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILP-------DFTA----FEIVnv 101
Cdd:PRK12582 79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPayslmshDHAKlkhlFDLV-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 102 iehsESSVVIVSEKLHYK--LSASLLDSLKLV-----------ISMDTLEVIKSAGEQDYTLNELpRPEDLASIIYTSGT 168
Cdd:PRK12582 157 ----KPRVVFAQSGAPFAraLAALDLLDVTVVhvtgpgegiasIAFADLAATPPTAAVAAAIAAI-TPDTVAKYLFTSGS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 169 SGASKGVMLTHRNLVTQNYMANKLLPIFRED---VFLSILPLSHayeCSLGLIL--PLSRGAQVVYLH-GAPTPSLL--- 239
Cdd:PRK12582 232 TGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNH---TMGGNANfnGLLWGGGTLYIDdGKPLPGMFeet 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 240 LPALTQVRPTIMLSVPlivekiyknkirpmftktwitqflysISFIRRALHKVAGKKLCQTFGGNLRFFGIGGSKL-DGV 318
Cdd:PRK12582 309 IRNLREISPTVYGNVP--------------------------AGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLsDDL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 319 VEKFLADA------GFPYGIGYGLTETSPllagaIPGKVKWQS-----TGPKLPDIEMKILnPNHKKIgEIVVKGPNVMS 387
Cdd:PRK12582 363 YERMQALAvrttghRIPFYTGYGATETAP-----TTTGTHWDTervglIGLPLPGVELKLA-PVGDKY-EVRVKGPNVTP 435
|
410 420 430
....*....|....*....|....*....|.
gi 1309054211 388 GYYKDPVTTASCFTEDGWFRTKDLG-YIDKN 417
Cdd:PRK12582 436 GYHKDPELTAAAFDEEGFYRLGDAArFVDPD 466
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
33-469 |
7.66e-24 |
|
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: 104.59 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLhyklSASLLDSLKLVISMDTLEviksaGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVT----QNYm 188
Cdd:cd12117 101 DRSL----AGRAGGLEVAVVIDEALD-----AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRlvknTNY- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 189 anklLPIFREDVFLSILPLS---HAYEcslgLILPLSRGAQvvyLHGAPTPSLLLP-ALTQvrptimlsvpLIVEkiykN 264
Cdd:cd12117 171 ----VTLGPDDRVLQTSPLAfdaSTFE----IWGALLNGAR---LVLAPKGTLLDPdALGA----------LIAE----E 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 265 KIrpmfTKTWITQFLYsisfirRALHKVAGkklcQTFGGnLRFFGIGGSKLD-GVVEKFLAD-AGFPYGIGYGLTETS-- 340
Cdd:cd12117 226 GV----TVLWLTAALF------NQLADEDP----ECFAG-LRELLTGGEVVSpPHVRRVLAAcPGLRLVNGYGPTENTtf 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 341 ---------PLLAGAIPgkvkwqsTGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFTEDGW- 405
Cdd:cd12117 291 ttshvvtelDEVAGSIP-------IGRPIANTRVYVLDEDGRPVppgvpGELYVGGDGLALGYLNRPALTAERFVADPFg 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 406 -----FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV-----NTKGKLVAMV 469
Cdd:cd12117 364 pgerlYRTGDLARWLPDGRLEFLGRIDD-QVKIRGFRIELGEIEAALRAHPGVREAVVVvredaGGDKRLVAYV 436
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
31-459 |
1.16e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 104.09 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 31 NKEKLTYREFGDSVEHLTEILNKHGvKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVV 110
Cdd:PRK07638 23 NDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 IVSEKLHYKLSAS-----LLDSLKLVIS--MDTLEVIKSAGEQDYTLNelprpedlasiiYTSGTSGASKGVMLTHRNLV 183
Cdd:PRK07638 102 VTERYKLNDLPDEegrviEIDEWKRMIEkyLPTYAPIENVQNAPFYMG------------FTSGSTGKPKAFLRAQQSWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 184 TQNYMANKLLPIFREDVFLSILPLSHayecSL---GLILPLSRGaQVVYLHGAPTPSLLLPALTQVRPTIMLSVPLIVEK 260
Cdd:PRK07638 170 HSFDCNVHDFHMKREDSVLIAGTLVH----SLflyGAISTLYVG-QTVHLMRKFIPNQVLDKLETENISVMYTVPTMLES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 261 IYKnkirpmfTKTWITQFLYSISfiRRALHKVAGKKLCQTFGGNLRFFGI-GGSKLDGVVekFLADAGFpygigygltet 339
Cdd:PRK07638 245 LYK-------ENRVIENKMKIIS--SGAKWEAEAKEKIKNIFPYAKLYEFyGASELSFVT--ALVDEES----------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 340 spllagaipgKVKWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTAScFTEDGWFRTKDLGYI 414
Cdd:PRK07638 303 ----------ERRPNSVGRPFHNVQVRICNEAGEEvqkgeIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYE 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1309054211 415 DKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07638 372 DEEGFIYIVGREKNMIL-FGGINIFPEEIESVLHEHPAVDEIVVI 415
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
33-469 |
1.87e-23 |
|
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: 103.17 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd12115 23 ESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 seklhyklsaslldslklvismdtleviksageqdytlnelpRPEDLASIIYTSGTSGASKGVMLTHRNLVT--QNYMAN 190
Cdd:cd12115 103 ------------------------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAflQWAAAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 kllpiFREDVFLSILP-------LShAYEcslgLILPLSRGAQVVYLHGAPTPsLLLPALTQVrpTIMLSVP-LIVEKIY 262
Cdd:cd12115 141 -----FSAEELAGVLAstsicfdLS-VFE----LFGPLATGGKVVLADNVLAL-PDLPAAAEV--TLINTVPsAAAELLR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 263 KNKIRPmftktwitqflySISFIrralhKVAGKKLCQTFGGNLRffgiggsKLDGVVEKF-LadagfpygigYGLTETSP 341
Cdd:cd12115 208 HDALPA------------SVRVV-----NLAGEPLPRDLVQRLY-------ARLQVERVVnL----------YGPSEDTT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 342 LLAGAI--PGKVKWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFTEDGW------FRT 408
Cdd:cd12115 254 YSTVAPvpPGASGEVSIGRPLANTQAYVLDRALQPvplgvPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRT 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 409 KDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKGK-----LVAMV 469
Cdd:cd12115 334 GDLVRWRPDGLLEFLGRADN-QVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAagerrLVAYI 398
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
32-504 |
2.21e-23 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 103.95 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 32 KEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVI 111
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VseklHYKLSASLLDSLKLVISMDT---LEVI----------KSAGEQDY---TLNELPRPEDLASII------------ 163
Cdd:PLN03102 117 V----DRSFEPLAREVLHLLSSEDSnlnLPVIfiheidfpkrPSSEELDYeclIQRGEPTPSLVARMFriqdehdpisln 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 164 YTSGTSGASKGVMLTHRN--LVTQNYMANKLLPIFreDVFLSILPLSHayeCSlGLILPLS---RGAQVVYLHGAPTPsl 238
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTC--PVYLWTLPMFH---CN-GWTFTWGtaaRGGTSVCMRHVTAP-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 239 llpaltqvrptimlsvpliveKIYKN----KIRPMFTKTWITQFLysisfirralhkVAGKKLCQTFGGNLRFFGIGGSK 314
Cdd:PLN03102 265 ---------------------EIYKNiemhNVTHMCCVPTVFNIL------------LKGNSLDLSPRSGPVHVLTGGSP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 315 LDGVVEKFLADAGFPYGIGYGLTE-TSPLLAgaipgkVKWQSTGPKLPD---IEMK--------------ILNP------ 370
Cdd:PLN03102 312 PPAALVKKVQRLGFQVMHAYGLTEaTGPVLF------CEWQDEWNRLPEnqqMELKarqgvsilgladvdVKNKetqesv 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 371 --NHKKIGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATIN 448
Cdd:PLN03102 386 prDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIII-SGGENISSVEVENVLY 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309054211 449 EHDMVLESLVvntkgklVAMVHFNYEQIEKLHTFNEEAEVNMTQRVEEV---KKELMEY 504
Cdd:PLN03102 464 KYPKVLETAV-------VAMPHPTWGETPCAFVVLEKGETTKEDRVDKLvtrERDLIEY 515
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
36-459 |
2.46e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 103.49 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEK 115
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 116 LH--YKLSASLLDSLK-LVISMDTLEVIKSA--GEQDYT--LNE--------LPRPE-DLASIIYTSGTSGASKGVMLTH 179
Cdd:PRK08162 125 FAevAREALALLPGPKpLVIDVDDPEYPGGRfiGALDYEafLASgdpdfawtLPADEwDAIALNYTSGTTGNPKGVVYHH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 180 RNlVTQNYMANKL---LPifREDVFLSILPLSHayeC----------------------SLGLILPLSRGAQVVYLHGAP 234
Cdd:PRK08162 205 RG-AYLNALSNILawgMP--KHPVYLWTLPMFH---CngwcfpwtvaaragtnvclrkvDPKLIFDLIREHGVTHYCGAP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 235 -TPSLLLPALTQVRPTIMlsvplivekiyknkirpmftktwitqflysisfirralHKVagkklcqtfggnlRFFGIGGS 313
Cdd:PRK08162 279 iVLSALINAPAEWRAGID--------------------------------------HPV-------------HAMVAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 314 KLDGVVEKfLADAGFPYGIGYGLTET-SPLLAGAipgkvkWQSTGPKLPDIE-----------------MKILNPN---- 371
Cdd:PRK08162 308 PPAAVIAK-MEEIGFDLTHVYGLTETyGPATVCA------WQPEWDALPLDEraqlkarqgvryplqegVTVLDPDtmqp 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 372 ----HKKIGEIVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEAT 446
Cdd:PRK08162 381 vpadGETIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRsKDIIISG--GENISSIEVEDV 457
|
490
....*....|...
gi 1309054211 447 INEHDMVLESLVV 459
Cdd:PRK08162 458 LYRHPAVLVAAVV 470
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
29-464 |
3.88e-23 |
|
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: 102.16 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 29 LINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESS 108
Cdd:cd17650 7 SDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 109 VVIVseklhyklsaslldslklvismdtleviksageqdytlnelpRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNY- 187
Cdd:cd17650 87 LLLT------------------------------------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHa 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 188 ---------MANKLLPI--FREDVFLSILPLShayECSLGLILPLSRGAQVvylhgapTPSLLLPALTQVRPTIMLSVPL 256
Cdd:cd17650 125 wrreyeldsFPVRLLQMasFSFDVFAGDFARS---LLNGGTLVICPDEVKL-------DPAALYDLILKSRITLMESTPA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 257 ----IVEKIYKNKIRPMFTKTWITqflysisfirralhkvagkklcqtfggnlrffgigGSklDGVVEKFLADAGFPYGI 332
Cdd:cd17650 195 lirpVMAYVYRNGLDLSAMRLLIV-----------------------------------GS--DGCKAQDFKTLAARFGQ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 333 G------YGLTETS------PLLAGAIPGkVKWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVT 395
Cdd:cd17650 238 GmriinsYGVTEATidstyyEEGRDPLGD-SANVPIGRPLPNTAMYVLDERLQPqpvgvAGELYIGGAGVARGYLNRPEL 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309054211 396 TASCFTEDGW------FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKGK 464
Cdd:cd17650 317 TAERFVENPFapgermYRTGDLARWRADGNVELLGRVDH-QVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK 390
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
8-459 |
1.23e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 101.78 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 8 LSLADI--YSRSLVDFSEQTAFSLINKEKLTYREFGDSVEHLTEIL-NKHGVKKGEKVAILgnnMPNWAV---SYFAITT 81
Cdd:PRK05620 10 LSLTRIleYGSTVHGDTTVTTWGGAEQEQTTFAAIGARAAALAHALhDELGITGDQRVGSM---MYNCAEhleVLFAVAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 82 SSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEKLHYKLSASL--LDSLKLVI-----SMDTLEVIKSAGEQDYTLNEL- 153
Cdd:PRK05620 87 MGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILkeCPCVRAVVfigpsDADSAAAHMPEGIKVYSYEALl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 154 -------PRPE----DLASIIYTSGTSGASKGVMLTHRNLVTQ--NYMANKLLPIFREDVFLSILPLSHAyecsLGLILP 220
Cdd:PRK05620 167 dgrstvyDWPEldetTAAAICYSTGTTGAPKGVVYSHRSLYLQslSLRTTDSLAVTHGESFLCCVPIYHV----LSWGVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 221 LS---RGAQVVYlhgaPTPSLLLPALTQVRPTIMLSVPLIVEKIyknkirpmftktWITQFLYSIsfirralhKVAGKKL 297
Cdd:PRK05620 243 LAafmSGTPLVF----PGPDLSAPTLAKIIATAMPRVAHGVPTL------------WIQLMVHYL--------KNPPERM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 298 cqtfggNLRFFGIGGSKLDGVVEKFLADAgfpYGIG----YGLTETSPLLAGAIP-----GKVKWQ---STGPKLPDIEM 365
Cdd:PRK05620 299 ------SLQEIYVGGSAVPPILIKAWEER---YGVDvvhvWGMTETSPVGTVARPpsgvsGEARWAyrvSQGRFPASLEY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 366 KILNPNH------KKIGEIVVKGPNVMSGYYKDPVTT----------------ASCFTEDGWFRTKDLGYIDKNGNLYIK 423
Cdd:PRK05620 370 RIVNDGQvmestdRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIH 449
|
490 500 510
....*....|....*....|....*....|....*.
gi 1309054211 424 GRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK05620 450 DRARD-VIRSGGEWIYSAQLENYIMAAPEVVECAVI 484
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
35-459 |
1.90e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 100.77 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMpNWAVsyFAITTSSRVVVPIL---PDFTAFEIVNVIEHSESSVVI 111
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNH-RGFV--LALYAAGKVGARIIllnTGFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VSEKLHYKLSASLLDSLKLVISMDTLEVIKSAGEQDYTLNEL---------PRPEDLASI-IYTSGTSGASKGVMLTH-- 179
Cdd:PRK07788 152 YDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLiagsstaplPKPPKPGGIvILTSGTTGTPKGAPRPEps 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 180 -----RNLVTQnymanklLPIFREDVFLSILPLSHA--YECsLGLILPLsrGAQVVyLHGAPTPSLLLPALTQVRPTIML 252
Cdd:PRK07788 232 plaplAGLLSR-------VPFRAGETTLLPAPMFHAtgWAH-LTLAMAL--GSTVV-LRRRFDPEATLEDIAKHKATALV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 253 SVPlivekiyknkirpmftkTWITQFLysisfirRALHKVAGKKLCQtfggNLRFFGIGGSKLDG-VVEKFLADAGfP-- 329
Cdd:PRK07788 301 VVP-----------------VMLSRIL-------DLGPEVLAKYDTS----SLKIIFVSGSALSPeLATRALEAFG-Pvl 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 330 YGIgYGLTETSpllAGAI---------PGKVkwqstGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYykdpVT 395
Cdd:PRK07788 352 YNL-YGSTEVA---FATIatpedlaeaPGTV-----GRPPKGVTVKILDENGNEVprgvvGRIFVGNGFPFEGY----TD 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 396 TASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07788 419 GRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIV-SGGENVFPAEVEDLLAGHPDVVEAAVI 481
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
31-469 |
2.97e-22 |
|
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: 99.36 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 31 NKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAfeivnviehsessvv 110
Cdd:cd17649 9 GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPA--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 ivsEKLHYKLSASlldSLKLVISMDtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMAN 190
Cdd:cd17649 74 ---ERLRYMLEDS---GAGLLLTHH--------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 KLLPIFREDVFLSILPLSH--AYECslgLILPLSRGAQVVylhgAPTPSLLLPALTQVRPTIMLSVPLIVekiyknkirp 268
Cdd:cd17649 128 ERYGLTPGDRELQFASFNFdgAHEQ---LLPPLICGACVV----LRPDELWASADELAEMVRELGVTVLD---------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 269 mFTKTWITQFLysisfiRRALHKVAGKKlcqtfgGNLRFFGIGGSKLDGvveKFLADAgFPYGI----GYGLTET--SPL 342
Cdd:cd17649 191 -LPPAYLQQLA------EEADRTGDGRP------PSLRLYIFGGEALSP---ELLRRW-LKAPVrlfnAYGPTEAtvTPL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 343 LAGAIPG-KVKWQST--GPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDG-------WFR 407
Cdd:cd17649 254 VWKCEAGaARAGASMpiGRPLGGRSAYILDADLNpvpvgVTGELYIGGEGLARGYLGRPELTAERFVPDPfgapgsrLYR 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 408 TKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV----NTKGKLVAMV 469
Cdd:cd17649 334 TGDLARWRDDGVIEYLGRVDH-QVKIRGFRIELGEIEAALLEHPGVREAAVValdgAGGKQLVAYV 398
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
34-450 |
6.79e-22 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 99.12 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKHgvkKGEKVAILgnnMPNWA---VSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVV 110
Cdd:PRK06334 45 KLSYNQVRKAVIALATKVSKY---PDQHIGIM---MPASAgayIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 IVSEKLHYKLSASLLDSLK---LVISMDT-------LEVIKSAGEQDYTLNELPR--------PEDLASIIYTSGTSGAS 172
Cdd:PRK06334 119 LTSKQLMQHLAQTHGEDAEypfSLIYMEEvrkelsfWEKCRIGIYMSIPFEWLMRwfgvsdkdPEDVAVILFTSGTEKLP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 173 KGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGAPTPSLLLPALTQVRPTIML 252
Cdd:PRK06334 199 KGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 253 SVPLIVEKIYKnkirpmftktwitqflysisfirralhkvAGKKLCQTFGgNLRFFGIGGSKL-DGVVEKFLADagFPYG 331
Cdd:PRK06334 279 STPVFFDYILK-----------------------------TAKKQESCLP-SLRFVVIGGDAFkDSLYQEALKT--FPHI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 332 I---GYGLTETSPLLAGAIPGKVKWQS-TGPKLPDIEMKILNPNHK------KIGEIVVKGPNVMSGYY-KDPVTTASCF 400
Cdd:PRK06334 327 QlrqGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIVSEETKvpvssgETGLVLTRGTSLFSGYLgEDFGQGFVEL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1309054211 401 TEDGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEH 450
Cdd:PRK06334 407 GGETWYVTGDLGYVDRHGELFLKGRLSR-FVKIGAEMVSLEALESILMEG 455
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
26-464 |
1.28e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 98.43 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 26 AFSLINKEkLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITtssRV-VVPILPDfTAFEIVNV--- 101
Cdd:PRK09274 34 DGKLAYDE-LSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALF---KAgAVPVLVD-PGMGIKNLkqc 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 102 IEHSESSVVIVSEKLHYklsASLL-----DSLKLVI-----------SMDTLEVIKSAGEqdYTLNELPrPEDLASIIYT 165
Cdd:PRK09274 109 LAEAQPDAFIGIPKAHL---ARRLfgwgkPSVRRLVtvggrllwggtTLATLLRDGAAAP--FPMADLA-PDDMAAILFT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 166 SGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGL--ILP---LSRgaqvvylhgaptpslll 240
Cdd:PRK09274 183 SGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPALGMtsVIPdmdPTR----------------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 241 PAltQVRPTImlsvplIVEKIYKNKIRPMFTktwitqflySISFIRRALHkvAGKKLCQTFGgNLRFFGIGGSKLDG-VV 319
Cdd:PRK09274 246 PA--TVDPAK------LFAAIERYGVTNLFG---------SPALLERLGR--YGEANGIKLP-SLRRVISAGAPVPIaVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 320 EKFLA--DAGFPYGIGYGLTETSP--------LLAGAipgkvkWQST--------GPKLPDIEMKI-------------- 367
Cdd:PRK09274 306 ERFRAmlPPDAEILTPYGATEALPissiesreILFAT------RAATdngagicvGRPVDGVEVRIiaisdapipewdda 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 368 --LNPNhkKIGEIVVKGPNVMSGYYKDPVTTASCFTEDG----WFRTKDLGYIDKNGNLYIKGRKDNMMVGANGeNIYPE 441
Cdd:PRK09274 380 lrLATG--EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGG-TLYTI 456
|
490 500
....*....|....*....|....*
gi 1309054211 442 EIEATINEHDMVLES-LV-VNTKGK 464
Cdd:PRK09274 457 PCERIFNTHPGVKRSaLVgVGVPGA 481
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
25-459 |
2.17e-21 |
|
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: 97.41 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 25 TAFSLINKE-KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIE 103
Cdd:cd17651 10 DAPALVAEGrRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 104 HSESSVVIvsekLHYKLSASLLDSLKLVISMDTleviksagEQDYTLNELPR-----PEDLASIIYTSGTSGASKGVMLT 178
Cdd:cd17651 90 DAGPVLVL----THPALAGELAVELVAVTLLDQ--------PGAAAGADAEPdpaldADDLAYVIYTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 179 HRNLVTQNYMANKLLPIFREDVFLSILPLShaYECSLGLILP-LSRGAqvvylhgaptpslllpALTQVRPTIMLSVPLI 257
Cdd:cd17651 158 HRSLANLVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFStLCAGA----------------TLVLPPEEVRTDPPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 258 VEKIYKNKIRPMFTKTWITQFLysisfirrALHKVAGKklcqTFGGNLRFFGIGGSKL--DGVVEKFLADAGFPYGI-GY 334
Cdd:cd17651 220 AAWLDEQRISRVFLPTVALRAL--------AEHGRPLG----VRLAALRYLLTGGEQLvlTEDLREFCAGLPGLRLHnHY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 335 GLTETSPLLAGAIPGKVK-WQST---GPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFTEDGW 405
Cdd:cd17651 288 GPTETHVVTALSLPGDPAaWPAPppiGRPIDNTRVYVLDAALRPVppgvpGELYIGGAGLARGYLNRPELTAERFVPDPF 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 406 ------FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17651 368 vpgarmYRTGDLARWLPDGELEFLGRADD-QVKIRGFRIELGEIEAALARHPGVREAVVL 426
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
34-535 |
5.99e-21 |
|
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: 96.00 E-value: 5.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKH-GVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd05928 41 KWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLhyklsASLLDSL---------KLVIS-------MDTLEVIKSAGEQDYTLNElpRPEDLASIIYTSGTSGASKGVM 176
Cdd:cd05928 121 SDEL-----APEVDSVasecpslktKLLVSeksrdgwLNFKELLNEASTEHHCVET--GSQEPMAIYFTSGTTGSPKMAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 177 LTHRNLVTQNYM-ANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAqVVYLHGAPT--PSLLLPALTQVRPTIMLS 253
Cdd:cd05928 194 HSHSSLGLGLKVnGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGA-CVFVHHLPRfdPLVILKTLSSYPITTFCG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 254 VPLIvekiYKnkirpMFtktwITQFLYSISFirRALhkvagkKLCQTFGGNLrffgiggskLDGVVEKFLADAGFPYGIG 333
Cdd:cd05928 273 APTV----YR-----ML----VQQDLSSYKF--PSL------QHCVTGGEPL---------NPEVLEKWKAQTGLDIYEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 334 YGLTETSpLLAGAIPG-KVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVK-GPN----VMSGYYKDPVTTASCFTE 402
Cdd:cd05928 323 YGQTETG-LICANFKGmKIKPGSMGKASPPYDVQIIDDNGNvlppgTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 403 DGWFrTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVVNT----KGKLV-AMVHFNYEqie 477
Cdd:cd05928 402 DFYL-TGDRGIMDEDGYFWFMGRADDVIN-SSGYRIGPFEVESALIEHPAVVESAVVSSpdpiRGEVVkAFVVLAPQ--- 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309054211 478 klhtFNEEAEvnmtqrvEEVKKELMEYVNSrVNKSSKILEILEQSSPFEKTATQKIKR 535
Cdd:cd05928 477 ----FLSHDP-------EQLTKELQQHVKS-VTAPYKYPRKVEFVQELPKTVTGKIQR 522
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-459 |
1.35e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 94.45 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 154 PRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGL--ILP---LSRGAQVv 228
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLtsVIPdmdPTRPARA- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 229 ylhgapTPSLLLPALTQVRPTIMLSVPLIVEKIYKnkirpmftktWITQFLYSISFIRRALhkvagkklcqTFGGNLRFf 308
Cdd:cd05910 161 ------DPQKLVGAIRQYGVSIVFGSPALLERVAR----------YCAQHGITLPSLRRVL----------SAGAPVPI- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 309 giggskldGVVEKF--LADAGFPYGIGYGLTETSPLLA----------GAIPGKVKWQSTGPKLPDIEMKIL----NPNH 372
Cdd:cd05910 214 --------ALAARLrkMLSDEAEILTPYGATEALPVSSigsrellattTAATSGGAGTCVGRPIPGVRVRIIeiddEPIA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 373 K----------KIGEIVVKGPNVMSGYYKDPVTTASCFTEDG----WFRTKDLGYIDKNGNLYIKGRKDNMMVGANGeNI 438
Cdd:cd05910 286 EwddtlelprgEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGG-TL 364
|
330 340
....*....|....*....|.
gi 1309054211 439 YPEEIEATINEHDMVLESLVV 459
Cdd:cd05910 365 YTEPVERVFNTHPGVRRSALV 385
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
162-459 |
1.53e-20 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 92.75 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 162 IIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSH--AYECSLGLILPlsrGAQVVYLHGApTPSLL 239
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHigTLMFTLATFHA---GGTNVFVRRV-DAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 240 LPALTQVRPTIMLSVPLIVEKIYK-NKIRpmftktwitqfLYSISfirrALHKVAGKKlcqtfggnlrffgigGSKLDGV 318
Cdd:cd17636 81 LELIEAERCTHAFLLPPTIDQIVElNADG-----------LYDLS----SLRSSPAAP---------------EWNDMAT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 319 VEkflADAGFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDP 393
Cdd:cd17636 131 VD---TSPWGRKPGGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVpdgevGEIVARGPTVMAGYWNRP 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 394 VTTASCFTeDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGAnGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17636 208 EVNARRTR-GGWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAVI 271
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
155-425 |
1.64e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 95.55 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 155 RPEDLASIIYTSGTSGASKGVMLTHRNLvtqnyMAN----KLLPIFR-EDVFLSILPLSHAYECSLGLILPLSRGAQvVY 229
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSL-----LANveqiKTIADFTpNDRFMSALPLFHSFGLTVGLFTPLLTGAE-VF 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 230 LHGAPTPSLLLPALTQVRPTIMLsvplivekiyknkirpmF-TKTWI---TQFLYSISFIRralhkvagkklcqtfggnL 305
Cdd:PRK08043 437 LYPSPLHYRIVPELVYDRNCTVL-----------------FgTSTFLgnyARFANPYDFAR------------------L 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 306 RFFGIGGSKLDGVVEKFLADAgfpYGI----GYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKILN-PNHKKIGEIVV 380
Cdd:PRK08043 482 RYVVAGAEKLQESTKQLWQDK---FGLrileGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvPGIEQGGRLQL 558
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 381 KGPNVMSGYYK--DP-------VTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR 425
Cdd:PRK08043 559 KGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGR 612
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
156-438 |
1.72e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 95.56 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 156 PEDLASIIYTSGTSGASKGVMLTHRNLVtqnymaNKLLPIFREDVF--------LSILPLSHAYECSLGLILPLSRGAQV 227
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLY------NTVVPLCKHSIFkkynpkthLSYLPISHIYERVIAYLSFMLGGTIN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 228 VYlhgAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPM----FTKTWITQFLYSI----------SFIRRALHkvA 293
Cdd:PTZ00342 377 IW---SKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEInnlpPLKRFLVKKILSLrksnnnggfsKFLEGITH--I 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 294 GKKLCQTFGGNLRFFGIGGSKLDGVVEKFLADA-GFPYGIGYGLTETSpllaGAIPGK-VKWQST----GPKLPDIEMKI 367
Cdd:PTZ00342 452 SSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLlNVNYYQGYGLTETT----GPIFVQhADDNNTesigGPISPNTKYKV 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309054211 368 LNPNHKKI------GEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGANGENI 438
Cdd:PTZ00342 528 RTWETYKAtdtlpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYI 604
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
35-459 |
2.52e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 94.44 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLSASLLD---SLKLVISMDTLEVIKSAGEQDYTLNELPRPEDLAS--IIYTSGTSGASKGVmlthRNLVTQNYMA 189
Cdd:PRK13382 149 EFSATVDRALADcpqATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGrvILLTSGTTGTPKGA----RRSGPGGIGT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 190 NKLL----PIFREDVFLSILPLSHAYECSlGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVPLivekiyknk 265
Cdd:PRK13382 225 LKAIldrtPWRAEEPTVIVAPMFHAWGFS-QLVLAASLACTIV-TRRRFDPEATLDLIDRHRATGLAVVPV--------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 266 irpMFtktwitqflysisfiRRALHKVAgKKLCQTFGGNLRFFGIGGSKL-DGVVEKFLADAGFPYGIGYGLTETSpLLA 344
Cdd:PRK13382 294 ---MF---------------DRIMDLPA-EVRNRYSGRSLRFAAASGSRMrPDVVIAFMDQFGDVIYNNYNATEAG-MIA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 345 GAIPGKVKWQ-STGPKLPD-IEMKILNPNHK-----KIGEIVVKGPNVMSGYykDPVTTAScfTEDGWFRTKDLGYIDKN 417
Cdd:PRK13382 354 TATPADLRAApDTAGRPAEgTEIRILDQDFRevptgEVGTIFVRNDTQFDGY--TSGSTKD--FHDGFMASGDVGYLDEN 429
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1309054211 418 GNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK13382 430 GRLFVVGRDDEMIV-SGGENVYPIEVEKTLATHPDVAEAAVI 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-469 |
4.92e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.64 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 29 LINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESS 108
Cdd:PRK12316 4571 VFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAA 4650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 109 VVIVSEKLHYKL-SASLLDSLklviSMDTLEVIKSAGEQDYTLNElpRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNY 187
Cdd:PRK12316 4651 LLLTQSHLLQRLpIPDGLASL----ALDRDEDWEGFPAHDPAVRL--HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH 4724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 188 MANKLLPIFREDVFLSILPLShaYECS-LGLILPLSRGAQVVylhgAPTPSLLLPALTqvrptimlsvpliVEKIYKNKI 266
Cdd:PRK12316 4725 ATGERYELTPDDRVLQFMSFS--FDGShEGLYHPLINGASVV----IRDDSLWDPERL-------------YAEIHEHRV 4785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 267 RPM-FTKTWITQFLYSisfIRRALHKVAGKKLCqtFGGNlrffGIGGSKLDGVVEKFLADAGFPygiGYGLTETS--PLL 343
Cdd:PRK12316 4786 TVLvFPPVYLQQLAEH---AERDGEPPSLRVYC--FGGE----AVAQASYDLAWRALKPVYLFN---GYGPTETTvtVLL 4853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 344 AGAIPGKVKWQSTGP---KLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGW-------FRT 408
Cdd:PRK12316 4854 WKARDGDACGAAYMPigtPLGNRSGYVLDGQLNplpvgVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRT 4933
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309054211 409 KDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKG----KLVAMV 469
Cdd:PRK12316 4934 GDLARYRADGVIDYLGRVDH-QVKIRGFRIELGEIEARLREHPAVREAVVIAQEGavgkQLVGYV 4997
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
31-535 |
1.40e-19 |
|
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: 91.79 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 31 NKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSE-SSV 109
Cdd:cd05970 44 EERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADiKMI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 110 VIVSEKL---HYKLSASLLDSLKLVISM---------DTLEVIKSAGE--QDYTLNELPRPEDLASIIYTSGTSGASKgv 175
Cdd:cd05970 124 VAIAEDNipeEIEKAAPECPSKPKLVWVgdpvpegwiDFRKLIKNASPdfERPTANSYPCGEDILLVYFSSGTTGMPK-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 176 MLTHRN------LVTQNYMANkllpiFRED-VFLSILPLSHAyECSLGLILP--LSRGAQVVYLHGAPTPSLLLPALTQV 246
Cdd:cd05970 202 MVEHDFtyplghIVTAKYWQN-----VREGgLHLTVADTGWG-KAVWGKIYGqwIAGAAVFVYDYDKFDPKALLEKLSKY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 247 RPTIMLSVPliveKIYKNKIRPMFTKtwitqflYSISFIRRALhkVAGKKLCQTfggnlrffgiggskldgVVEKFLADA 326
Cdd:cd05970 276 GVTTFCAPP----TIYRFLIREDLSR-------YDLSSLRYCT--TAGEALNPE-----------------VFNTFKEKT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 327 GFPYGIGYGLTETSpLLAGAIPG-KVKWQSTGPKLPDIEMKILNPNHKKI-----GEIVV---KGPNV--MSGYYKDPVT 395
Cdd:cd05970 326 GIKLMEGFGQTETT-LTIATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCeageeGEIVIrtsKGKPVglFGGYYKDAEK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 396 TASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMmVGANGENIYPEEIEATINEHDMVLESLVVNT----KGKLVamvhf 471
Cdd:cd05970 405 TAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDL-IKSSGYRIGPFEVESALIQHPAVLECAVTGVpdpiRGQVV----- 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309054211 472 nyeqieklhtfneEAEVNMT---QRVEEVKKELMEYVNsRVNKSSKILEILEQSSPFEKTATQKIKR 535
Cdd:cd05970 478 -------------KATIVLAkgyEPSEELKKELQDHVK-KVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
36-459 |
1.41e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 92.08 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVI---- 111
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLfdlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 ---VSEKLHYKLSA-----SLLDSLKL---VISMDTLEVIKSAGEQDYtlnELPR-PEDLAS-IIYTSGTSGASKGVMLT 178
Cdd:PRK07008 121 flpLVDALAPQCPNvkgwvAMTDAAHLpagSTPLLCYETLVGAQDGDY---DWPRfDENQASsLCYTSGTTGNPKGALYS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 179 HRNLVTQNYMANklLP----IFREDVFLSILPLSHAYECSLGLILPLSrGAQVVYlhgaPTPSL----LLPALTQVRPTI 250
Cdd:PRK07008 198 HRSTVLHAYGAA--LPdamgLSARDAVLPVVPMFHVNAWGLPYSAPLT-GAKLVL----PGPDLdgksLYELIEAERVTF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 251 MLSVPlivekiyknkirpmftktwiTQFLYSISFIRRalhkvAGKKLcqtfgGNLRFFGIGGSKLDGVVEKFLADAgfpY 330
Cdd:PRK07008 271 SAGVP--------------------TVWLGLLNHMRE-----AGLRF-----STLRRTVIGGSACPPAMIRTFEDE---Y 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 331 GI----GYGLTETSPLlaGAIpGKVKWQSTGpkLPD----------------IEMKILNPNHKKI-------GEIVVKGP 383
Cdd:PRK07008 318 GVevihAWGMTEMSPL--GTL-CKLKWKHSQ--LPLdeqrkllekqgrviygVDMKIVGDDGRELpwdgkafGDLQVRGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 384 NVMSGYYK---DPVTtascfteDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07008 393 WVIDRYFRgdaSPLV-------DGWFPTGDVATIDADGFMQITDRsKDVIKSG--GEWISSIDIENVAVAHPAVAEAACI 463
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
32-464 |
1.42e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 91.88 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 32 KEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPIlpdFTAF---EIVNVIEHSESS 108
Cdd:PRK04319 71 KEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL---FEAFmeeAVRDRLEDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 109 VVIVSEKLHYKLSASLLDSLKLVISMDTLEvikSAGEQDYTLNEL------------PRPEDLASIIYTSGTSGASKGVM 176
Cdd:PRK04319 148 VLITTPALLERKPADDLPSLKHVLLVGEDV---EEGPGTLDFNALmeqasdefdiewTDREDGAILHYTSGSTGKPKGVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 177 LTHrNLVTQNYMANKLLPIFREDvflsilplsHAYEC----------SLGLILPLSRGAQVVYLHGAPTPSLLLPALTQV 246
Cdd:PRK04319 225 HVH-NAMLQHYQTGKYVLDLHED---------DVYWCtadpgwvtgtSYGIFAPWLNGATNVIDGGRFSPERWYRILEDY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 247 RPTIMLSVPlivekiyknkirpmftktwiTQFlysisfirRALHKvAGKKLCQTFG-GNLRFFGIGGSKLDGVVEKFLAD 325
Cdd:PRK04319 295 KVTVWYTAP--------------------TAI--------RMLMG-AGDDLVKKYDlSSLRHILSVGEPLNPEVVRWGMK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 326 A-GFPYGIGYGLTETspllaGAI-----PG-KVKWQSTGPKLPDIEMKI-------LNPNhkKIGEIVVKG--PNVMSGY 389
Cdd:PRK04319 346 VfGLPIHDNWWMTET-----GGImianyPAmDIKPGSMGKPLPGIEAAIvddqgneLPPN--RMGNLAIKKgwPSMMRGI 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309054211 390 YKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVGAnGENIYPEEIEATINEHDMVLESLVVntkGK 464
Cdd:PRK04319 419 WNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKLMEHPAVAEAGVI---GK 488
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
36-459 |
1.58e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 91.74 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVS-- 113
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 114 -----EKLhyklsASLLDSLKLVISM--------DTL------EVIKSAGEQDYTLNELPrpEDLAS-IIYTSGTSGASK 173
Cdd:PRK06018 121 fvpilEKI-----ADKLPSVERYVVLtdaahmpqTTLknavayEEWIAEADGDFAWKTFD--ENTAAgMCYTSGTTGDPK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 174 GVMLTHRNLVTQNYMANK--LLPIFREDVFLSILPLSHAYECSLGLILPlSRGAQVVY----LHGAPTPSLLlpALTQVr 247
Cdd:PRK06018 194 GVLYSHRSNVLHALMANNgdALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVMpgakLDGASVYELL--DTEKV- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 248 pTIMLSVPLIvekiyknkirpmftktWITQFLYsisfirraLHKvAGKKLcqtfgGNLRFFGIGGSKL-DGVVEKFLaDA 326
Cdd:PRK06018 270 -TFTAGVPTV----------------WLMLLQY--------MEK-EGLKL-----PHLKMVVCGGSAMpRSMIKAFE-DM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 327 GFPYGIGYGLTETSPL-LAGAIPG---------KVKWQSTGPKLP-DIEMKILNPNHKKI-------GEIVVKGPNVMSG 388
Cdd:PRK06018 318 GVEVRHAWGMTEMSPLgTLAALKPpfsklpgdaRLDVLQKQGYPPfGVEMKITDDAGKELpwdgktfGRLKVRGPAVAAA 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309054211 389 YYKdpvTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDnmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK06018 398 YYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRsKD--VIKSGGEWISSIDLENLAVGHPKVAEAAVI 464
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
33-458 |
2.05e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 91.29 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SeKLHYKLSASLLDSLK------LVISMDTLEVIKSAGEQDYTLNELPRPEDL--ASIIYTSGTSGASKGVM--LTHRNL 182
Cdd:PRK13391 103 S-AAKLDVARALLKQCPgvrhrlVLDGDGELEGFVGYAEAVAGLPATPIADESlgTDMLYSSGTTGRPKGIKrpLPEQPP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 183 VTQNYMANKLLPI--FRED-VFLSILPLSH-AYECSLGLILPLSrGAQVVYLHGAPTPSLLL-----PALTQVRPTI--- 250
Cdd:PRK13391 182 DTPLPLTAFLQRLwgFRSDmVYLSPAPLYHsAPQRAVMLVIRLG-GTVIVMEHFDAEQYLALieeygVTHTQLVPTMfsr 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 251 MLSVPlivekiykNKIRPMftktwitqflYSISFIRRALHKVAGkklC--QTFGGNLRFFGiggskldGVVEKFladagf 328
Cdd:PRK13391 261 MLKLP--------EEVRDK----------YDLSSLEVAIHAAAP---CppQVKEQMIDWWG-------PIIHEY------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 329 pYGI--GYGLTETSPLLAGAIPGKVKWQSTG-PKLPDIEMKILNPnhKKIGEIVVKGPNVMSgYYKDPVTTASCFTEDG- 404
Cdd:PRK13391 307 -YAAteGLGFTACDSEEWLAHPGTVGRAMFGdLHILDDDGAELPP--GEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGt 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 405 WFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLV 458
Cdd:PRK13391 383 WSTVGDIGYVDEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLITHPKVADAAV 435
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
35-459 |
1.73e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 88.51 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLSASllDSLKLVISMDTLEVIKSAGeqdytlnelpRPEDLAS---IIYTSGTSGASKGVMLTHRnLVTQNYMANK 191
Cdd:PRK13383 141 EFAERIAGA--DDAVAVIDPATAGAEESGG----------RPAVAAPgriVLLTSGTTGKPKGVPRAPQ-LRSAVGVWVT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 192 LLPIFREDVFLSI---LPLSHAYECSLgLILPLSRGAQVV-YLHGAPTPSLLLPALTqvRPTIMLSVPLIVEKIYK--NK 265
Cdd:PRK13383 208 ILDRTRLRTGSRIsvaMPMFHGLGLGM-LMLTIALGGTVLtHRHFDAEAALAQASLH--RADAFTAVPVVLARILElpPR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 266 IRpmftktwitqflysisfirralhkvAGKKLCQtfggnLRFFGIGGSKLD-GVVEKFLADAGFPYGIGYGLTETSpLLA 344
Cdd:PRK13383 285 VR-------------------------ARNPLPQ-----LRVVMSSGDRLDpTLGQRFMDTYGDILYNGYGSTEVG-IGA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 345 GAIPGKVK-WQST-GPKLPDIEMKILNPNHKKIGEIVVK----GPNVMSGYYKDPVTTASCfteDGWFRTKDLGYIDKNG 418
Cdd:PRK13383 334 LATPADLRdAPETvGKPVAGCPVRILDRNNRPVGPRVTGrifvGGELAGTRYTDGGGKAVV---DGMTSTGDMGYLDNAG 410
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1309054211 419 NLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK13383 411 RLFIVGREDDMII-SGGENVYPRAVENALAAHPAVADNAVI 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
35-501 |
3.47e-18 |
|
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: 87.21 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAI-LGNNMpnWA-VSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:cd05918 25 LTYAELDRLSSRLAHHLRSLGVGPGVFVPLcFEKSK--WAvVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SeklhyklsaslldslklvismdtleviksageqdytlnelpRPEDLASIIYTSGTSGASKGVMLTHRNLVTqNYMA-NK 191
Cdd:cd05918 103 S-----------------------------------------SPSDAAYVIFTSGSTGKPKGVVIEHRALST-SALAhGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 192 LLPIFREDVFL--SilplSHAYECSLGLIL-PLSRGAQVVylhgAPTPSLLLPALTQVrptimlsvplivekIYKNKIrp 268
Cdd:cd05918 141 ALGLTSESRVLqfA----SYTFDVSILEIFtTLAAGGCLC----IPSEEDRLNDLAGF--------------INRLRV-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 269 mftkTWItqFLYSiSFIRrALHKvagkKLCQTfggnLRFFGIGGSKLD-GVVEKFlADagfpyGI----GYGLTETSPL- 342
Cdd:cd05918 197 ----TWA--FLTP-SVAR-LLDP----EDVPS----LRTLVLGGEALTqSDVDTW-AD-----RVrlinAYGPAECTIAa 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 343 LAGAIPGKVKWQSTGPKLPDIeMKILNP-NHKK------IGEIVVKGPNVMSGYYKDPVTTASCFTED-GW--------- 405
Cdd:cd05918 255 TVSPVVPSTDPRNIGRPLGAT-CWVVDPdNHDRlvpigaVGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrg 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 406 ---FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV--------NTKGKLVAMVHFNYE 474
Cdd:cd05918 334 rrlYRTGDLVRYNPDGSLEYVGRKDT-QVKIRGQRVELGEIEHHLRQSLPGAKEVVVevvkpkdgSSSPQLVAFVVLDGS 412
|
490 500
....*....|....*....|....*....
gi 1309054211 475 QIEKLHTFNEEAEVN--MTQRVEEVKKEL 501
Cdd:cd05918 413 SSGSGDGDSLFLEPSdeFRALVAELRSKL 441
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
35-444 |
2.12e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 85.06 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLhyKLSASLLDSLKLVISMDTLEVIKSAGEQDYTLnELPRP--------EDLASIIYTSGTSGASKGVMLTHRNLVTqn 186
Cdd:PRK05857 122 GS--KMASSAVPEALHSIPVIAVDIAAVTRESEHSL-DAASLagnadqgsEDPLAMIFTSGTTGEPKAVLLANRTFFA-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 187 ymanklLP-IFREDVFLSI---------LPLSHAYECSLGLILP-LSRGAQVVyLHGAPTPSLllpalTQVrptimlsvp 255
Cdd:PRK05857 197 ------VPdILQKEGLNWVtwvvgettySPLPATHIGGLWWILTcLMHGGLCV-TGGENTTSL-----LEI--------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 256 LIVEKIYKNKIRPmftkTWITQFLYSIsfirralhkvagkKLCQTFGGNLRFFGIGGSKLDGVVEKFLADAGFPYGIGYG 335
Cdd:PRK05857 256 LTTNAVATTCLVP----TLLSKLVSEL-------------KSANATVPSLRLVGYGGSRAIAADVRFIEATGVRTAQVYG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 336 LTETS------PLLAGAIpGKVKWQSTGPKLPDIEMKILNPN-----------HKKIGEIVVKGPNVMSGYYKDPVTTAS 398
Cdd:PRK05857 319 LSETGctalclPTDDGSI-VKIEAGAVGRPYPGVDVYLAATDgigptapgagpSASFGTLWIKSPANMLGYWNNPERTAE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1309054211 399 CFTeDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIE 444
Cdd:PRK05857 398 VLI-DGWVNTGDLLERREDGFFYIKGRSSEMII-CGGVNIAPDEVD 441
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
62-458 |
2.37e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 85.12 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 62 VAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEKlhyklSASLLDSLKL---VISMDTL- 137
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESA-----HAELLDGLDPgvrVINVDSPa 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 138 ---EVIKSAGEQDYTLNelPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECS 214
Cdd:PRK07867 132 wadELAAHRDAEPPFRV--ADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVM 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 215 LGLILPLSRGAQVVylhgaptpslllpaltqvrptimlsvplivekiyknkIRPMFTktwITQFLysiSFIRR----ALH 290
Cdd:PRK07867 210 AGWAVALAAGASIA-------------------------------------LRRKFS---ASGFL---PDVRRygatYAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 291 KVaGKKLCQTFG---------GNLRF-FGIGGSKLDgvVEKFLADAGFPYGIGYGLTETSPLLA---GAIPGkvkwqSTG 357
Cdd:PRK07867 247 YV-GKPLSYVLAtperpddadNPLRIvYGNEGAPGD--IARFARRFGCVVVDGFGSTEGGVAITrtpDTPPG-----ALG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 358 PKLPDIemKILNPN------------------HKKIGEIV-VKGPNVMSGYYKDPVTTAScFTEDGWFRTKDLGYIDKNG 418
Cdd:PRK07867 319 PLPPGV--AIVDPDtgtecppaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPEADAE-RMRGGVYWSGDLAYRDADG 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1309054211 419 NLYIKGRKDNMMvGANGENIYPEEIEATINEHDMVLESLV 458
Cdd:PRK07867 396 YAYFAGRLGDWM-RVDGENLGTAPIERILLRYPDATEVAV 434
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
31-465 |
4.03e-17 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 84.67 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 31 NKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILgnnMPNWAVSYFAITTSSRV-----VVpiLPDFTAFEIVNVIEHS 105
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIY---MPMIPEAAIAMLACARIgaihsVV--FGGFAAKELASRIDDA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 106 ESSVVIVS-------------EKLHYKLSASLLDSLK-LVISMDTLEVIKSAGEQDYTLNEL-----PRP------EDLA 160
Cdd:cd05967 154 KPKLIVTAscgiepgkvvpykPLLDKALELSGHKPHHvLVLNRPQVPADLTKPGRDLDWSELlakaePVDcvpvaaTDPL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 161 SIIYTSGTSGASKGVML-THRNLVTQNYMANKLLPIFREDVFLSILPLS----HAYECsLGlilPLSRGAQVVYLHGAP- 234
Cdd:cd05967 234 YILYTSGTTGKPKGVVRdNGGHAVALNWSMRNIYGIKPGDVWWAASDVGwvvgHSYIV-YG---PLLHGATTVLYEGKPv 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 235 -TPSlllpaltqvrPTIMLSVplivekIYKNKIRPMFTKTwiTQFlysisfirRALHK--VAGKKLCQTFGGNLRFFGIG 311
Cdd:cd05967 310 gTPD----------PGAFWRV------IEKYQVNALFTAP--TAI--------RAIRKedPDGKYIKKYDLSSLRTLFLA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 312 GSKLDGVVEKFLADA-GFPYGIGYGLTET-SPLLA---GAIPGKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVK 381
Cdd:cd05967 364 GERLDPPTLEWAENTlGVPVIDHWWQTETgWPITAnpvGLEPLPIKAGSPGKPVPGYQVQVLDEDGEpvgpnELGNIVIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 382 GP---NVMSGYYKDPVT-TASCFTED-GWFRTKDLGYIDKNGNLYIKGRKDNMMVGAnGENIYPEEIEATINEHDMVLES 456
Cdd:cd05967 444 LPlppGCLLTLWKNDERfKKLYLSKFpGYYDTGDAGYKDEDGYLFIMGRTDDVINVA-GHRLSTGEMEESVLSHPAVAEC 522
|
....*....
gi 1309054211 457 LVVNTKGKL 465
Cdd:cd05967 523 AVVGVRDEL 531
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
32-469 |
6.00e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.83 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 32 KEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVI 111
Cdd:PRK12467 535 EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VSEKLHYKLSasLLDSLK-LVISMDTLEVIKSAGEqdytlNELPR--PEDLASIIYTSGTSGASKGVMLTHRNLVTQNYM 188
Cdd:PRK12467 615 TQSHLLAQLP--VPAGLRsLCLDEPADLLCGYSGH-----NPEVAldPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 189 ANKLLPIFREDVFLSILPLshAYECS-LGLILPLSRGAqvvylhgaptpSLLLPALTQVRPTIMLSVPLIVEKIYKNKIR 267
Cdd:PRK12467 688 IAERLQLAADDSMLMVSTF--AFDLGvTELFGALASGA-----------TLHLLPPDCARDAEAFAALMADQGVTVLKIV 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 268 PMFTKtwitQFLYS--ISFIRRALHKVAGKKLCQtfggnlrffgiggskLDGVVEKFLADAGFPYGIGYGLTETS----- 340
Cdd:PRK12467 755 PSHLQ----ALLQAsrVALPRPQRALVCGGEALQ---------------VDLLARVRALGPGARLINHYGPTETTvgvst 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 341 ------PLLAGAIPgkvkwqsTGPKLPDIEMKI----LNP-NHKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGW---- 405
Cdd:PRK12467 816 yelsdeERDFGNVP-------IGQPLANLGLYIldhyLNPvPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadg 888
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054211 406 ---FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKG----KLVAMV 469
Cdd:PRK12467 889 grlYRTGDLARYRADGVIEYLGRMDH-QVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGdaglQLVAYL 958
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
36-537 |
6.05e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 83.74 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEK 115
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 116 -----------LHYKLSASLLDSLKLVISMDT--------------LEVIKSAGEQDYTLNELPRPEDLASII--YTSGT 168
Cdd:PLN02479 127 fftlaeealkiLAEKKKSSFKPPLLIVIGDPTcdpkslqyalgkgaIEYEKFLETGDPEFAWKPPADEWQSIAlgYTSGT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 169 SGASKGVMLTHRNLVTQNyMANKLLPIFRED-VFLSILPLSHAYECSLGLILPLSRGAQVVYLHgaPTPSLLLPALTQVR 247
Cdd:PLN02479 207 TASPKGVVLHHRGAYLMA-LSNALIWGMNEGaVYLWTLPMFHCNGWCFTWTLAALCGTNICLRQ--VTAKAIYSAIANYG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 248 PTIMLSVPLIVEKIY----KNKIRPMftktwitqflysisfiRRALHKVagkklcqtfggnlrffgIGGSKLDGVVEKFL 323
Cdd:PLN02479 284 VTHFCAAPVVLNTIVnapkSETILPL----------------PRVVHVM-----------------TAGAAPPPSVLFAM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 324 ADAGFPYGIGYGLTETSPllagaiPGKV-KWQSTGPKLPDIE-------------------------MKILNPNHKKIGE 377
Cdd:PLN02479 331 SEKGFRVTHTYGLSETYG------PSTVcAWKPEWDSLPPEEqarlnarqgvryiglegldvvdtktMKPVPADGKTMGE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 378 IVVKGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMVGanGENIYPEEIEATINEHDMVLES 456
Cdd:PLN02479 405 IVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRsKDIIISG--GENISSLEVENVVYTHPAVLEA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 457 LVVntkgklvAMVHFNY-EQIEKLHTFNEEAEVNMTQRVEEvkkELMEYVNSR-----VNKSSKIleileqsSPFEKTAT 530
Cdd:PLN02479 482 SVV-------ARPDERWgESPCAFVTLKPGVDKSDEAALAE---DIMKFCRERlpaywVPKSVVF-------GPLPKTAT 544
|
....*..
gi 1309054211 531 QKIKRYL 537
Cdd:PLN02479 545 GKIQKHV 551
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
25-502 |
8.12e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 83.45 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 25 TAFSLIN--------KEKLTYREFGDSVEHLTEILNKHGVKkGEKVAILGNNMPNWAVSYFAITTSSRVVVPI-LPDFTA 95
Cdd:PRK05850 18 AAFTFIDyeqdpagvAETLTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGLEYIVAFLGALQAGLIAVPLsVPQGGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 96 FE--IVNVIEHSESSVV-----IVSEKLHYkLSASLLDSLKLVISMDTLEViKSAGEQDYTLNELPrpeDLASIIYTSGT 168
Cdd:PRK05850 97 HDerVSAVLRDTSPSVVlttsaVVDDVTEY-VAPQPGQSAPPVIEVDLLDL-DSPRGSDARPRDLP---STAYLQYTSGS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 169 SGASKGVMLTHRNLVT------QNYMA--NKLLPifREDVFLSILPLSHAYECSLGLILPLSRGaqvvylhgaptpslll 240
Cdd:PRK05850 172 TRTPAGVMVSHRNVIAnfeqlmSDYFGdtGGVPP--PDTTVVSWLPFYHDMGLVLGVCAPILGG---------------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 241 paltqvRPTIMLSvplivekiyknkirPMftktwitqflysiSFIRRA---LHKVAGKKLCQTFGGNLRF---------F 308
Cdd:PRK05850 234 ------CPAVLTS--------------PV-------------AFLQRParwMQLLASNPHAFSAAPNFAFelavrktsdD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 309 GIGGSKLDGV--------------VEKFlADAGFPYGI-------GYGLTETSPLLAGAIP----------------GKV 351
Cdd:PRK05850 281 DMAGLDLGGVlgiisgservhpatLKRF-ADRFAPFNLretairpSYGLAEATVYVATREPgqppesvrfdyeklsaGHA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 352 KWQSTG----------PKLP-----DIEMKILNPNhKKIGEIVVKGPNVMSGYYKDPVTTASCF----------TEDG-W 405
Cdd:PRK05850 360 KRCETGggtplvsygsPRSPtvrivDPDTCIECPA-GTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpW 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 406 FRTKDLGYIDkNGNLYIKGR-KDNMMVgaNGENIYPEEIEATINE---HDMVLESLVVNTKGKLVAMVHFNyeqieKLHT 481
Cdd:PRK05850 439 LRTGDLGFIS-EGELFIVGRiKDLLIV--DGRNHYPDDIEATIQEitgGRVAAISVPDDGTEKLVAIIELK-----KRGD 510
|
570 580
....*....|....*....|.
gi 1309054211 482 FNEEAevnmTQRVEEVKKELM 502
Cdd:PRK05850 511 SDEEA----MDRLRTVKREVT 527
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
36-459 |
2.23e-16 |
|
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: 82.24 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSEK 115
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 116 LHYK-----LSASLLDSLKL-VISMDTLEVIKSAGE-------QDYTLNEL-----PR-------PEDLASIIYTSGTSG 170
Cdd:cd17634 166 GVRAgrsvpLKKNVDDALNPnVTSVEHVIVLKRTGSdidwqegRDLWWRDLiakasPEhqpeamnAEDPLFILYTSGTTG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 171 ASKGVMLTHRNLVTqnYMANKLLPIFR---EDVFLSILPLSHAYECSLGLILPLSRGAQVVYLHGA---PTPSLLLPALT 244
Cdd:cd17634 246 KPKGVLHTTGGYLV--YAATTMKYVFDygpGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVpnwPTPARMWQVVD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 245 QVRPTIMLSVPLIVekiyknkirpmftktwitqflysisfirRALHKVAGKKLCQTFGGNLRFFGIGGSKLDG-----VV 319
Cdd:cd17634 324 KHGVNILYTAPTAI----------------------------RALMAAGDDAIEGTDRSSLRILGSVGEPINPeayewYW 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 320 EKfLADAGFPYGIGYGLTETSPLLAGAIPGKVKWQSTGPKLPDIEMKIL------NPNHK-KIGEIVVKGP---NVMSGY 389
Cdd:cd17634 376 KK-IGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAvvdnegHPQPGgTEGNLVITDPwpgQTRTLF 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054211 390 YKDPVTTASCF-TEDGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17634 455 GDHERFEQTYFsTFKGMYFSGDGARRDEDGYYWITGRSDD-VINVAGHRLGTAEIESVLVAHPKVAEAAVV 524
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
33-459 |
2.39e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 81.86 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSASL--LDSLKLVISMD------------TLEVIKSAGEQDYTLNElPRPEDLAsIIYTSGTSGASKGVMLT 178
Cdd:PRK07798 107 EREFAPRVAEVLprLPKLRTLVVVEdgsgndllpgavDYEDALAAGSPERDFGE-RSPDDLY-LLYTGGTTGMPKGVMWR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 179 H----------RNLVTQNYMANK--LLPIFREDVFLSILPLShayecslglilPLsrgaqvvyLHGAPTPSLLLpALTQV 246
Cdd:PRK07798 185 QedifrvllggRDFATGEPIEDEeeLAKRAAAGPGMRRFPAP-----------PL--------MHGAGQWAAFA-ALFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 247 RPTIMLSVPL-----IVEKIYKNKI-----------RPM-----FTKTWITQFLYSIS--------FIRRALhkvagkkl 297
Cdd:PRK07798 245 QTVVLLPDVRfdadeVWRTIEREKVnvitivgdamaRPLldaleARGPYDLSSLFAIAsggalfspSVKEAL-------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 298 cqtfggnLRFF-------GIGGSkldgvvekflaDAGFpygIGYGLTETSPLLAGAipGKVKWQSTGpKLPDIEMKILNP 370
Cdd:PRK07798 317 -------LELLpnvvltdSIGSS-----------ETGF---GGSGTVAKGAVHTGG--PRFTIGPRT-VVLDEDGNPVEP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 371 NHKKIGeIVVKGPNVMSGYYKDPVTTASCFTE-DG--WFRTKDLGYIDKNGNLYIKGRkDNMMVGANGENIYPEEIEATI 447
Cdd:PRK07798 373 GSGEIG-WIARRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGR-GSVCINTGGEKVFPEEVEEAL 450
|
490
....*....|..
gi 1309054211 448 NEHDMVLESLVV 459
Cdd:PRK07798 451 KAHPDVADALVV 462
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-469 |
2.45e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.08 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 31 NKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVV 110
Cdd:PRK12316 3079 GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 IVSEKLHYKLSASlldslklVISMDTLEVIKSAGEQDYTLNELPrpEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMAN 190
Cdd:PRK12316 3159 LSQSHLRLPLAQG-------VQVLDLDRGDENYAEANPAIRTMP--ENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQ 3229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 KLLPIFREDVFLSILPLSHAYEcSLGLILPLSRGAQVVyLHGaptpslllpaltqvrPTIMLSVPLIVEkiyknkirpMF 270
Cdd:PRK12316 3230 QAYGLGVGDRVLQFTTFSFDVF-VEELFWPLMSGARVV-LAG---------------PEDWRDPALLVE---------LI 3283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 271 TKTWITQFLYSISFIRRALHKVAGKKLcqtfgGNLRFFGIGGSKLDGVVEKfLADAGFPYGIGYGLTETS--PLLAGAIP 348
Cdd:PRK12316 3284 NSEGVDVLHAYPSMLQAFLEEEDAHRC-----TSLKRIVCGGEALPADLQQ-QVFAGLPLYNLYGPTEATitVTHWQCVE 3357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 349 GKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGW------FRTKDLGYIDKN 417
Cdd:PRK12316 3358 EGKDAVPIGRPIANRACYILDGSLEpvpvgALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRAD 3437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1309054211 418 GNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKG-KLVAMV 469
Cdd:PRK12316 3438 GVIEYIGRVDH-QVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGrQLVAYV 3489
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
33-459 |
3.53e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 81.10 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLhYKLSASLLDSLKL---VISMDTLEViksAGEQDYT--LNELPrPEDLAS------IIYTSGTSGASKGVM--LTH 179
Cdd:PRK08276 90 SAAL-ADTAAELAAELPAgvpLLLVVAGPV---PGFRSYEeaLAAQP-DTPIADetagadMLYSSGTTGRPKGIKrpLPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 180 RN-LVTQNYMANKLL---PIFREDVFLSILPLSHAyecslgliLPLSRGAQVVYLHGaptPSLLLP------AL------ 243
Cdd:PRK08276 165 LDpDEAPGMMLALLGfgmYGGPDSVYLSPAPLYHT--------APLRFGMSALALGG---TVVVMEkfdaeeALaliery 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 244 ----TQVRPTI---MLSVPlivEKIyKNKirpmftktwitqflYSISFIRRALHKVA------GKKLCQTFGGnlrffgi 310
Cdd:PRK08276 234 rvthSQLVPTMfvrMLKLP---EEV-RAR--------------YDVSSLRVAIHAAApcpvevKRAMIDWWGP------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 311 ggskldgVVEKFLADAGfpygiGYGLTETSPLLAGAIPGKV--KWQStgpklpdiEMKILNPNHK-----KIGEIVVKGP 383
Cdd:PRK08276 289 -------IIHEYYASSE-----GGGVTVITSEDWLAHPGSVgkAVLG--------EVRILDEDGNelppgEIGTVYFEMD 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054211 384 NVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK08276 349 GYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMII-SGGVNIYPQEIENLLVTHPKVADVAVF 423
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
8-535 |
5.65e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 80.55 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 8 LSLADIYSRSLVDFSEQTAFSLinkeKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVV 87
Cdd:cd05915 2 ERAAALFGRKEVVSRLHTGEVH----RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 88 PILPDFTAFEIVNVIEHSESSVVIVSEKLHYKLSASLldSLKLVISMDTLEVIKSAGEQDYTLNELP-----RPEDLASI 162
Cdd:cd05915 78 TANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIR--GELKTVQHFVVMDEKAPEGYLAYEEALGeeadpVRVPERAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 163 I---YTSGTSGASKGVMLTHRN-------LVTQNYMANKLLPifredVFLSILPLSHAYE-CSLGLILPLsrGAQVVYLH 231
Cdd:cd05915 156 CgmaYTTGTTGLPKGVVYSHRAlvlhslaASLVDGTALSEKD-----VVLPVVPMFHVNAwCLPYAATLV--GAKQVLPG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 232 GAPTPSLLLPALTQVRPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFLYsisfirralhkvagkklcqtfggnlrffgiG 311
Cdd:cd05915 229 PRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVV------------------------------G 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 312 GSKLDGVVEKFLADAGFPYGIGYGLTETSPLLAGAIpgkvkWQSTGPKLPDIE----------------MKILNP----- 370
Cdd:cd05915 279 GSAAPRSLIARFERMGVEVRQGYGLTETSPVVVQNF-----VKSHLESLSEEEkltlkaktglpiplvrLRVADEegrpv 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 371 --NHKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATIN 448
Cdd:cd05915 354 pkDGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIK-SGGEWISSVDLENALM 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 449 EHDMVLESLVVNTKGKLVAmvhfnyeqiEKLHTFNEEAEvnmtqrVEEVKKELMEYVNSRVNKSSKILEILEQSSPFEKT 528
Cdd:cd05915 433 GHPKVKEAAVVAIPHPKWQ---------ERPLAVVVPRG------EKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRT 497
|
....*..
gi 1309054211 529 ATQKIKR 535
Cdd:cd05915 498 SAGKFLK 504
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
35-537 |
6.23e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 80.25 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPIlpdFTAFEiVNVIEH----SESSVV 110
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPL---FTAFG-PKAIEHrlrtSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 IVSEKLHYKLSaslldslklvismdtleviksageqdytlnelprpEDLASIIYTSGTSGASKGVMLTHRNLVT-QNYMA 189
Cdd:cd05973 77 VTDAANRHKLD-----------------------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAfGAYLR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 190 NKLlPIFREDVFLSILPLSHAYECSLGLILPLSRGAqvvylhgaptpslllpaltqvrPTIMLSVPLIVEKIYKnkirpM 269
Cdd:cd05973 122 DAV-DLRPEDSFWNAADPGWAYGLYYAITGPLALGH----------------------PTILLEGGFSVESTWR-----V 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 FTKTWITQFLYSISFIRraLHKVAGKKLCQTFGGNLRFFGIGGSKLD-GVVEKFLADAGFPYGIGYGLTETSPLLAG--A 346
Cdd:cd05973 174 IERLGVTNLAGSPTAYR--LLMAAGAEVPARPKGRLRRVSSAGEPLTpEVIRWFDAALGVPIHDHYGQTELGMVLANhhA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 347 IPGKVKWQSTGPKLPDIEMKILNPNHKKIGE-------IVVKGPNVM--SGYYKDPVTTAScfteDGWFRTKDLGYIDKN 417
Cdd:cd05973 252 LEHPVHAGSAGRAMPGWRVAVLDDDGDELGPgepgrlaIDIANSPLMwfRGYQLPDTPAID----GGYYLTGDTVEFDPD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 418 GNLYIKGRKDNMMVGAnGENIYPEEIEATINEHDMVLESLVV----NTKGKLVamvhfnyeqieklhtfneEAEV---NM 490
Cdd:cd05973 328 GSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAVIgvpdPERTEVV------------------KAFVvlrGG 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1309054211 491 TQRVEEVKKELMEYVNSRVNKSS--KILEILEQsspFEKTATQKIKRYL 537
Cdd:cd05973 389 HEGTPALADELQLHVKKRLSAHAypRTIHFVDE---LPKTPSGKIQRFL 434
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-469 |
1.24e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.77 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 29 LINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESS 108
Cdd:PRK12316 2023 VFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAA 2102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 109 VVIVSEklhyklsaSLLDSLKLVISMDTLEVIKSAGEQDY-TLNELPR--PEDLASIIYTSGTSGASKGVMLTHRNLVTQ 185
Cdd:PRK12316 2103 LLLTQR--------HLLERLPLPAGVARLPLDRDAEWADYpDTAPAVQlaGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 186 NYMANKLLPIFREDVFLSILPLSH--AYEcslGLILPLSRGAQVVYLHGaptpSLLLP---ALTQVRPTIMLSVplivek 260
Cdd:PRK12316 2175 CQAAGERYELSPADCELQFMSFSFdgAHE---QWFHPLLNGARVLIRDD----ELWDPeqlYDEMERHGVTILD------ 2241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 261 iyknkirpmFTKTWITQFlysISFIRRALHKVAGKKLCqtFGGNlrffGIGGSKLDGVVEKFLADAGFPygiGYGLTET- 339
Cdd:PRK12316 2242 ---------FPPVYLQQL---AEHAERDGRPPAVRVYC--FGGE----AVPAASLRLAWEALRPVYLFN---GYGPTEAv 2300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 340 -SPLLAGA---IPGKVKWQSTGPKLPDIEMKILNPN-----HKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGW----- 405
Cdd:PRK12316 2301 vTPLLWKCrpqDPCGAAYVPIGRALGNRRAYILDADlnllaPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasge 2380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 406 --FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKG----KLVAMV 469
Cdd:PRK12316 2381 rlYRTGDLARYRADGVVEYLGRIDH-QVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGasgkQLVAYV 2449
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
35-462 |
2.11e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 79.31 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITtsSRVVVPIL--PDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACL--ARGVMAFLanPELHRDDHALAARNTEPALVVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSASlldslKLVISMDTLEVIKSAGEQDYtlnELPRPEDLASIIYTSGTSGASKGVMLTHRNLVT-QNYMANK 191
Cdd:PRK06060 109 SDALRDRFQPS-----RVAEAAELMSEAARVAPGGY---EPMGGDALAYATYTSGTTGPPKAAIHRHADPLTfVDAMCRK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 192 LLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPAL-TQVRPTIMLSVPLIVEKIYKNKIRPMF 270
Cdd:PRK06060 181 ALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAV-INSAPVTPEAAAILsARFGPSVLYGVPNFFARVIDSCSPDSF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 271 TKtwitqfLYSISFIRRALHKVAGKKLCQTFGGNLRFFGIGGSKldgVVEKFLADAGFPYGIGygltetspllagaipgk 350
Cdd:PRK06060 260 RS------LRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTE---VGQTFVSNRVDEWRLG----------------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 351 vkwqSTGPKLPDIEMKILNPNHKKIG-----EIVVKGPNVMSGYYKDPvttASCFTEDGWFRTKDLGYIDKNGNLYIKGR 425
Cdd:PRK06060 314 ----TLGRVLPPYEIRVVAPDGTTAGpgvegDLWVRGPAIAKGYWNRP---DSPVANEGWLDTRDRVCIDSDGWVTYRCR 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 1309054211 426 KDNM-MVGanGENIYPEEIEATINEHDMVLESLVVNTK 462
Cdd:PRK06060 387 ADDTeVIG--GVNVDPREVERLIIEDEAVAEAAVVAVR 422
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
33-533 |
8.14e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHyKLSASLLDSLKLVISM--------DTLEVIKSAGEQdytLNELPRPedlASIIYTSGTSGASKGVM--LTHRNL 182
Cdd:PRK13390 103 SAALD-GLAAKVGADLPLRLSFggeidgfgSFEAALAGAGPR---LTEQPCG---AVMLYSSGTTGFPKGIQpdLPGRDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 183 VTQN----YMANKLLPIFREDVFLSILPLSHAYE---CSLGLILplsrGAQVVyLHGAPTPSLLLPALTQVRPTIMLSVP 255
Cdd:PRK13390 176 DAPGdpivAIARAFYDISESDIYYSSAPIYHAAPlrwCSMVHAL----GGTVV-LAKRFDAQATLGHVERYRITVTQMVP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 256 LIVEKIYK--NKIRPMftktwitqflYSISFIRRALHKVAGkklCQTfggNLRFFGIggSKLDGVVEKFLADAGfpygiG 333
Cdd:PRK13390 251 TMFVRLLKldADVRTR----------YDVSSLRAVIHAAAP---CPV---DVKHAMI--DWLGPIVYEYYSSTE-----A 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 334 YGLT--ETSPLLAGaiPGKVKWQSTGpklpdiEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCF--TEDG 404
Cdd:PRK13390 308 HGMTfiDSPDWLAH--PGSVGRSVLG------DLHICDDDGNelpagRIGTVYFERDRLPFRYLNDPEKTAAAQhpAHPF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 405 WFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLESLVVNTKGKLVAmvhfnyEQIeklhtfne 484
Cdd:PRK13390 380 WTTVGDLGSVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMG------EQV-------- 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 485 EAEVNMTQRV---EEVKKELMEYVNSRVN--KSSKILEILEQsspFEKTATQKI 533
Cdd:PRK13390 445 KAVIQLVEGIrgsDELARELIDYTRSRIAhyKAPRSVEFVDE---LPRTPTGKL 495
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
334-453 |
8.58e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 76.57 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 334 YGLTETS-------P--LLAGAIpgkvkwqSTGPKLPDIEMKILNPnhkKIGEIVVKGPNVMSGYYKDPVTTASCFTEDg 404
Cdd:PRK07445 261 YGMTETAsqiatlkPddFLAGNN-------SSGQVLPHAQITIPAN---QTGNITIQAQSLALGYYPQILDSQGIFETD- 329
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1309054211 405 wfrtkDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEATINEHDMV 453
Cdd:PRK07445 330 -----DLGYLDAQGYLHILGRNSQKII-TGGENVYPAEVEAAILATGLV 372
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
31-464 |
1.09e-14 |
|
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: 76.44 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 31 NKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTafeivnviehsessvv 110
Cdd:cd17645 20 RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 111 ivSEKLHYKLSASlldSLKLVISmdtleviksageqdytlnelpRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMAN 190
Cdd:cd17645 84 --GERIAYMLADS---SAKILLT---------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 KLLPIFREDVflSILPLSHAYECSLGLILP-LSRGAQvvyLHgaptpslLLPALTQvrptimlsvpLIVEKIYKnkirpM 269
Cdd:cd17645 138 PYFGVTPADK--SLVYASFSFDASAWEIFPhLTAGAA---LH-------VVPSERR----------LDLDALND-----Y 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 FTKTWITqflysISFirraLHKVAGKKLCQTFGGNLRFFGIGGSKLDGVVEKfladagfPYGI--GYGLTETSpLLAGAI 347
Cdd:cd17645 191 FNQEGIT-----ISF----LPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERK-------GYKLvnNYGPTENT-VVATSF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 348 PGKVKWQS--TGPKLPDIEMKILNPNHK-----KIGEIVVKGPNVMSGYYKDPVTTASCFTEDGW------FRTKDLGYI 414
Cdd:cd17645 254 EIDKPYANipIGKPIDNTRVYILDEALQlqpigVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKF 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1309054211 415 DKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKGK 464
Cdd:cd17645 334 LPDGNIEFLGRLDQ-QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDA 382
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
32-482 |
1.35e-14 |
|
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: 75.93 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 32 KEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTafeivnviehsessvvi 111
Cdd:cd17644 23 DQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP----------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 vSEKLHYKLSASLLDSLklvismdtleviksageqdytlneLPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANK 191
Cdd:cd17644 86 -QERLTYILEDAQISVL------------------------LTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 192 LLPIFRED---VFLSIlplshAYECSLGLILPLsrgaqvvYLHGAptpSLLLpaltqvRPTIML-SVPLIVEKIYKNKIR 267
Cdd:cd17644 141 EYGITSSDrvlQFASI-----AFDVAAEEIYVT-------LLSGA---TLVL------RPEEMRsSLEDFVQYIQQWQLT 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 268 -----PMFTKTWITQFLYSISFIRRALHKVAgkklcqtfggnlrffgIGGSKLDG--VVEKFLADAGFPYGI-GYGLTE- 338
Cdd:cd17644 200 vlslpPAYWHLLVLELLLSTIDLPSSLRLVI----------------VGGEAVQPelVRQWQKNVGNFIQLInVYGPTEa 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 339 ----TSPLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFTEDGW---- 405
Cdd:cd17644 264 tiaaTVCRLTQLTERNITSVPIGRPIANTQVYILDENLQPVpvgvpGELHIGGVGLARGYLNRPELTAEKFISHPFnsse 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 406 ----FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV---NTKG--KLVAMVHFNYEQ- 475
Cdd:cd17644 344 serlYKTGDLARYLPDGNIEYLGRIDN-QVKIRGFRIELGEIEAVLSQHNDVKTAVVIvreDQPGnkRLVAYIVPHYEEs 422
|
....*....
gi 1309054211 476 --IEKLHTF 482
Cdd:cd17644 423 psTVELRQF 431
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
35-449 |
6.43e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 74.38 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILnKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVP---------------ILPDFTAFEIV 99
Cdd:PRK07769 56 LTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPlfdpaepghvgrlhaVLDDCTPSAIL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 100 NVIEHSESSvvivsEKLHYKLSAsllDSLKLVISMDTLEVIKSAGEQDYTLNElprpEDLASIIYTSGTSGASKGVMLTH 179
Cdd:PRK07769 135 TTTDSAEGV-----RKFFRARPA---KERPRVIAVDAVPDEVGATWVPPEANE----DTIAYLQYTSGSTRIPAGVQITH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 180 RNLVTQNYMANKLLPIFREDVFLSILPLSHayecSLGLIlplsrgaqvvylhgaptpSLLLPALTQVRPTIMlSVPLIVE 259
Cdd:PRK07769 203 LNLPTNVLQVIDALEGQEGDRGVSWLPFFH----DMGLI------------------TVLLPALLGHYITFM-SPAAFVR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 260 KIYKnKIRPMFTKTWITQFLYSIS--FirrALHKVAGKKLCQTFGGNLRFFGIGGSkLDG-------VVEKFlADAGFPY 330
Cdd:PRK07769 260 RPGR-WIRELARKPGGTGGTFSAApnF---AFEHAAARGLPKDGEPPLDLSNVKGL-LNGsepvspaSMRKF-NEAFAPY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 331 GI-------GYGLTE------TSP--------------LLAG-----------AIP----GKV---KWQ-----STGPKL 360
Cdd:PRK07769 334 GLpptaikpSYGMAEatlfvsTTPmdeeptviyvdrdeLNAGrfvevpadapnAVAqvsaGKVgvsEWAvivdpETASEL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 361 PDiemkilnpNHkkIGEIVVKGPNVMSGYYKDPVTTASCF----------------TEDG-WFRTKDLG-YIDknGNLYI 422
Cdd:PRK07769 414 PD--------GQ--IGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegaPDDAlWVRTGDYGvYFD--GELYI 481
|
490 500
....*....|....*....|....*...
gi 1309054211 423 KGR-KDnmMVGANGENIYPEEIEATINE 449
Cdd:PRK07769 482 TGRvKD--LVIIDGRNHYPQDLEYTAQE 507
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
10-449 |
7.15e-14 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 74.39 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 10 LADIYSRSLVDFSEQTAFSLInkeKLTYREFGDSVEHLTEILNKHgVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPI 89
Cdd:PRK12476 47 VGDTVAYRYLDHSHSAAGCAV---ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 90 ----LPDFTAfEIVNVIEHSESSVVI----VSEKLHYKLSASLLDSLKLVISMDtlEVIKSAGEqDYTLNELpRPEDLAS 161
Cdd:PRK12476 123 fapeLPGHAE-RLDTALRDAEPTVVLtttaAAEAVEGFLRNLPRLRRPRVIAID--AIPDSAGE-SFVPVEL-DTDDVSH 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 162 IIYTSGTSGASKGVMLTHRNL---VTQNYMANKLLPifREDVFLSILPLSHayecSLGLILplsrgaqvvylhgaptpsL 238
Cdd:PRK12476 198 LQYTSGSTRPPVGVEITHRAVgtnLVQMILSIDLLD--RNTHGVSWLPLYH----DMGLSM------------------I 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 239 LLPAL-----TQVRPTIMLSVPL--IVEKIYKNKIRPMFTKTwiTQFLYSISfIRRALHKvAGKKLcqtfggNLRFFG-I 310
Cdd:PRK12476 254 GFPAVygghsTLMSPTAFVRRPQrwIKALSEGSRTGRVVTAA--PNFAYEWA-AQRGLPA-EGDDI------DLSNVVlI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 311 GGSKLDGV--VEKFlaDAGF-PYGI-------GYGLTETSPLLA---------------------------GAIPGKVKW 353
Cdd:PRK12476 324 IGSEPVSIdaVTTF--NKAFaPYGLprtafkpSYGIAEATLFVAtiapdaepsvvyldreqlgagravrvaADAPNAVAH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 354 QSTGPKLPDIEMKILNPNHK------KIGEIVVKGPNVMSGYYKDPVTTASCF----------------TEDG--WFRTK 409
Cdd:PRK12476 402 VSCGQVARSQWAVIVDPDTGaelpdgEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgAADDgtWLRTG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1309054211 410 DLG-YIDknGNLYIKGR-KDnmMVGANGENIYPEEIEATINE 449
Cdd:PRK12476 482 DLGvYLD--GELYITGRiAD--LIVIDGRNHYPQDIEATVAE 519
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
123-459 |
8.07e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 74.03 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 123 SLLDSLKLVIS-MDTLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLThRNLVTQNY--MANKLLPIFRED 199
Cdd:PRK05851 117 SHLERLRAVDSsVTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILS-PGAVLSNLrgLNARVGLDAATD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 200 VFLSILPLSHayecSLGLILPLSRGAQVVYLHGAPT------PSLLLPALTQVRPTImlsvplivekiyknkirpmftkT 273
Cdd:PRK05851 196 VGCSWLPLYH----DMGLAFLLTAALAGAPLWLAPTtafsasPFRWLSWLSDSRATL----------------------T 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 274 WITQFLYSIsfIRRALHKVAGKKLcqtfgGNLRFFGIGGSKLDGVVEKFLADAGFPYGI-------GYGLTETSPLLAGA 346
Cdd:PRK05851 250 AAPNFAYNL--IGKYARRVSDVDL-----GALRVALNGGEPVDCDGFERFATAMAPFGFdagaaapSYGLAESTCAVTVP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 347 IPG---------------KVKWQSTGPKLPDIEMKILNPNH------KKIGEIVVKGPNVMSGYYKDPVTTAscfteDGW 405
Cdd:PRK05851 323 VPGiglrvdevttddgsgARRHAVLGNPIPGMEVRISPGDGaagvagREIGEIEIRGASMMSGYLGQAPIDP-----DDW 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 406 FRTKDLGYIdKNGNLYIKGRKDNMMVGAnGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK05851 398 FPTGDLGYL-VDGGLVVCGRAKELITVA-GRNIFPTEIERVAAQVRGVREGAVV 449
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
33-459 |
8.57e-14 |
|
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: 73.44 E-value: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAfeivnviehsessvviv 112
Cdd:cd17652 11 ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPA----------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 sEKLHYKLSASlldSLKLVISMdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKL 192
Cdd:cd17652 74 -ERIAYMLADA---RPALLLTT---------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 193 LPIFREDVFLSILPLS---HAYECSLGLilpLSRGAQVVylhgaPTPSLLLP------ALTQVRPTIMLSVPLIVEKIYK 263
Cdd:cd17652 129 FDVGPGSRVLQFASPSfdaSVWELLMAL---LAGATLVL-----APAEELLPgepladLLREHRITHVTLPPAALAALPP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 264 NKIRPmftktwitqflysisfiRRALhKVAGK----KLCQTFGGNLRFFGiggskldgvvekfladagfpygiGYGLTET 339
Cdd:cd17652 201 DDLPD-----------------LRTL-VVAGEacpaELVDRWAPGRRMIN-----------------------AYGPTET 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 340 S-------PLLAGAIPgkvkwqSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFTEDGW-- 405
Cdd:cd17652 240 TvcatmagPLPGGGVP------PIGRPVPGTRVYVLDARLRPvppgvPGELYIAGAGLARGYLNRPGLTAERFVADPFga 313
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309054211 406 -----FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17652 314 pgsrmYRTGDLARWRADGQLEFLGRADD-QVKIRGFRIELGEVEAALTEHPGVAEAVVV 371
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
35-535 |
2.50e-13 |
|
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: 72.52 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYK-----LSASLLDSLKLVISMDTLEVIKSAGEQDYTLNELPR-----------------PEDLASIIYTSGTSGAS 172
Cdd:cd05968 172 GFTRRgrevnLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLsydeeketagdgaerteSEDPLMIIYTSGTTGKP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 173 KGVMLTHRNL-VTQNYMANKLLPIFREDVFLSILPLSHAYECSL---GLILplsrGAQVVYLHGAP---TPSLLLPALTQ 245
Cdd:cd05968 252 KGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLifgGLIL----GATMVLYDGAPdhpKADRLWRMVED 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 246 VRPTIMLSVPLIVEkiyknkirpmftktwitqflysiSFIRRALHKVAGKKLCQtfggnLRFFGIGGSKLDG-----VVE 320
Cdd:cd05968 328 HEITHLGLSPTLIR-----------------------ALKPRGDAPVNAHDLSS-----LRVLGSTGEPWNPepwnwLFE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 321 KFLADAgFPYgIGY-GLTETSPLLAGAIPGK-VKWQSTGPKLPDIEMKIL----NPNHKKIGEIVVKGP--NVMSGYYKD 392
Cdd:cd05968 380 TVGKGR-NPI-INYsGGTEISGGILGNVLIKpIKPSSFNGPVPGMKADVLdesgKPARPEVGELVLLAPwpGMTRGFWRD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 393 P---VTTASCFTEDGWFRtKDLGYIDKNGNLYIKGRKDNMMVGAnGENIYPEEIEATINEHDMVLESLVV----NTKGkl 465
Cdd:cd05968 458 EdryLETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVA-GKRVGPAEIESVLNAHPAVLESAAIgvphPVKG-- 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054211 466 vamvhfnyeqiEKLHTFN-EEAEVNMTqrvEEVKKELMEYVNSRVNKSSKILEILEQSSpFEKTATQKIKR 535
Cdd:cd05968 534 -----------EAIVCFVvLKPGVTPT---EALAEELMERVADELGKPLSPERILFVKD-LPKTRNAKVMR 589
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
102-458 |
2.80e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 72.37 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 102 IEHSESSVVIVsEKLHyklsASLLDSLKL----VISMDTLEVI-KSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVM 176
Cdd:PRK13388 95 IRRADCQLLVT-DAEH----RPLLDGLDLpgvrVLDVDTPAYAeLVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 177 LTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTIM----- 251
Cdd:PRK13388 170 CSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVA-LPAKFSASGFLDDVRRYGATYFnyvgk 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 252 -----LSVPLIVEKIyKNKIRPMF----TKTWITQFlysisfIRRalhkvagkklcqtFGGNLrFFGIGGSKLDGVVekf 322
Cdd:PRK13388 249 playiLATPERPDDA-DNPLRVAFgneaSPRDIAEF------SRR-------------FGCQV-EDGYGSSEGAVIV--- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 323 LADAGFPYG-IGYGltetspllagaIPGKVKWQS-TGPKLP----DIEMKILNPNhKKIGEIVVK-GPNVMSGYYKDPVT 395
Cdd:PRK13388 305 VREPGTPPGsIGRG-----------APGVAIYNPeTLTECAvarfDAHGALLNAD-EAIGELVNTaGAGFFEGYYNNPEA 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 396 TASCFtEDGWFRTKDLGYIDKNGNLYIKGRK-DNMMVgaNGENIYPEEIEATINEHDMVLESLV 458
Cdd:PRK13388 373 TAERM-RHGMYWSGDLAYRDADGWIYFAGRTaDWMRV--DGENLSAAPIERILLRHPAINRVAV 433
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-459 |
2.94e-13 |
|
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: 71.83 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 51 LNKHGVKKGEKVAI-LGNNMPNWAVSYFAITTSSrVVVPILPDFTAFEIVNVIEHSESSVVIVSEKLHyklsaslldslk 129
Cdd:cd05974 17 LRSIGVGRGDRILLmLGNVVELWEAMLAAMKLGA-VVIPATTLLTPDDLRDRVDRGGAVYAAVDENTH------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 130 lvismdtleviksageqdytlnelprPEDLASIIYTSGTSGASKGVMLTHRNlvtqnYMANKLLPIF-----REDVFLSI 204
Cdd:cd05974 84 --------------------------ADDPMLLYFTSGTTSKPKLVEHTHRS-----YPVGHLSTMYwiglkPGDVHWNI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 205 LP---LSHAYECslgLILPLSRGAQV-VYLHGAPTPSLLLPALTQVRPTIMLSVPLIVEkiyknkirpMFTKTWITQFly 280
Cdd:cd05974 133 SSpgwAKHAWSC---FFAPWNAGATVfLFNYARFDAKRVLAALVRYGVTTLCAPPTVWR---------MLIQQDLASF-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 281 sisfiRRALHKVAGkklcqtfggnlrffgiGGSKLD-GVVEKFLADAGFPYGIGYGLTETSpLLAGAIPGK-VKWQSTGP 358
Cdd:cd05974 199 -----DVKLREVVG----------------AGEPLNpEVIEQVRRAWGLTIRDGYGQTETT-ALVGNSPGQpVKAGSMGR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 359 KLPDIEMKILNP--NHKKIGEIVV-----KGPNVMSGYYKDPVTTASCFtEDGWFRTKDLGYIDKNGNLYIKGRKDNMMv 431
Cdd:cd05974 257 PLPGYRVALLDPdgAPATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVF- 334
|
410 420
....*....|....*....|....*...
gi 1309054211 432 GANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd05974 335 KSSDYRISPFELESVLIEHPAVAEAAVV 362
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
364-459 |
6.58e-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: 70.87 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 364 EMKILNPNHKK-----IGEIVVKGPNVmSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENI 438
Cdd:cd05929 306 KVHILDEDGNEvppgeIGEVYFANGPG-FEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMII-SGGVNI 383
|
90 100
....*....|....*....|.
gi 1309054211 439 YPEEIEATINEHDMVLESLVV 459
Cdd:cd05929 384 YPQEIENALIAHPKVLDAAVV 404
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
26-466 |
1.78e-12 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 69.68 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 26 AFSLIN-KEK----LTYREFGDSVEHLTE-ILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIV 99
Cdd:cd05905 1 AYTLLDsKGKeattLTWGKLLSRAEKIAAvLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 100 NVIEHSESSVVIVSEKLHYKLSASLLDSLKLVISMD-----------TLEVIKSAGEQDYTLNELPRPEDLASIIYTSGT 168
Cdd:cd05905 81 FLLGTCKVRVALTVEACLKGLPKKLLKSKTAAEIAKkkgwpkildfvKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 169 SGASKGVMLTHRNLVTQnyMAN-KLLPIFRE-DVFLSILPLShayeCSLGLILPLSRGaqvVYLhGAPTpsLLLPaltqv 246
Cdd:cd05905 161 DGSLSGVAVSHSSLLAH--CRAlKEACELYEsRPLVTVLDFK----SGLGLWHGCLLS---VYS-GHHT--ILIP----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 247 rPTIMLSVP-LIVEKIYKNKIRPMFTKT----WITQFL---------YSISFIR-RALHKVAGKK----LCQTFggnLRF 307
Cdd:cd05905 224 -PELMKTNPlLWLQTLSQYKVRDAYVKLrtlhWCLKDLsstlaslknRDVNLSSlRMCMVPCENRprisSCDSF---LKL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 308 FGIGGSKLDGVVEKFL----------ADAGFPYGIGY----GLTETSPLLAGA-IPGKVKWQSTGPKLPDIEMKILNPNH 372
Cdd:cd05905 300 FQTLGLSPRAVSTEFGtrvnpficwqGTSGPEPSRVYldmrALRHGVVRLDERdKPNSLPLQDSGKVLPGAQVAIVNPET 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 373 K------KIGEIVVKGPNVMSGYY----------KDPVTTASCF--TEDGWFRTKDLGYI----------DKNGNLYIKG 424
Cdd:cd05905 380 KglckdgEIGEIWVNSPANASGYFlldgetndtfKVFPSTRLSTgiTNNSYARTGLLGFLrptkctdlnvEEHDLLFVVG 459
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1309054211 425 RKDNMMVgANGENIYPEEIEATINE-HDMVLESLVVNTKGKLV 466
Cdd:cd05905 460 SIDETLE-VRGLRHHPSDIEATVMRvHPYRGRCAVFSITGLVV 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-469 |
1.97e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.37 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSaslLDSLKLVISMD--TLEViksAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVtqNYMaN 190
Cdd:PRK12316 615 QSHLGRKLP---LAAGVQVLDLDrpAAWL---EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALS--NRL-C 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 KLLPIFREDVFLSIL-PLSHAYECSL-GLILPLSRGAQvvyLHGAP-----TPSLLLPALTQVRPTIMLSVPLIVEkiyk 263
Cdd:PRK12316 686 WMQQAYGLGVGDTVLqKTPFSFDVSVwEFFWPLMSGAR---LVVAApgdhrDPAKLVELINREGVDTLHFVPSMLQ---- 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 264 nkirpmftktwitqflysisfirrALHKVAGKKLCQTfggnLRFFGIGGSKLDGV----VEKFLADAGFpYGIgYGLTET 339
Cdd:PRK12316 759 ------------------------AFLQDEDVASCTS----LRRIVCSGEALPADaqeqVFAKLPQAGL-YNL-YGPTEA 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 340 SPLL---------AGAIPgkvkwqsTGPKLPDIEMKILNPNHKKI-----GEIVVKGPNVMSGYYKDPVTTASCFTEDGW 405
Cdd:PRK12316 809 AIDVthwtcveegGDSVP-------IGRPIANLACYILDANLEPVpvgvlGELYLAGRGLARGYHGRPGLTAERFVPSPF 881
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054211 406 ------FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKGK-LVAMV 469
Cdd:PRK12316 882 vagermYRTGDLARYRADGVIEYAGRIDH-QVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKqLVGYV 951
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-469 |
2.17e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.19 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK12467 1598 QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKL-SASLLDSLKLVISMDTLEviksaGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANK 191
Cdd:PRK12467 1678 QSHLQARLpLPDGLRSLVLDQEDDWLE-----GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQE 1752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 192 LLPIFREDVFLSILPlsHAYECSL-GLILPLSRGAQVVYlhgaptpslllpaltqVRPTIMLSVPLIVEKIYKNKIRPM- 269
Cdd:PRK12467 1753 AYQLSAADVVLQFTS--FAFDVSVwELFWPLINGARLVI----------------APPGAHRDPEQLIQLIERQQVTTLh 1814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 270 FTKTWITQFLYSISFIRRALhkvagkklcqtfggNLRFFGIGGSKL-----DGVVEKFLADAGFPygiGYGLTETS---- 340
Cdd:PRK12467 1815 FVPSMLQQLLQMDEQVEHPL--------------SLRRVVCGGEALevealRPWLERLPDTGLFN---LYGPTETAvdvt 1877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 341 --PLLAGAIPGKVkWQSTGPKLPDIEMKI----LNPNHKK-IGEIVVKGPNVMSGYYKDPVTTASCFTEDGW-------F 406
Cdd:PRK12467 1878 hwTCRRKDLEGRD-SVPIGQPIANLSTYIldasLNPVPIGvAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlY 1956
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309054211 407 RTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVVNTKG----KLVAMV 469
Cdd:PRK12467 1957 RTGDLARYRADGVIEYLGRIDH-QVKIRGFRIELGEIEARLREQGGVREAVVIAQDGangkQLVAYV 2022
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
38-445 |
3.81e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 68.57 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 38 REFGDSVEHLTEI---LNKHGVKKGEKVAIL-GNNMPNWAVSYFAITTSSrVVVPILPDFTAFEIVNVIEHSESSVVIVS 113
Cdd:PRK12406 12 RSFDELAQRAARAaggLAALGVRPGDCVALLmRNDFAFFEAAYAAMRLGA-YAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 114 EKLHYKLsASLLDSLKLVISMDTLEVIKSA------------GEQDY-------TLNELPRPEDLASIIYTSGTSGASKG 174
Cdd:PRK12406 91 ADLLHGL-ASALPAGVTVLSVPTPPEIAAAyrispalltppaGAIDWegwlaqqEPYDGPPVPQPQSMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 175 VML---THRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILplSRGAQVVYLHGAPTPSLLLPALTQVRPTIM 251
Cdd:PRK12406 170 VRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRA--GRLGGVLVLQPRFDPEELLQLIERHRITHM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 252 LSVPLIVEKIYK--NKIRPMftktwitqflYSISFIRRALHKVA------GKKLCQTFGGnlrffgiggskldgVVEKFl 323
Cdd:PRK12406 248 HMVPTMFIRLLKlpEEVRAK----------YDVSSLRHVIHAAApcpadvKRAMIEWWGP--------------VIYEY- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 324 adagfpygigYGLTETSPLL------AGAIPGKVkwqstGPKLPDIEMKILNPNHK-----KIGEIVVKGP-NVMSGYYK 391
Cdd:PRK12406 303 ----------YGSTESGAVTfatsedALSHPGTV-----GKAAPGAELRFVDEDGRplpqgEIGEIYSRIAgNPDFTYHN 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1309054211 392 DPVTTAScFTEDGWFRTKDLGYIDKNGNLYIKGRKDNMMVgANGENIYPEEIEA 445
Cdd:PRK12406 368 KPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVI-SGGVNIYPAEIEA 419
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
358-468 |
6.24e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 64.63 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 358 PKLPDIEMKILNPN-----HKKIGEIVVKGPNVMSGYYKDPVTTASCFTEDGWFRTKDLGYIDKNGNLYIKGR-KDNMMV 431
Cdd:PRK10946 358 PMSPDDEVWVADADgnplpQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGReKDQINR 437
|
90 100 110
....*....|....*....|....*....|....*..
gi 1309054211 432 GanGENIYPEEIEATINEHDMVLESlvvntkgKLVAM 468
Cdd:PRK10946 438 G--GEKIAAEEIENLLLRHPAVIHA-------ALVSM 465
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
157-459 |
9.80e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 63.53 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 157 EDLASIIYTSGTSGASKGVMLTHRNLV-----TQNYMANkllpifrEDVFLSILPLSHAyecslglilplsRGAQVvylh 231
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTasadaTHDRLGG-------PGQWLLALPAHHI------------AGLQV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 232 gaptpsLLLPALTQVRPTIM-----LSVPLIVEKIYKNKIRPMFTKTWITQFLysisfirRALHKVAGKKLCQTFGGNLr 306
Cdd:PRK07824 92 ------LVRSVIAGSEPVELdvsagFDPTALPRAVAELGGGRRYTSLVPMQLA-------KALDDPAATAALAELDAVL- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 307 ffgIGGSKLDGVVEKFLADAGFPYGIGYGLTETSpllAGAIpgkvkwqSTGPKLPDIEMKILNpnhkkiGEIVVKGPNVM 386
Cdd:PRK07824 158 ---VGGGPAPAPVLDAAAAAGINVVRTYGMSETS---GGCV-------YDGVPLDGVRVRVED------GRIALGGPTLA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309054211 387 SGYyKDPVTTAScFTEDGWFRTKDLGYIDkNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK07824 219 KGY-RNPVDPDP-FAEPGWFRTDDLGALD-DGVLTVLGRADD-AISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
156-459 |
1.94e-10 |
|
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: 63.19 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 156 PEDLASIIYTSGTSGASKGVMLTHR---NLVTQ---------------NYMANKLLPIFREDVFLSILP------LSHAY 211
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGsvvNLRTSlseryfgrdngdeavLFFSNYVFDFFVEQMTLALLNgqklvvPPDEM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 212 ECSLGLILPLSRGAQVVYLHGapTPSLLlpaltqvrptimlsvpliveKIYKNKIRPMftktwitqfLYSISFIRRALHK 291
Cdd:cd17648 173 RFDPDRFYAYINREKVTYLSG--TPSVL--------------------QQYDLARLPH---------LKRVDAAGEEFTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 292 VAGKKLCQTFGGnlrffgiggskldgvvekfladagfPYGIGYGLTETS--PLLAGAIPGKVKWQSTGPKLPDIEMKILN 369
Cdd:cd17648 222 PVFEKLRSRFAG-------------------------LIINAYGPTETTvtNHKRFFPGDQRFDKSLGRPVRNTKCYVLN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 370 PNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFTEDGW--------------FRTKDLGYIDKNGNLYIKGRKDnMM 430
Cdd:cd17648 277 DAMKRvpvgaVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRND-FQ 355
|
330 340
....*....|....*....|....*....
gi 1309054211 431 VGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:cd17648 356 VKIRGQRIEPGEVEAALASYPGVRECAVV 384
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-469 |
3.66e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 61.63 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 154 PRPEDLAsIIYTSGTSGASKGVMLTH----------RNLVTQNYMANKLLPIFRED----VFLSILPLSHAYECSLGLIL 219
Cdd:cd05924 1 RSADDLY-ILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTPSEDAHKAAAAaagtVMFPAPPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 220 PLsrGAQVVYLHGAP-TPSLLLPALTQVRPTIMLSV------PLIvEKIYKNKIRPMFTktwitqfLYSISFIRRALHKV 292
Cdd:cd05924 80 LL--GGQTVVLPDDRfDPEEVWRTIEKHKVTSMTIVgdamarPLI-DALRDAGPYDLSS-------LFAISSGGALLSPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 293 AGKKLCQTFGGNLRFFGIGGSkldgvvekflaDAGFpygIGYGLTetspllAGAIPGKVKWQSTGPK--LPDIEMKILNP 370
Cdd:cd05924 150 VKQGLLELVPNITLVDAFGSS-----------ETGF---TGSGHS------AGSGPETGPFTRANPDtvVLDDDGRVVPP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 371 NHKKIGEIVVKGpNVMSGYYKDPVTTASCFTE-DG--WFRTKDLGYIDKNGNLYIKGRkDNMMVGANGENIYPEEIEATI 447
Cdd:cd05924 210 GSGGVGWIARRG-HIPLGYYGDEAKTAETFPEvDGvrYAVPGDRATVEADGTVTLLGR-GSVCINTGGEKVFPEEVEEAL 287
|
330 340
....*....|....*....|....*.
gi 1309054211 448 NEHDMVLESLVVNTK----GKLVAMV 469
Cdd:cd05924 288 KSHPAVYDVLVVGRPderwGQEVVAV 313
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
35-482 |
6.77e-10 |
|
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: 61.33 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 35 LTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVSE 114
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLsaslLDSLKLVISMDtleviksageqdytlneLPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLP 194
Cdd:cd17654 97 ELDNAP----LSFTPEHRHFN-----------------IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 195 IFREDVFLSILPLShaYECS-LGLILPLSRGAQVVY--LHGAPTPSLLLPALTQV-RPTIMLSVPLIVEkiyknkirpMF 270
Cdd:cd17654 156 ITSEDILFLTSPLT--FDPSvVEIFLSLSSGATLLIvpTSVKVLPSKLADILFKRhRITVLQATPTLFR---------RF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 271 TKTWITQFLYSISfirralhkvagkklcqtfgGNLRFFGIGGSKLDGVVEKFLADAGFP----YGIgYGLTETSpllAGA 346
Cdd:cd17654 225 GSQSIKSTVLSAT-------------------SSLRVLALGGEPFPSLVILSSWRGKGNrtriFNI-YGITEVS---CWA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 347 IPGKVKWQSTGPKL--PDIEMKIL---NPNHKKIGEIVVKGPNVMsGYYKDPVTTAscftEDGWFRTKDLGYIdKNGNLY 421
Cdd:cd17654 282 LAYKVPEEDSPVQLgsPLLGTVIEvrdQNGSEGTGQVFLGGLNRV-CILDDEVTVP----KGTMRATGDFVTV-KDGELF 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054211 422 IKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVvntkgklvamvhfNYEQIEKLHTF 482
Cdd:cd17654 356 FLGRKDS-QIKRRGKRINLDLIQQVIESCLGVESCAV-------------TLSDQQRLIAF 402
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
33-458 |
1.69e-09 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 60.06 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSrvVVPILpdftafeivnviehsessvviv 112
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIG--AVAAL---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 sekLHYKLSA-SLLDSLKLVismDTLEVIKsageqdytlnelprpeDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANK 191
Cdd:cd05940 58 ---INYNLRGeSLAHCLNVS---SAKHLVV----------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 192 LLPIFREDVFLSILPLSHAYECSLGLILPLSRGAQVVyLHGAPTPSLLLPALTQVRPTI----------MLSVPLI---- 257
Cdd:cd05940 116 SGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLV-IRKKFSASNFWDDIRKYQATIfqyigelcryLLNQPPKpter 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 258 ---VEKIYKNKIRPMFTKTWITQFlysisfirralhKVAgkKLCQTFG---GNLRFFGIGGSklDGVV--EKFLADAGFP 329
Cdd:cd05940 195 khkVRMIFGNGLRPDIWEEFKERF------------GVP--RIAEFYAateGNSGFINFFGK--PGAIgrNPSLLRKVAP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 330 YGIGYGLTETSPLLAGAiPGKVKwqstgpKLPDIEMKILnpnhkkIGEIVVKGPnvMSGYYKDPVTTAS----CFTE-DG 404
Cdd:cd05940 259 LALVKYDLESGEPIRDA-EGRCI------KVPRGEPGLL------ISRINPLEP--FDGYTDPAATEKKilrdVFKKgDA 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309054211 405 WFRTKDLGYIDKNGNLYIKGRkdnmmVGAN----GENIYPEEIEATINEHDMVLESLV 458
Cdd:cd05940 324 WFNTGDLMRLDGEGFWYFVDR-----LGDTfrwkGENVSTTEVAAVLGAFPGVEEANV 376
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
34-228 |
5.44e-09 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 59.29 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 34 KLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIVS 113
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 114 eklhyklsASLLDSLKLVISMDTLEVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVtqnymaNKLL 193
Cdd:PRK10252 563 --------ADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV------NRLL 628
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1309054211 194 ------PIFREDVFLSILPLShaYECSL-GLILPLSRGAQVV 228
Cdd:PRK10252 629 wmqnhyPLTADDVVLQKTPCS--FDVSVwEFFWPFIAGAKLV 668
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-475 |
6.86e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.02 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT 3198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SeklhyklsASLLDSLKLVISMDTLEVIKSA--GEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMAN 190
Cdd:PRK12467 3199 Q--------AHLLEQLPAPAGDTALTLDRLDlnGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIA 3270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 191 KLLPIFREDVFLSILPLSH--AYECSLGlilPLSRGAQVVYLHGAP-TPSLLLPALTQVRPTIMLSVPlivekiyknkir 267
Cdd:PRK12467 3271 EAYELDANDRVLLFMSFSFdgAQERFLW---TLICGGCLVVRDNDLwDPEELWQAIHAHRISIACFPP------------ 3335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 268 pmftkTWITQFLysisfirrALHKVAGkklcqtfGGNLRFFGIGGSKL-DGVVEKFLADAGfPYGI--GYGLTET--SPL 342
Cdd:PRK12467 3336 -----AYLQQFA--------EDAGGAD-------CASLDIYVFGGEAVpPAAFEQVKRKLK-PRGLtnGYGPTEAvvTVT 3394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 343 L----AGAIPGKVkWQSTGPKLPDIEMKILNPNHKK-----IGEIVVKGPNVMSGYYKDPVTTASCFTEDGW-------F 406
Cdd:PRK12467 3395 LwkcgGDAVCEAP-YAPIGRPVAGRSIYVLDGQLNPvpvgvAGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlY 3473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309054211 407 RTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV---NTKGK-LVAMVHFNYEQ 475
Cdd:PRK12467 3474 RTGDLARYRADGVIEYLGRIDH-QVKIRGFRIELGEIEARLLQHPSVREAVVLardGAGGKqLVAYVVPADPQ 3545
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
161-455 |
1.26e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 54.36 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 161 SIIYTSGTSGASKGVMLTH-RNLVTQNYMANKLLPIFREDVFLSilplsHAyecSLGLILplsrgaqvvyLHGAPTPSLL 239
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNgPHLVGLKYYWRSIIEKDIPTVVFS-----HS---SIGWVS----------FHGFLYGSLS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 240 LPaltqvRPTIMLSVPLIVEKIYKNKIRPMFTKTWITQFLYSISFIRRaLHKV--AGKKLCQTFG-GNLRFFGIGGSKLD 316
Cdd:PTZ00237 320 LG-----NTFVMFEGGIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRY-LIKTdpEATIIRSKYDlSNLKEIWCGGEVIE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 317 GVVEKFLADA-GFPYGIGYGLTETS-PLLAGAIPGKVKWQSTGPKLPDIEMKILNPNHK-----KIGEIVVK---GPNVM 386
Cdd:PTZ00237 394 ESIPEYIENKlKIKSSRGYGQTEIGiTYLYCYGHINIPYNATGVPSIFIKPSILSEDGKelnvnEIGEVAFKlpmPPSFA 473
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 387 SGYYKDPVTTASCFTE-DGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLE 455
Cdd:PTZ00237 474 TTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDD-QIKISGNKVQLNTIETSILKHPLVLE 542
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
8-210 |
1.49e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 54.11 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 8 LSLADIYSRSLVDFSEQTAFsLINKEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITtssRV-V 86
Cdd:PRK08279 37 RSLGDVFEEAAARHPDRPAL-LFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLA---KLgA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 87 VpilpdfTAFeiVN------VIEHS----ESSVVIVSEKL--HYKLSASLLDSLKLVISMDTLEVIKSAGEQDY-TLNEL 153
Cdd:PRK08279 113 V------VAL--LNtqqrgaVLAHSlnlvDAKHLIVGEELveAFEEARADLARPPRLWVAGGDTLDDPEGYEDLaAAAAG 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 154 PRPEDLAS-----------IIYTSGTSGASKGVMLTHRNlvTQNYMA--NKLLPIFREDVFLSILPLSHA 210
Cdd:PRK08279 185 APTTNPASrsgvtakdtafYIYTSGTTGLPKAAVMSHMR--WLKAMGgfGGLLRLTPDDVLYCCLPLYHN 252
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-239 |
2.15e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVIV 112
Cdd:PRK05691 1155 GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 SEKLHYKLSASLLDSlklVISMDTLEvIKSAGEQDYTLNElpRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKL 192
Cdd:PRK05691 1235 QSHLLERLPQAEGVS---AIALDSLH-LDSWPSQAPGLHL--HGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQAT 1308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309054211 193 LPIFREDVFLSILPLS---HAYECSLGLI----LPLS---------RGAQVVYLHGAPT----PSLL 239
Cdd:PRK05691 1309 YALDDSDVLMQKAPISfdvSVWECFWPLItgcrLVLAgpgehrdpqRIAELVQQYGVTTlhfvPPLL 1375
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
36-228 |
3.56e-07 |
|
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: 52.82 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 36 TYREFGDSVEHLTEILNK-HGVKKGEKVAILGNNMPNWAVSYFAIttssrvvvpilpdftafeivnviehseSSVVIVSE 114
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGL---------------------------WSIGAAPA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 115 KLHYKLS-ASLLDSLKlvISMDTLEVIKsageqdytlnelprPEDLASIIYTSGTSGASKGVMLT-HRNLVTQNYMANKL 192
Cdd:cd05937 60 FINYNLSgDPLIHCLK--LSGSRFVIVD--------------PDDPAILIYTSGTTGLPKAAAISwRRTLVTSNLLSHDL 123
|
170 180 190
....*....|....*....|....*....|....*.
gi 1309054211 193 LPIFrEDVFLSILPLSHAYECSLGLILPLSRGAQVV 228
Cdd:cd05937 124 NLKN-GDRTYTCMPLYHGTAAFLGACNCLMSGGTLA 158
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
144-458 |
3.13e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 49.65 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 144 GEQDYTLNELPR--PEDLASIIYTSGTSGASKGVMLTHRNLVTQNYMANKLLPIFREDVFLSILPLSHAYECSLGLILPL 221
Cdd:PRK08308 86 GESDFTKLEAVNylAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 222 SRGAQVVYLhGAPTPSLLLPALTQVRPTIMLSVPLivekiyknkirpmftktwitqFLYSISFIRRA---LHKV--AGKK 296
Cdd:PRK08308 166 TRGSKPVII-TNKNPKFALNILRNTPQHILYAVPL---------------------MLHILGRLLPGtfqFHAVmtSGTP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 297 LCQTFGGNLRffgiggSKLDGVVEKfladagfpygigYGLTEtspllAGAI---PGKVKWQSTGPKLPDIEMKIlNPNHK 373
Cdd:PRK08308 224 LPEAWFYKLR------ERTTYMMQQ------------YGCSE-----AGCVsicPDMKSHLDLGNPLPHVSVSA-GSDEN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 374 KIGEIVVKgpnvmsgyykdpvttascfTEDGWFRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMV 453
Cdd:PRK08308 280 APEEIVVK-------------------MGDKEIFTKDLGYKSERGTLHFMGRMDD-VINVSGLNVYPIEVEDVMLRLPGV 339
|
....*
gi 1309054211 454 LESLV 458
Cdd:PRK08308 340 QEAVV 344
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-504 |
7.07e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAIL---GNNMPNWAVSYFAITTSsrvVVPILPDFTAFEIVNVIEHSESSV 109
Cdd:PRK05691 3744 QQWSYAELNRAANRLGHALRAAGVGVDQPVALLaerGLDLLGMIVGSFKAGAG---YLPLDPGLPAQRLQRIIELSRTPV 3820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 110 VIVSEKLHyKLSASLLDSLKLVISMDTL--EVIKSAGEQDYTLNELPRPEDLASIIYTSGTSGASKGVMLTHRNLVTQNY 187
Cdd:PRK05691 3821 LVCSAACR-EQARALLDELGCANRPRLLvwEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQL 3899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 188 MANKLLPIFREDVFLSILplSHAYECSLGLIL--PLSrGAQVVYLHG--APTPSLLLPALTQVRPTIMLSVPLIVEKIYK 263
Cdd:PRK05691 3900 SKVPYLALSEADVIAQTA--SQSFDISVWQFLaaPLF-GARVEIVPNaiAHDPQGLLAHVQAQGITVLESVPSLIQGMLA 3976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 264 NKIRPMFTKTWI--TQFLYSISFIRRALhkvagkklcqtfggnLRFFGIGgskldgvvekfLADAgfpygigYGLTETSP 341
Cdd:PRK05691 3977 EDRQALDGLRWMlpTGEAMPPELARQWL---------------QRYPQIG-----------LVNA-------YGPAECSD 4023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 342 LLAGAipgKVKWQST-GPKLPdiemkILNP--NHK--------------KIGEIVVKGPNVMSGYYKDPVTTASCFTEDG 404
Cdd:PRK05691 4024 DVAFF---RVDLASTrGSYLP-----IGSPtdNNRlylldealelvplgAVGELCVAGTGVGRGYVGDPLRTALAFVPHP 4095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 405 W-------FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLV-----VNTK---GKLVAmv 469
Cdd:PRK05691 4096 FgapgerlYRTGDLARRRSDGVLEYVGRIDH-QVKIRGYRIELGEIEARLHEQAEVREAAVavqegVNGKhlvGYLVP-- 4172
|
490 500 510
....*....|....*....|....*....|....*....
gi 1309054211 470 hfnyeqieklhtfnEEAEVNMTQRVEEVKK----ELMEY 504
Cdd:PRK05691 4173 --------------HQTVLAQGALLERIKQrlraELPDY 4197
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
33-228 |
1.09e-05 |
|
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: 48.06 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKH-GVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVI 111
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VSeklhyklsASLLDSLKLVISM---DTLEV-----------IKSAGEQDYTLNELPRPEDL---------ASIIYTSGT 168
Cdd:cd05938 84 VA--------PELQEAVEEVLPAlraDGVSVwylshtsntegVISLLDKVDAASDEPVPASLrahvtikspALYIYTSGT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309054211 169 SGASKGVMLTHRNLVtqnyMANKLLPIF---REDVFLSILPLSHAYECSLGLILPLSRGAQVV 228
Cdd:cd05938 156 TGLPKAARISHLRVL----QCSGFLSLCgvtADDVIYITLPLYHSSGFLLGIGGCIELGATCV 214
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-459 |
2.20e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.47 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 33 EKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAfeivnviehsessvviv 112
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL----------------- 2274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 113 sEKLHYKLSAS----LLDSLKLVISMDTL--EVIKSAGEQD------YTLNELPR---PEDLASIIYTSGTSGASKGVML 177
Cdd:PRK05691 2275 -ERLHYMIEDSgiglLLSDRALFEALGELpaGVARWCLEDDaaalaaYSDAPLPFlslPQHQAYLIYTSGSTGKPKGVVV 2353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 178 THRNLVTQNYMANKLLPIFREDVFLsilplsHAYE-----CSLGLILPLSRGAQVVylhgaptpslllpaltqVRPTIML 252
Cdd:PRK05691 2354 SHGEIAMHCQAVIERFGMRADDCEL------HFYSinfdaASERLLVPLLCGARVV-----------------LRAQGQW 2410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 253 SVPLIVEKIYKNKIRPM-FTKTW---ITQFLYSisfiRRALHKVagkKLCQTFGGNLRffgigGSKLDGVVEKFLADAGF 328
Cdd:PRK05691 2411 GAEEICQLIREQQVSILgFTPSYgsqLAQWLAG----QGEQLPV---RMCITGGEALT-----GEHLQRIRQAFAPQLFF 2478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 329 PygiGYGLTET--SPLL----------AGAIP-GKVKWQSTGPKLpDIEMKILnPnHKKIGEIVVKGPNVMSGYYKDPVT 395
Cdd:PRK05691 2479 N---AYGPTETvvMPLAclapeqleegAASVPiGRVVGARVAYIL-DADLALV-P-QGATGELYVGGAGLAQGYHDRPGL 2552
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054211 396 TASCFTEDGW-------FRTKDLGYIDKNGNLYIKGRKDNmMVGANGENIYPEEIEATINEHDMVLESLVV 459
Cdd:PRK05691 2553 TAERFVADPFaadggrlYRTGDLVRLRADGLVEYVGRIDH-QVKIRGFRIELGEIESRLLEHPAVREAVVL 2622
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
334-469 |
4.67e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 42.83 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 334 YGLTETSPLLAGAIPGKvkwqsTGPKLPD----IEmkILNPNHKK------IGEIVVkgpnvmsgyykdpvTTascFTED 403
Cdd:COG1541 235 YGLTEVGPGVAYECEAQ-----DGLHIWEdhflVE--IIDPETGEpvpegeEGELVV--------------TT---LTKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 404 GW----FRTKDLGYIDkNGN----------LYIKGRKDNMMVgANGENIYPEEIEATINEHDMVLES--LVVNTKGKLVA 467
Cdd:COG1541 291 AMplirYRTGDLTRLL-PEPcpcgrthpriGRILGRADDMLI-IRGVNVFPSQIEEVLLRIPEVGPEyqIVVDREGGLDE 368
|
..
gi 1309054211 468 MV 469
Cdd:COG1541 369 LT 370
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
32-179 |
9.51e-04 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 41.87 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 32 KEKLTYREFGDSVEHLTEILNKHGVKKGEKVAILGNNMPNWAVSYFAITTSSRVVVPILPDFTAFEIVNVIEHSESSVVI 111
Cdd:cd05943 96 RTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054211 112 VSEKLHYK------------LSASLLDSLKLVISMDTLevikSAGEQDY-------TLNELPRPEDLAS----------- 161
Cdd:cd05943 176 AVDAYTYNgkrhdvrekvaeLVKGLPSLLAVVVVPYTV----AAGQPDLskiakalTLEDFLATGAAGElefeplpfdhp 251
|
170 180
....*....|....*....|
gi 1309054211 162 --IIYTSGTSGASKGVMLTH 179
Cdd:cd05943 252 lyILYSSGTTGLPKCIVHGA 271
|
|
| |
