|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
28-382 |
0e+00 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 513.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 28 ALDGE-VSLLPVPLHDGTRASILRNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQWLLA 106
Cdd:PRK07824 1 ALAGRaPALLPVPAQDERRAALLRDALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQWLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 107 MPAYHIAGLQVLIRSLLAGTNPVCVDVTDGFDVAAFADGAEALTSDRAYTSLAPMQLAKAMEEPFGAAALRLFDAVLVGG 186
Cdd:PRK07824 81 LPAHHIAGLQVLVRSVIAGSEPVELDVSAGFDPTALPRAVAELGGGRRYTSLVPMQLAKALDDPAATAALAELDAVLVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 187 AALNPQVAARAEELGINVVTTYGSSETAGGCVYDGQPIEGAQVAIENGRVWLGGPMIAHGYRNAPSHEAFHKPGWFATSD 266
Cdd:PRK07824 161 GPAPAPVLDAAAAAGINVVRTYGMSETSGGCVYDGVPLDGVRVRVEDGRIALGGPTLAKGYRNPVDPDPFAEPGWFRTDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 267 AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGLgDAED 346
Cdd:PRK07824 241 LGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEAL-RAHV 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 1080381800 347 AGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAALF 382
Cdd:PRK07824 320 ARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
62-382 |
5.42e-101 |
|
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: 301.94 E-value: 5.42e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 62 SIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVtdgfdv 139
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGfgGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLER------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 140 aAFADGAEALTSDRAYTSLAPMQLAKAMEEPFGAAALRLFDAVLVGGAALNPQVAARAEELGINVVTTYGSSETAG---- 215
Cdd:cd17630 75 -NQALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASqvat 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 216 ------GCVYDGQPIEGAQVAI-ENGRVWLGGPMIAHGYRNAPSHEAFHKPGWFATSDAGEIH-DGRLVITGRLDTIIDS 287
Cdd:cd17630 154 krpdgfGRGGVGVLLPGRELRIvEDGEIWVGGASLAMGYLRGQLVPEFNEDGWFTTKDLGELHaDGRLTVLGRADNMIIS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 288 GGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEG--IAELGDVMDGLgdaedAGRINHWMIPKDLRRVEVL 365
Cdd:cd17630 234 GGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGrgPADPAELRAWL-----KDKLARFKLPKRIYPVPEL 308
|
330
....*....|....*..
gi 1080381800 366 PLIGPGKVDRKKVAALF 382
Cdd:cd17630 309 PRTGGGKVDRRALRAWL 325
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
63-382 |
1.26e-56 |
|
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: 191.56 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 63 IALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ--WLLAMPAYHIAGL-QVLIRSLLAGTNPVCVDvtdGFDV 139
Cdd:COG0318 102 TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGdvVLVALPLFHVFGLtVGLLAPLLAGATLVLLP---RFDP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 140 AAFADgaeALTSDRA-YTSLAP----MQLAKAMEEPFGAAALRLfdaVLVGGAALNPQVAARAEE-LGINVVTTYGSSET 213
Cdd:COG0318 179 ERVLE---LIERERVtVLFGVPtmlaRLLRHPEFARYDLSSLRL---VVSGGAPLPPELLERFEErFGVRIVEGYGLTET 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 214 AGGCVYD------------GQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAP--SHEAFHkPGWFATSDAG 268
Cdd:COG0318 253 SPVVTVNpedpgerrpgsvGRPLPGVEVRIvdedgrelppgEVGEIVVRGPNVMKGYWNDPeaTAEAFR-DGWLRTGDLG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 269 EI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEgIAELGDVmdglgDAED- 346
Cdd:COG0318 332 RLdEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV-LRPGAEL-----DAEEl 405
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1080381800 347 ----AGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAALF 382
Cdd:COG0318 406 raflRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
60-378 |
2.13e-56 |
|
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: 190.74 E-value: 2.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQ-WLLAMPAYHIAGLQVLIRSLLAGTNPVCVDvtdgf 137
Cdd:TIGR01923 110 MDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGfTEDDnWLLSLPLYHISGLSILFRWLIEGATLRIVD----- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 138 dvaAFADGAEALTSDR-AYTSLAPMQLAKAMEEPFGAAALRLFdavLVGGAALNPQVAARAEELGINVVTTYGSSETAG- 215
Cdd:TIGR01923 185 ---KFNQLLEMIANERvTHISLVPTQLNRLLDEGGHNENLRKI---LLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSq 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 216 ----------GCVYDGQPIEGAQVAIEN------GRVWLGGPMIAHGY-RNAPSHEAFHKPGWFATSDAGEI-HDGRLVI 277
Cdd:TIGR01923 259 vttatpemlhARPDVGRPLAGREIKIKVdnkeghGEIMVKGANLMKGYlYQGELTPAFEQQGWFNTGDIGELdGEGFLYV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 278 TGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAelgDVMDGLGDAEDAGRINHWMIPK 357
Cdd:TIGR01923 339 LGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSES---DISQAKLIAYLTEKLAKYKVPI 415
|
330 340
....*....|....*....|.
gi 1080381800 358 DLRRVEVLPLIGPGKVDRKKV 378
Cdd:TIGR01923 416 AFEKLDELPYNASGKILRNQL 436
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
63-374 |
2.67e-50 |
|
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: 171.70 E-value: 2.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 63 IALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ--WLLAMPAYHIAGLQVLIRSLLAGTNPVCVDvtdGFDVA 140
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGdvFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 141 AFADGAEALTSDRAYTSlaPMQLAKAMEEP-FGAAALRLFDAVLVGGAALNPQVAARAEEL-GINVVTTYGSSETAGGCV 218
Cdd:cd04433 79 AALELIEREKVTILLGV--PTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 219 YD------------GQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSH-EAFHKPGWFATSDAGEIH-DG 273
Cdd:cd04433 157 TGppdddarkpgsvGRPVPGVEVRIvdpdggelppgEIGELVVRGPSVMKGYWNNPEAtAAVDEDGWYRTGDLGRLDeDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 274 RLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAA----YEGIAELGDVMDGLgdaedAGR 349
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVvvlrPGADLDAEELRAHV-----RER 311
|
330 340
....*....|....*....|....*
gi 1080381800 350 INHWMIPKDLRRVEVLPLIGPGKVD 374
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
57-377 |
1.14e-40 |
|
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: 148.26 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 57 EPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYHIAGLQVLIRSLLAGTNpvcVDVT 134
Cdd:cd05912 73 DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGltEDDNWLCALPLFHISGLSILMRSVIYGMT---VYLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 135 DGFDVaafADGAEALTSDRAYT-SLAPMQLAKAMEEpFGAAALRLFDAVLVGGAALNPQVAARAEELGINVVTTYGSSET 213
Cdd:cd05912 150 DKFDA---EQVLHLINSGKVTIiSVVPTMLQRLLEI-LGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTET 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 214 AG--------------GCVydGQPIEGAQVAIEN--------GRVWLGGPMIAHGYRN-APSHEAFHKPGWFATSDAGEI 270
Cdd:cd05912 226 CSqivtlspedalnkiGSA--GKPLFPVELKIEDdgqppyevGEILLKGPNVTKGYLNrPDATEESFENGWFKTGDIGYL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 271 -HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG---HAIVAAYEGI--AELGDVMDglgda 344
Cdd:cd05912 304 dEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGqvpVAFVVSERPIseEELIAYCS----- 378
|
330 340 350
....*....|....*....|....*....|...
gi 1080381800 345 edaGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd05912 379 ---EKLAKYKVPKKIYFVDELPRTASGKLLRHE 408
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
25-379 |
5.85e-40 |
|
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: 147.84 E-value: 5.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 25 LRAALDGEVSLLPVPLHD-GTRASILRNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSAT---ATHQwLGGE 100
Cdd:cd05926 112 LELALDVGVLIRAPSAESlSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATnitNTYK-LTPD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 101 GQWLLAMPAYHIAGL-QVLIRSLLAGTNPVCvdvTDGFDVAAFADGAEALtsdRA--YTSLAPMQ---LAKAMEEPFGAA 174
Cdd:cd05926 191 DRTLVVMPLFHVHGLvASLLSTLAAGGSVVL---PPRFSASTFWPDVRDY---NAtwYTAVPTIHqilLNRPEPNPESPP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 175 A-LRLfdaVLVGGAALNPQVAARAEE-LGINVVTTYGSSETAG--------------GCVydGQPIeGAQVAI------- 231
Cdd:cd05926 265 PkLRF---IRSCSASLPPAVLEALEAtFGAPVLEAYGMTEAAHqmtsnplppgprkpGSV--GKPV-GVEVRIldedgei 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 232 ----ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAI 304
Cdd:cd05926 339 lppgVVGEICLRGPNVTRGYLNNPeaNAEAAFKDGWFRTGDLGYLdADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 305 DGVTGACVVGVPHPRLGHAIVAAyegiaelgdVMDGLGDAEDAGRINHWM--------IPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd05926 419 PAVLEAVAFGVPDEKYGEEVAAA---------VVLREGASVTEEELRAFCrkhlaafkVPKKVYFVDELPKTATGKIQRR 489
|
...
gi 1080381800 377 KVA 379
Cdd:cd05926 490 KVA 492
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
11-326 |
1.27e-36 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 138.08 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 11 LSINPHNP----TAILPDL--RAALDGEVSLLPVPLHDGTRASILRNSQRAGEPidESIALVVGTSGSTGTPKGAQLTVD 84
Cdd:PRK09029 81 LPLNPQLPqpllEELLPSLtlDFALVLEGENTFSALTSLHLQLVEGAHAVAWQP--QRLATMTLTSGSTGLPKAAVHTAQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 85 NLVSSATATHQWLGGEGQ--WLLAMPAYHIAGLQVLIRSLLAGTNPVcvdvtdgfdVAAFADGAEALtSDRAYTSLAPMQ 162
Cdd:PRK09029 159 AHLASAEGVLSLMPFTAQdsWLLSLPLFHVSGQGIVWRWLYAGATLV---------VRDKQPLEQAL-AGCTHASLVPTQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 163 LAKAMEEPFGAAALRlfdAVLVGGAALNPQVAARAEELGINVVTTYGSSETAGG-CV--YD-----GQPIEGAQVAIENG 234
Cdd:PRK09029 229 LWRLLDNRSEPLSLK---AVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTvCAkrADglagvGSPLPGREVKLVDG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 235 RVWLGGPMIAHGY-RNAPSHEAFHKPGWFATSDAGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVV 313
Cdd:PRK09029 306 EIWLRGASLALGYwRQGQLVPLVNDEGWFATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV 385
|
330
....*....|...
gi 1080381800 314 GVPHPRLGHAIVA 326
Cdd:PRK09029 386 PVADAEFGQRPVA 398
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
16-375 |
2.94e-36 |
|
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: 136.97 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 16 HNPTAILPDLRAALDGEVSLLPVP--LHDGTRASILRNSqRAGEPIDEsIALVVGTSGSTGTPKGAQLTVDNLVSSATAT 93
Cdd:cd17631 53 KNSPEFLELLFAAARLGAVFVPLNfrLTPPEVAYILADS-GAKVLFDD-LALLMYTSGTTGRPKGAMLTHRNLLWNAVNA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 94 --HQWLGGEGQWLLAMPAYHIAGLQVLIRSLLAgtNPVCVDVTDGFDVAAFADGAEA--LTSdrayTSLAPMQLAKAMEE 169
Cdd:cd17631 131 laALDLGPDDVLLVVAPLFHIGGLGVFTLPTLL--RGGTVVILRKFDPETVLDLIERhrVTS----FFLVPTMIQALLQH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 170 P-FGAAALRLFDAVLVGGAALNPQVAARAEELGINVVTTYGSSETAGG-CVYD-----------GQPIEGAQVAI----- 231
Cdd:cd17631 205 PrFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGvTFLSpedhrrklgsaGRPVFFVEVRIvdpdg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 232 ------ENGRVWLGGPMIAHGYRNAP--SHEAFHKpGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELL 302
Cdd:cd17631 285 revppgEVGEIVVRGPHVMAGYWNRPeaTAAAFRD-GWFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLY 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 303 AIDGVTGACVVGVPHPRLG---HAIVAAYEGIAELGDVMdglgDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDR 375
Cdd:cd17631 364 EHPAVAEVAVIGVPDEKWGeavVAVVVPRPGAELDEDEL----IAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
33-333 |
4.95e-36 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 136.57 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 33 VSLLPVPLHDGTRAS----ILRNSQR----AGEPidESIALVVGTSGSTGTPKGAQLTVDNLVS-SATATHQWLGGEGQW 103
Cdd:cd05907 53 IGAVPVPIYPTSSAEqiayILNDSEAkalfVEDP--DDLATIIYTSGTTGRPKGVMLSHRNILSnALALAERLPATEGDR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 104 LLAM-PAYHIAG-LQVLIRSLLAGtnpVCVdvtdgfdvaAFADGAEALTSDRA---YTSLA-------PMQLA-KAMEEP 170
Cdd:cd05907 131 HLSFlPLAHVFErRAGLYVPLLAG---ARI---------YFASSAETLLDDLSevrPTVFLavprvweKVYAAiKVKAVP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 171 ------FGAAALRLFDAVLVGGAALNPQVAARAEELGINVVTTYGSSETAG------------GCVydGQPIEGAQVAI- 231
Cdd:cd05907 199 glkrklFDLAVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAvvtlnppgdnriGTV--GKPLPGVEVRIa 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 232 ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEIH-DGRLVITGRL-DTIIDSGGLKLHPEVLERELLAIDGV 307
Cdd:cd05907 277 DDGEILVRGPNVMLGYYKNPeaTAEALDADGWLHTGDLGEIDeDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLI 356
|
330 340
....*....|....*....|....*.
gi 1080381800 308 TGACVVGVPHPRLGHAIVAAYEGIAE 333
Cdd:cd05907 357 SQAVVIGDGRPFLVALIVPDPEALEA 382
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
4-285 |
6.89e-34 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 130.12 E-value: 6.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 4 VVRTLSLLSINPHNPTAILPDLRAALDGEVSLLPVPLHDgtRASILRNSQRAGEPID-ESIALVVGTSGSTGTPKGAQLT 82
Cdd:pfam00501 99 TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPE--EAKPADVPPPPPPPPDpDDLAYIIYTSGTTGKPKGVMLT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 83 VDNLVSSATATHQ------WLGGEGQWLLAMPAYHIAGLQV-LIRSLLAGTNPVCVDVTDGFDVAAFADGAEAL--Tsdr 153
Cdd:pfam00501 177 HRNLVANVLSIKRvrprgfGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPALDPAALLELIERYkvT--- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 154 aYTSLAP----MQLAKAMEEPFGAAALRLfdaVLVGGAALNPQVAARAEELGIN-VVTTYGSSETAGGCVYD-------- 220
Cdd:pfam00501 254 -VLYGVPtllnMLLEAGAPKRALLSSLRL---VLSGGAPLPPELARRFRELFGGaLVNGYGLTETTGVVTTPlpldedlr 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 221 -----GQPIEGAQVAIEN------------GRVWLGGPMIAHGYRNAPSH--EAFHKPGWFATSDAGEIH-DGRLVITGR 280
Cdd:pfam00501 330 slgsvGRPLPGTEVKIVDdetgepvppgepGELCVRGPGVMKGYLNDPELtaEAFDEDGWYRTGDLGRRDeDGYLEIVGR 409
|
....*
gi 1080381800 281 LDTII 285
Cdd:pfam00501 410 KKDQI 414
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
60-381 |
8.49e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 130.85 E-value: 8.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYHIAGLQVLIRSLLAGtnpVCVDVTDGF 137
Cdd:PRK03640 140 LDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGltEDDCWLAAVPIFHISGLSILMRSVIYG---MRVVLVEKF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 138 DVAAFadgAEALTSDRAYT-SLAPMQLAKAMEEPFGAAALRLFDAVLVGGAALNPQVAARAEELGINVVTTYGSSETAG- 215
Cdd:PRK03640 217 DAEKI---NKLLQTGGVTIiSVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASq 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 216 -------------GCVydGQPIEGAQVAIEN----------GRVWLGGPMIAHGYRNAPS--HEAFHKpGWFATSDAGEI 270
Cdd:PRK03640 294 ivtlspedaltklGSA--GKPLFPCELKIEKdgvvvppfeeGEIVVKGPNVTKGYLNREDatRETFQD-GWFKTGDIGYL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 271 -HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG---HAIVAAYEGIAElgDVMDGLGDAed 346
Cdd:PRK03640 371 dEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGqvpVAFVVKSGEVTE--EELRHFCEE-- 446
|
330 340 350
....*....|....*....|....*....|....*
gi 1080381800 347 agRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAAL 381
Cdd:PRK03640 447 --KLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
63-380 |
9.88e-32 |
|
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: 124.32 E-value: 9.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 63 IALVVGTSGSTGTPKGAQLTVDNLVSSATA-THQWlggegQW------LLAMPAYHIAGL-QVLIRSLLAGTNpvcVDVT 134
Cdd:cd05941 91 PALILYTSGTTGRPKGVVLTHANLAANVRAlVDAW-----RWteddvlLHVLPLHHVHGLvNALLCPLFAGAS---VEFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 135 DGFDVAAfadGAEALTSDRA---------YTSLA--------PMQLAKAmeepFGAAALRLFdavLVGGAALNPQVAARA 197
Cdd:cd05941 163 PKFDPKE---VAISRLMPSItvfmgvptiYTRLLqyyeahftDPQFARA----AAAERLRLM---VSGSAALPVPTLEEW 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 198 EEL-GINVVTTYGSSET--AGGCVYD--------GQPIEGAQVAI------------ENGRVWLGGPMIAHGYRNAP--S 252
Cdd:cd05941 233 EAItGHTLLERYGMTEIgmALSNPLDgerrpgtvGMPLPGVQARIvdeetgeplprgEVGEIQVRGPSVFKEYWNKPeaT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 253 HEAFHKPGWFATSDAGEI-HDGRLVITGRL-DTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAA--Y 328
Cdd:cd05941 313 KEEFTDDGWFKTGDLGVVdEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVvvL 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1080381800 329 EGIAELGDVMDGLGDAedAGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:cd05941 393 RAGAAALSLEELKEWA--KQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
58-378 |
1.68e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 121.83 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 58 PIDE-SIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGgegqW------LLAMPAYHIAGLQVLIRSLLAGTNPVc 130
Cdd:PRK06187 163 DIDEnDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK----LsrddvyLVIVPMFHVHAWGLPYLALMAGAKQV- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 131 vdVTDGFDVAAFADGAEAltsDRAYTSLA-P----MQLAKAMEEPFGAAALRLfdaVLVGGAALNPQVAARAEE-LGINV 204
Cdd:PRK06187 238 --IPRRFDPENLLDLIET---ERVTFFFAvPtiwqMLLKAPRAYFVDFSSLRL---VIYGGAALPPALLREFKEkFGIDL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 205 VTTYGSSETAG-GCV---------------YDGQPIEGAQVAI--ENGRV--WLG---------GPMIAHGYRNAP--SH 253
Cdd:PRK06187 310 VQGYGMTETSPvVSVlppedqlpgqwtkrrSAGRPLPGVEARIvdDDGDElpPDGgevgeiivrGPWLMQGYWNRPeaTA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 254 EAFHKpGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG---HAIVAAYE 329
Cdd:PRK06187 390 ETIDG-GWLHTGDVGYIDeDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGerpVAVVVLKP 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1080381800 330 GiAELgdvmdglgDAED-----AGRINHWMIPKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:PRK06187 469 G-ATL--------DAKElraflRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
69-382 |
4.79e-30 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 120.10 E-value: 4.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQWL-GGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVTDgfdvaaFADGAE 147
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQGFQRYFqLQQVNSFCVLPLYHVSGLMQFMRSFLTGGKLVILPYKR------LKSGQE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 148 ALTS-DRAYTSLAPMQLAKAMEEPfgAAALRLFDAVLVGGAALNPQVAARAEELGINVVTTYGSSETAG----------- 215
Cdd:PRK07445 202 LPPNpSDFFLSLVPTQLQRLLQLR--PQWLAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASqiatlkpddfl 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 216 -GCVYDGQPIEGAQVAIEN---GRVWLGGPMIAHGYrnAPSHEAfhKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGL 290
Cdd:PRK07445 280 aGNNSSGQVLPHAQITIPAnqtGNITIQAQSLALGY--YPQILD--SQGIFETDDLGYLdAQGYLHILGRNSQKIITGGE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 291 KLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMdglgdaedagRINHWM--------IPKDLRRV 362
Cdd:PRK07445 356 NVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE----------ELKTAIkdqlspfkQPKHWIPV 425
|
330 340
....*....|....*....|
gi 1080381800 363 EVLPLIGPGKVDRKKVAALF 382
Cdd:PRK07445 426 PQLPRNPQGKINRQQLQQIA 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-326 |
1.49e-29 |
|
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: 118.82 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 15 PHNPTAILPDLRAAL-DGEVSLLPVPLhdgTRASILRNSQRAGEPI---DESIALVVGTSGSTGTPKGAQLTVDNLVSSA 90
Cdd:cd05936 78 PLNPLYTPRELEHILnDSGAKALIVAV---SFTDLLAAGAPLGERValtPEDVAVLQYTSGTTGVPKGAMLTHRNLVANA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 91 TATHQWLGGEGQ----WLLAMPAYHIAGLQV-LIRSLLAG------TNPV---CVDVTDGFDVAAFAdGAEALtsdraYT 156
Cdd:cd05936 155 LQIKAWLEDLLEgddvVLAALPLFHVFGLTVaLLLPLALGativliPRFRpigVLKEIRKHRVTIFP-GVPTM-----YI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 157 SLapMQLAKAMEEPFgaAALRLfdaVLVGGAALNPQVAARAEEL-GINVVTTYGSSET--------------AGGCvydG 221
Cdd:cd05936 229 AL--LNAPEFKKRDF--SSLRL---CISGGAPLPVEVAERFEELtGVPIVEGYGLTETspvvavnpldgprkPGSI---G 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 222 QPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSH--EAFHKpGWFATSDAGEI-HDGRLVITGRLDTIIDS 287
Cdd:cd05936 299 IPLPGTEVKIvdddgeelppgEVGELWVRGPQVMKGYWNRPEEtaEAFVD-GWLRTGDIGYMdEDGYFFIVDRKKDMIIV 377
|
330 340 350
....*....|....*....|....*....|....*....
gi 1080381800 288 GGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:cd05936 378 GGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKA 416
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
61-314 |
9.23e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 114.81 E-value: 9.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQW--LGGEGQWLLAMPAYHIAGLQVLIRSLLAGtnpVCVdvtdgfd 138
Cdd:COG1022 183 DDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERlpLGPGDRTLSFLPLAHVFERTVSYYALAAG---ATV------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 139 vaAFADGAEALTSD-----------------RAYTSLapmqLAKAMEEP------FGAAA-------------------- 175
Cdd:COG1022 253 --AFAESPDTLAEDlrevkptfmlavprvweKVYAGI----QAKAEEAGglkrklFRWALavgrryararlagkspslll 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 176 ---LRLFDAVL----------------VGGAALNPQVAA--RAeeLGINVVTTYGSSETAG------------GCVydGQ 222
Cdd:COG1022 327 rlkHALADKLVfsklrealggrlrfavSGGAALGPELARffRA--LGIPVLEGYGLTETSPvitvnrpgdnriGTV--GP 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 223 PIEGAQVAI-ENGRVWLGGPMIAHGYRNAPSH--EAFHKPGWFATSDAGEI-HDGRLVITGRL-DTIIDSGGLKLHPEVL 297
Cdd:COG1022 403 PLPGVEVKIaEDGEILVRGPNVMKGYYKNPEAtaEAFDADGWLHTGDIGELdEDGFLRITGRKkDLIVTSGGKNVAPQPI 482
|
330
....*....|....*..
gi 1080381800 298 ERELLAIDGVTGACVVG 314
Cdd:COG1022 483 ENALKASPLIEQAVVVG 499
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
63-376 |
1.53e-26 |
|
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: 110.49 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 63 IALVVGTSGSTGTPKGAQLTVDNLVSSATATHQW--LGGEGQWLLAMPAYHIAGLQV--LIRSLLAGTNPVCVDVTDGFD 138
Cdd:cd05920 141 VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVcgLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDPSPDA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 139 VAAFADgAEALTSDRAYTSLAPMQLAKAMEEPFGAAALRLfdaVLVGGAALNPQVAARAEE-LGINVVTTYGSSEtaGGC 217
Cdd:cd05920 221 AFPLIE-REGVTVTALVPALVSLWLDAAASRRADLSSLRL---LQVGGARLSPALARRVPPvLGCTLQQVFGMAE--GLL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 218 VY-------------DGQPI-----------EGAQVAI-ENGRVWLGGPMIAHGYRNAPSH--EAFHKPGWFATSDAGEI 270
Cdd:cd05920 295 NYtrlddpdeviihtQGRPMspddeirvvdeEGNPVPPgEEGELLTRGPYTIRGYYRAPEHnaRAFTPDGFYRTGDLVRR 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 271 H-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA------AYEGIAELGDVMDGLGD 343
Cdd:cd05920 375 TpDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAfvvlrdPPPSAAQLRRFLRERGL 454
|
330 340 350
....*....|....*....|....*....|...
gi 1080381800 344 AEdagrinhWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd05920 455 AA-------YKLPDRIEFVDSLPLTAVGKIDKK 480
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
53-378 |
1.61e-26 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 109.78 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 53 QRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSS--ATATHQWLGGEGQWLLAMPAYHIAG-LQVLIRSLLAGTNPV 129
Cdd:cd05903 85 QFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASirQYAERLGLGPGDVFLVASPMAHQTGfVYGFTLPLLLGAPVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 130 CVDVTDGfdvaafADGAEALTSDRAYTSLAP----MQLAKAMEEpfGAAALRLFDAVLVGGAALNPQVAARAEELGINVV 205
Cdd:cd05903 165 LQDIWDP------DKALALMREHGVTFMMGAtpflTDLLNAVEE--AGEPLSRLRTFVCGGATVPRSLARRAAELLGAKV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 206 -TTYGSSETAGGCVY------------DGQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSHEA-FHKPG 260
Cdd:cd05903 237 cSAYGSTECPGAVTSitpapedrrlytDGRPLPGVEIKVvddtgatlapgVEGELLSRGPSVFLGYLDRPDLTAdAAPEG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 261 WFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA-------AYEGIA 332
Cdd:cd05903 317 WFRTGDLARLdEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAvvvtksgALLTFD 396
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1080381800 333 ELGDVMDGLGDAEdagrinhWMIPKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:cd05903 397 ELVAYLDRQGVAK-------QYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
42-379 |
1.44e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 107.14 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 42 DGTRASILRNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYHIAGLQVLI 119
Cdd:cd05922 98 DADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGitADDRALTVLPLSYDYGLSVLN 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 120 RSLLAGTNPVcvdVTDGFdvaAFADGAEALTSDRAYTSLAPM-----QLAKAMEEPFGAAALRLFDAVlvgGAALNPQVA 194
Cdd:cd05922 178 THLLRGATLV---LTNDG---VLDDAFWEDLREHGATGLAGVpstyaMLTRLGFDPAKLPSLRYLTQA---GGRLPQETI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 195 ARAEEL--GINVVTTYGSSETAGGCVY------------DGQPIEGAQVAIEN-----------GRVWLGGPMIAHGYRN 249
Cdd:cd05922 249 ARLRELlpGAQVYVMYGQTEATRRMTYlpperilekpgsIGLAIPGGEFEILDddgtptppgepGEIVHRGPNVMKGYWN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 250 APSHEAfhKPGWFA----TSDAG-EIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPrLGHAI 324
Cdd:cd05922 329 DPPYRR--KEGRGGgvlhTGDLArRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKL 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080381800 325 VAAYEGIA--ELGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVA 379
Cdd:cd05922 406 ALFVTAPDkiDPKDVLRSL-----AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
60-377 |
6.95e-25 |
|
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: 105.30 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLT---VDNLVSSATATHQwLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVTDG 136
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEhrgLVNLLLWMQEAYP-LTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 FDVAAFADgaeALTSDRA-YTSLAPMQLAKAMEEPFGAAALRLfDAVLVGGAALNPQVAARAEEL--GINVVTTYGSSET 213
Cdd:cd05930 171 KDPEALAD---LLAEEGItVLHLTPSLLRLLLQELELAALPSL-RLVLVGGEALPPDLVRRWRELlpGARLVNLYGPTEA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 214 AGGCVYD--------------GQPIEGAQVAI--ENGR---------VWLGGPMIAHGYRNAPS-------HEAFHKPGW 261
Cdd:cd05930 247 TVDATYYrvppddeedgrvpiGRPIPNTRVYVldENLRpvppgvpgeLYIGGAGLARGYLNRPEltaerfvPNPFGPGER 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 262 -FATSDAG-EIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMD 339
Cdd:cd05930 327 mYRTGDLVrWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEE 406
|
330 340 350
....*....|....*....|....*....|....*...
gi 1080381800 340 GLgDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd05930 407 EL-RAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKA 443
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
10-321 |
1.57e-24 |
|
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: 104.60 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 10 LLSINPHNPTAILPDLRAALDGEVSLLPVPLHDGtrasilrnsqragepiDESIALVVGTSGSTGTPKGAQLTVDNLVSS 89
Cdd:cd05911 111 VLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDG----------------KDDTAAILYSSGTTGLPKGVCLSHRNLIAN 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 90 ATATHQWLGGEGQW----LLAMPAYHIAGLQVLIRSLLAGTnpvCVDVTDGFDVAAFADgaeaLTSDR--AYTSLAP--- 160
Cdd:cd05911 175 LSQVQTFLYGNDGSndviLGFLPLYHIYGLFTTLASLLNGA---TVIIMPKFDSELFLD----LIEKYkiTFLYLVPpia 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 161 MQLAK-AMEEPFGAAALRlfdAVLVGGAALNPQVAARAEELGINVVTT--YGSSETAGGCVYD----------GQPIEGA 227
Cdd:cd05911 248 AALAKsPLLDKYDLSSLR---VILSGGAPLSKELQELLAKRFPNATIKqgYGMTETGGILTVNpdgddkpgsvGRLLPNV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 228 QVAIEN------------GRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKL 292
Cdd:cd05911 325 EAKIVDddgkdslgpnepGEICVRGPQVMKGYYNNPeaTKETFDEDGWLHTGDIGYFdEDGYLYIVDRKKELIKYKGFQV 404
|
330 340
....*....|....*....|....*....
gi 1080381800 293 HPEVLERELLAIDGVTGACVVGVPHPRLG 321
Cdd:cd05911 405 APAELEAVLLEHPGVADAAVIGIPDEVSG 433
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
56-379 |
3.83e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 103.67 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 56 GEPIDESI-------ALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQWLLAMPA--YHIAG-LQVLIRSLLAG 125
Cdd:PRK06087 175 YEPLTTAItthgdelAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAplGHATGfLHGVTAPFLIG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 126 TNPVCVDVtdgFDVAAfadGAEALTSDRAYTSLAP----MQLAKAMEE-PFGAAALRLFdavLVGGAALNPQVAARAEEL 200
Cdd:PRK06087 255 ARSVLLDI---FTPDA---CLALLEQQRCTCMLGAtpfiYDLLNLLEKqPADLSALRFF---LCGGTTIPKKVARECQQR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 201 GINVVTTYGSSETAGGCV------------YDGQPIEGAQVAIENGR---VWLG--------GPMIAHGYRNAPS--HEA 255
Cdd:PRK06087 326 GIKLLSVYGSTESSPHAVvnlddplsrfmhTDGYAAAGVEIKVVDEArktLPPGcegeeasrGPNVFMGYLDEPEltARA 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 256 FHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG-----HAIVAAYE 329
Cdd:PRK06087 406 LDEEGWYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGerscaYVVLKAPH 485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1080381800 330 GIAELGDVMDGLGDAEDAGRInhWmiPKDLRRVEVLPLIGPGKVDRKKVA 379
Cdd:PRK06087 486 HSLTLEEVVAFFSRKRVAKYK--Y--PEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
69-378 |
3.89e-24 |
|
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: 103.10 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVS-SATATHQWLGGEGQWLLAMPAYHIaGLQV--LIRSLLAGTNPVCV--DVTDgfDVAAFA 143
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSfTNWMLSDFPLGPGDVFLNQAPFSF-DLSVmdLYPALASGATLVPVprDATA--DPKQLF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 144 DGAEALTSDRAYTSLAPMQLAkAMEEPFGAAALRLFDAVLVGGAALnpqVAARAEEL-----GINVVTTYGSSETAGGCV 218
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAMC-LLSPTFTPESLPSLRHFLFCGEVL---PHKTARALqqrfpDARIYNTYGPTEATVAVT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 219 YD---------------GQPIEGAQVAIEN-----------GRVWLGGPMIAHGYRNAPSH--EAFHKP---GWFATSDA 267
Cdd:cd05945 258 YIevtpevldgydrlpiGYAKPGAKLVILDedgrpvppgekGELVISGPSVSKGYLNNPEKtaAAFFPDegqRAYRTGDL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 268 GEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGLGDAED 346
Cdd:cd05945 338 VRLeADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIKAEL 417
|
330 340 350
....*....|....*....|....*....|..
gi 1080381800 347 AGRINHWMIPKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:cd05945 418 AERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
61-381 |
4.69e-24 |
|
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: 103.18 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATA--THQWLGGEGQWLLAMPAYHIAGLQV-LIRSLLAGTNPVCV-DVTDG 136
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQitAIFDPNPEDVVFGALPFFHSFGLTGcLWLPLLSGIKVVFHpNPLDY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 FDVAAFADGAEA--LTSdrayTSLAPMQLAKAMeEPFGAAALRLfdaVLVGGAALNPQVAARAEEL-GINVVTTYGSSET 213
Cdd:cd05909 227 KKIPELIYDKKAtiLLG----TPTFLRGYARAA-HPEDFSSLRL---VVAGAEKLKDTLRQEFQEKfGIRILEGYGTTEC 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 214 A-------------GGCVydGQPIEGAQVAI------------ENGRVWLGGPMIAHGYRNAPSH--EAFHKpGWFATSD 266
Cdd:cd05909 299 SpvisvntpqspnkEGTV--GRPLPGMEVKIvsvetheevpigEGGLLLVRGPNVMLGYLNEPELtsFAFGD-GWYDTGD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 267 AGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGAC-VVGVPHPRLGHAIVAAYEGiaELGDVMDGLGDA 344
Cdd:cd05909 376 IGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVaVVSVPDGRKGEKIVLLTTT--TDTDPSSLNDIL 453
|
330 340 350
....*....|....*....|....*....|....*..
gi 1080381800 345 EDAGRINHWmIPKDLRRVEVLPLIGPGKVDRKKVAAL 381
Cdd:cd05909 454 KNAGISNLA-KPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
57-375 |
1.94e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 101.42 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 57 EPID-ESIALVVGTSGSTGTPKGAQLTVDNLVSSA----TATHqwLGGEGQWLLAMPAYHIAGLQVLIRSLLA--GTnpv 129
Cdd:PRK09088 130 PSIPpERVSLILFTSGTSGQPKGVMLSERNLQQTAhnfgVLGR--VDAHSSFLCDAPMFHIIGLITSVRPVLAvgGS--- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 130 cVDVTDGFDVAA----FADGAEALTSdraYTSLAPMQLAKAMEEPFGAAALRLFDAVLVGGAAlNPQVAARAE-ELGINV 204
Cdd:PRK09088 205 -ILVSNGFEPKRtlgrLGDPALGITH---YFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAP-HAAEDILGWlDDGIPM 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 205 VTTYGSSEtaGGCVYdGQPIEGAQVAI---------------------------ENGRVWLGGPMIAHGYRNAP--SHEA 255
Cdd:PRK09088 280 VDGFGMSE--AGTVF-GMSVDCDVIRAkagaagiptptvqtrvvddqgndcpagVPGELLLRGPNLSPGYWRRPqaTARA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 256 FHKPGWFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH----AIVAAYEG 330
Cdd:PRK09088 357 FTGDGWFRTGDiARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEvgylAIVPADGA 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1080381800 331 IAELGDVMDGLGdaedaGRINHWMIPKDLRRVEVLPLIGPGKVDR 375
Cdd:PRK09088 437 PLDLERIRSHLS-----TRLAKYKVPKHLRLVDALPRTASGKLQK 476
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
38-303 |
9.13e-23 |
|
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: 99.44 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 38 VPLHDGTRASILRNSQRAGEPI------DESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQW-LGGEGQWLLAM-PA 109
Cdd:cd05914 60 VPILAEFTADEVHHILNHSEAKaifvsdEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVvLLGKGDKILSIlPL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 110 YHIAGLQV-LIRSLLAGTNPVCVD--VTDGFDVAAFADGAEALTSDRAY-------------TSLAPMQLA--------- 164
Cdd:cd05914 140 HHIYPLTFtLLLPLLNGAHVVFLDkiPSAKIIALAFAQVTPTLGVPVPLviekifkmdiipkLTLKKFKFKlakkinnrk 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 165 ------KAMEEPFGAAalrlFDAVLVGGAALNPQVAARAEELGINVVTTYGSSETAGGCVYD----------GQPIEGAQ 228
Cdd:cd05914 220 irklafKKVHEAFGGN----IKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSppnrirlgsaGKVIDGVE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 229 VAI-------ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRL-DTIIDSGGLKLHPEVL 297
Cdd:cd05914 296 VRIdspdpatGEGEIIVRGPNVMKGYYKNPeaTAEAFDKDGWFHTGDLGKIdAEGYLYIRGRKkEMIVLSSGKNIYPEEI 375
|
....*.
gi 1080381800 298 ERELLA 303
Cdd:cd05914 376 EAKINN 381
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
69-377 |
3.05e-22 |
|
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: 98.09 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQ---WLLAMPAYHIAGLQVLIRSLLAGTNPVcvdVTDGFDVAAFAd 144
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSLVLHAMAALLTDGlGLSEsdvVLPVVPMFHVNAWGLPYAAAMVGAKLV---LPGPYLDPASL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 145 gAEALTSDRAYTSLA-P---MQLAKAMEepfgAAALRLF--DAVLVGGAALNPQVAARAEELGINVVTTYGSSETAG-GC 217
Cdd:cd12119 247 -AELIEREGVTFAAGvPtvwQGLLDHLE----ANGRDLSslRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPlGT 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 218 V-----------YD---------GQPIEGAQVAI--ENGRV--WLG---------GPMIAHGY-RNAPSHEAFHKPGWFA 263
Cdd:cd12119 322 VarppsehsnlsEDeqlalrakqGRPVPGVELRIvdDDGRElpWDGkavgelqvrGPWVTKSYyKNDEESEALTEDGWLR 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 264 TSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEGIAElgdvmd 339
Cdd:cd12119 402 TGDVATIDeDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErplAVVVLKEGATV------ 475
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1080381800 340 glgDAED-----AGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd12119 476 ---TAEElleflADKVAKWWLPDDVVFVDEIPKTSTGKIDKKA 515
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
64-382 |
7.55e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.88 E-value: 7.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 64 ALVVGTSGSTGTPKGAQLTVDNLVSS--ATATHQWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVTDGFDVAA 141
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSvrAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 142 FADGAEAL--TSDRAYTSLAPMQLAKAMEEPFGA--AALRLFDAVlvgGAALNPQVA-ARAEELGINVVTTYGSSETA-- 214
Cdd:PRK05852 259 FWDDIKAVgaTWYTAVPTIHQILLERAATEPSGRkpAALRFIRSC---SAPLTAETAqALQTEFAAPVVCAFGMTEAThq 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 215 --------GGCVY----------------------DGQPIEGAQVaienGRVWLGGPMIAHGYRNAPSHEAFH-KPGWFA 263
Cdd:PRK05852 336 vtttqiegIGQTEnpvvstglvgrstgaqirivgsDGLPLPAGAV----GEVWLRGTTVVRGYLGDPTITAANfTDGWLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 264 TSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGLG 342
Cdd:PRK05852 412 TGDLGSLSaAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELV 491
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1080381800 343 dAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAALF 382
Cdd:PRK05852 492 -QFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
37-373 |
8.64e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 96.51 E-value: 8.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 37 PVPLHDGTRASILRN---SQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYH 111
Cdd:PRK07656 139 PHTEKMKTFTDFLAAgdpAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGltEGDRYLAANPFFH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 112 IAGLQV-LIRSLLAGTNPVCVDVtdgFDVAAFADGAEAltsDRA---------YTSLapmqLAKAMEEPFGAAALRLFda 181
Cdd:PRK07656 219 VFGYKAgVNAPLMRGATILPLPV---FDPDEVFRLIET---ERItvlpgpptmYNSL----LQHPDRSAEDLSSLRLA-- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 182 vLVGGAALNPQVAARAE-ELGINVVTT-YGSSETAGG---CVYD----------GQPIEGAQVAI-----------ENGR 235
Cdd:PRK07656 287 -VTGAASMPVALLERFEsELGVDIVLTgYGLSEASGVttfNRLDddrktvagtiGTAIAGVENKIvnelgeevpvgEVGE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 236 VWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACV 312
Cdd:PRK07656 366 LLVRGPNVMKGYYDDPeaTAAAIDADGWLHTGDLGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAV 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080381800 313 VGVPHPRLG---HAIVAAYEGiAELgdvmdglgDAEDagrINHWM--------IPKDLRRVEVLPLIGPGKV 373
Cdd:PRK07656 446 IGVPDERLGevgKAYVVLKPG-AEL--------TEEE---LIAYCrehlakykVPRSIEFLDELPKNATGKV 505
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
63-373 |
1.09e-21 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 94.49 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 63 IALVVGTSGSTGTPKGAQLTVDNLVSSATAthqW-----LGGEGQWLLAMPAYHIAGLQV-LIRSLLAGTNPVCVDVtdg 136
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAA---WadcadLTEDDRYLIINPFFHTFGYKAgIVACLLTGATVVPVAV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 FDVAAFAdgaEALTSDRAYTSLAPMQLAKAM-EEP----FGAAALRlfdaVLVGGAALNPQVAAR--AEELGI-NVVTTY 208
Cdd:cd17638 76 FDVDAIL---EAIERERITVLPGPPTLFQSLlDHPgrkkFDLSSLR----AAVTGAATVPVELVRrmRSELGFeTVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 209 GSSE--TAGGCVYD----------GQPIEGAQVAIEN-GRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEIHD- 272
Cdd:cd17638 149 GLTEagVATMCRPGddaetvattcGRACPGFEVRIADdGEVLVRGYNVMQGYLDDPeaTAEAIDADGWLHTGDVGELDEr 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 273 GRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEGIaelgdvmdGLgDAEDA-- 347
Cdd:cd17638 229 GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEvgkAFVVARPGV--------TL-TEEDVia 299
|
330 340
....*....|....*....|....*....
gi 1080381800 348 ---GRINHWMIPKDLRRVEVLPLIGPGKV 373
Cdd:cd17638 300 wcrERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
6-382 |
5.95e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 94.28 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 6 RTLSLLSINPHNPTAILPDLRAALDgevSLLPVPLHDGTRASilrnsqragepideSIALVVGTSGSTGTPKGAQLTVDN 85
Cdd:PRK06188 130 RVPSLKHVLTLGPVPDGVDLLAAAA---KFGPAPLVAAALPP--------------DIAGLAYTGGTTGKPKGVMGTHRS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 86 LVSSAtathQWLGGEGQW------LLAMPAYHIAGLQVLIRSLLAGTnpvcVDVTDGFDVAAFADGAEAltsDRA-YTSL 158
Cdd:PRK06188 193 IATMA----QIQLAEWEWpadprfLMCTPLSHAGGAFFLPTLLRGGT----VIVLAKFDPAEVLRAIEE---QRItATFL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 159 APMQLAKAMEEPFGAAA-LRLFDAVLVGGAALNPQVAARA-EELGINVVTTYGSSE-------------------TAGGC 217
Cdd:PRK06188 262 VPTMIYALLDHPDLRTRdLSSLETVYYGASPMSPVRLAEAiERFGPIFAQYYGQTEapmvitylrkrdhdpddpkRLTSC 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 218 vydGQPIEGAQVAI--ENGR-VWLG--------GPMIAHGYRNAP--SHEAFhKPGWFATSD-AGEIHDGRLVITGRLDT 283
Cdd:PRK06188 342 ---GRPTPGLRVALldEDGReVAQGevgeicvrGPLVMDGYWNRPeeTAEAF-RDGWLHTGDvAREDEDGFYYIVDRKKD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 284 IIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG---HAIVAAYEGIAelgdvmdgLGDAEDAGRINHW----MIP 356
Cdd:PRK06188 418 MIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGeavTAVVVLRPGAA--------VDAAELQAHVKERkgsvHAP 489
|
410 420
....*....|....*....|....*.
gi 1080381800 357 KDLRRVEVLPLIGPGKVDRKKVAALF 382
Cdd:PRK06188 490 KQVDFVDSLPLTALGKPDKKALRARY 515
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
69-382 |
9.82e-21 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.40 E-value: 9.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQ-WLGGEGQWLL-AMPAYHIAGLQVLIR-SLLAGTNPVCVDvtdGFDVAAFADG 145
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDyWRFTPDDVLIhALPIFHTHGLFVATNvALLAGASMIFLP---KFDPDAVLAL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 146 AEALTSDRA----YTSLapmqLAKAMEEPFGAAALRLFdavlVGGAAlnPQVA----ARAEELGINVVTTYGSSETA--- 214
Cdd:PRK07514 241 MPRATVMMGvptfYTRL----LQEPRLTREAAAHMRLF----ISGSA--PLLAethrEFQERTGHAILERYGMTETNmnt 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 215 ---------GGCVydGQPIEGAQVAI------------ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI- 270
Cdd:PRK07514 311 snpydgerrAGTV--GFPLPGVSLRVtdpetgaelppgEIGMIEVKGPNVFKGYWRMPekTAEEFRADGFFITGDLGKId 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 271 HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYegIAELGDVMDGLG-DAEDAGR 349
Cdd:PRK07514 389 ERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVV--VPKPGAALDEAAiLAALKGR 466
|
330 340 350
....*....|....*....|....*....|....*..
gi 1080381800 350 INHWMIPKDLRRVEVLPLIGPGKVD----RKKVAALF 382
Cdd:PRK07514 467 LARFKQPKRVFFVDELPRNTMGKVQknllREQYADLF 503
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
17-312 |
1.36e-20 |
|
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: 92.33 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 17 NPTAIL--PDLRAALDGEVS--LLPVPLHDGTRASILRNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVS--SA 90
Cdd:TIGR01733 72 GARLLLtdSALASRLAGLVLpvILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNllAW 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 91 TATHQWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVTDGFDVAAFadgAEALTSDRAYTSL----APMQLAkA 166
Cdd:TIGR01733 152 LARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAAL---LAALIAEHPVTVLnltpSLLALL-A 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 167 MEEPFGAAALRLfdaVLVGGAALNPQVAARAEEL--GINVVTTYGSSETAGGC---VYD------------GQPIEGAQV 229
Cdd:TIGR01733 228 AALPPALASLRL---VILGGEALTPALVDRWRARgpGARLINLYGPTETTVWStatLVDpddaprespvpiGRPLANTRL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 230 AI-----------ENGRVWLGGPMIAHGYRNAPSH--EAFhKPGWFATSDAGEI----------HDGRLVITGRLDTIID 286
Cdd:TIGR01733 305 YVldddlrpvpvgVVGELYIGGPGVARGYLNRPELtaERF-VPDPFAGGDGARLyrtgdlvrylPDGNLEFLGRIDDQVK 383
|
330 340
....*....|....*....|....*.
gi 1080381800 287 SGGLKLHPEVLERELLAIDGVTGACV 312
Cdd:TIGR01733 384 IRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
69-375 |
2.09e-20 |
|
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: 90.79 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATAT-HQW-LGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVcvdVTDGFDVAAfadGA 146
Cdd:cd17637 8 TAAVAGRPRGAVLSHGNLIAANLQLiHAMgLTEADVYLNMLPLFHIAGLNLALATFHAGGANV---VMEKFDPAE---AL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 147 EALTSDRA--YTSLAPMQ---LAKAMEEPFGAAALRLfdavlVGGAAlNPQVAARAEEL-GINVVTTYGSSETAG----- 215
Cdd:cd17637 82 ELIEEEKVtlMGSFPPILsnlLDAAEKSGVDLSSLRH-----VLGLD-APETIQRFEETtGATFWSLYGQTETSGlvtls 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 216 ------GCVydGQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSHEAF-HKPGWFATSDAGEI-HDGRLV 276
Cdd:cd17637 156 pyrerpGSA--GRPGPLVRVRIvddndrpvpagETGEIVVRGPLVFQGYWNLPELTAYtFRNGWHHTGDLGRFdEDGYLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 277 ITGRL--DTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA-------AYEGIAELGDVMdglgdaedA 347
Cdd:cd17637 234 YAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAvcvlkpgATLTADELIEFV--------G 305
|
330 340
....*....|....*....|....*...
gi 1080381800 348 GRINHWMIPKDLRRVEVLPLIGPGKVDR 375
Cdd:cd17637 306 SRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
11-377 |
2.86e-20 |
|
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: 91.97 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 11 LSINPHNPTA----ILPDLRAAL--------DGEVSLLPVPLHDGTRASILRNSQRAGePIDESIALVVGTSGSTGTPKG 78
Cdd:cd12116 65 VPLDPDYPADrlryILEDAEPALvltddalpDRLPAGLPVLLLALAAAAAAPAAPRTP-VSPDDLAYVIYTSGSTGRPKG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 79 AQLTVDNLVSSATATHQWLG-GEGQWLLAM--PAYHIAGLQVLIrSLLAGTNPVCVDVTDGFDVAAFAD--GAEALTSDR 153
Cdd:cd12116 144 VVVSHRNLVNFLHSMRERLGlGPGDRLLAVttYAFDISLLELLL-PLLAGARVVIAPRETQRDPEALARliEAHSITVMQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 154 AYTSLAPMQLAKAMEepfGAAALRLfdavLVGGAALNPQVAARAEELGINVVTTYGSSET-----------AGGCVYDGQ 222
Cdd:cd12116 223 ATPATWRMLLDAGWQ---GRAGLTA----LCGGEALPPDLAARLLSRVGSLWNLYGPTETtiwstaarvtaAAGPIPIGR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 223 PIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPS-------HEAFHKPG--WFATSD-AGEIHDGRLVITGRL 281
Cdd:cd12116 296 PLANTQVYVldaalrpvppgVPGELYIGGDGVAQGYLGRPAltaerfvPDPFAGPGsrLYRTGDlVRRRADGRLEYLGRA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 282 DTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH--AIVAAYEGIA-ELGDVMDGLgdaedAGRINHWMIPKD 358
Cdd:cd12116 376 DGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRlvAYVVLKAGAApDAAALRAHL-----RATLPAYMVPSA 450
|
410
....*....|....*....
gi 1080381800 359 LRRVEVLPLIGPGKVDRKK 377
Cdd:cd12116 451 FVRLDALPLTANGKLDRKA 469
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
61-375 |
3.46e-20 |
|
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: 90.40 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSA----TATHQWLGGEGQWLLaMPAYHIAGLQVLIRSLLAGTnpVCVDVTDG 136
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPdilqKEGLNWVVGDVTYLP-LPATHIGGLWWILTCLIHGG--LCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 FDVAAFADGAEalTSDRAYTSLAPMQLAKAMEEPFGAAA----LRLfdaVLVGGA-ALNPQVAARAEELGINVVTTYGSS 211
Cdd:cd17635 78 TTYKSLFKILT--TNAVTTTCLVPTLLSKLVSELKSANAtvpsLRL---IGYGGSrAIAADVRFIEATGLTNTAQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 212 ETAGGCVYD-----------GQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSHEA-FHKPGWFATSDAG 268
Cdd:cd17635 153 ETGTALCLPtdddsieinavGRPYPGVDVYLaatdgiagpsaSFGTIWIKSPANMLGYWNNPERTAeVLIDGWVNTGDLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 269 EI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGhAIVAAYEGIAELGD--VMDGLGDAE 345
Cdd:cd17635 233 ERrEDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFG-ELVGLAVVASAELDenAIRALKHTI 311
|
330 340 350
....*....|....*....|....*....|
gi 1080381800 346 DaGRINHWMIPKDLRRVEVLPLIGPGKVDR 375
Cdd:cd17635 312 R-RELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
61-381 |
7.63e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 91.52 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ--WLLAMPAYHIAGLQV-LIRSLLAGTNPVCV-DVTDG 136
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDdvILSSLPFFHSFGLTVtLWLPLLEGIKVVYHpDPTDA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 FDVAAFAD--GAEAL--TSD--RAYTslapmQLAKAMEEPFgaAALRLfdaVLVGGAALNPQVA-ARAEELGINVVTTYG 209
Cdd:PRK08633 862 LGIAKLVAkhRATILlgTPTflRLYL-----RNKKLHPLMF--ASLRL---VVAGAEKLKPEVAdAFEEKFGIRILEGYG 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 210 SSETAG----------------------GCVydGQPIEGAQVAI------------ENGRVWLGGPMIAHGYRNAPSHEA 255
Cdd:PRK08633 932 ATETSPvasvnlpdvlaadfkrqtgskeGSV--GMPLPGVAVRIvdpetfeelppgEDGLILIGGPQVMKGYLGDPEKTA 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 256 -----FHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAI--DGVTGACVVGVPHPRLGHAIVAA 327
Cdd:PRK08633 1010 evikdIDGIGWYVTGDKGHLdEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVFAVTAVPDEKKGEKLVVL 1089
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1080381800 328 YEGIAElgDVmDGLGDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAAL 381
Cdd:PRK08633 1090 HTCGAE--DV-EELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
69-377 |
7.77e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 89.64 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSA--TATHQWLGGEGQWLLAMPAYHIAGLQV-LIRSLLAGTnpVCVDVTDGFDVAAFAdg 145
Cdd:cd05917 10 TSGTTGSPKGATLTHHNIVNNGyfIGERLGLTEQDRLCIPVPLFHCFGSVLgVLACLTHGA--TMVFPSPSFDPLAVL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 146 aEALTSDRAyTSL--APMQLAKAMEEP----FGAAALRlfdAVLVGGAALNPQVAARA-EELGINVVTT-YGSSETAGGC 217
Cdd:cd05917 86 -EAIEKEKC-TALhgVPTMFIAELEHPdfdkFDLSSLR---TGIMAGAPCPPELMKRViEVMNMKDVTIaYGMTETSPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 218 -------------VYDGQPIEGAQVAI------------ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI 270
Cdd:cd05917 161 tqtrtddsiekrvNTVGRIMPHTEAKIvdpeggivppvgVPGELCIRGYSVMKGYWNDPekTAEAIDGDGWLHTGDLAVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 271 H-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYegIAELGDVMdglgDAED--- 346
Cdd:cd05917 241 DeDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWI--RLKEGAEL----TEEDika 314
|
330 340 350
....*....|....*....|....*....|...
gi 1080381800 347 --AGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd05917 315 ycKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFK 347
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
18-380 |
9.36e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 90.43 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 18 PTAILPDLRAALDGeVSLLPVPLHdgtrasiLRNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWL 97
Cdd:PRK07787 93 AQAWLGPAPDDPAG-LPHVPVRLH-------ARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 98 GGEGQWLL--AMPAYHIAGLQV-LIRSLLAGTNPVCvdvTDGFDVAAFAdgaEALTSDRAYTSLAPMQLAKAMEEPFGAA 174
Cdd:PRK07787 165 QWTADDVLvhGLPLFHVHGLVLgVLGPLRIGNRFVH---TGRPTPEAYA---QALSEGGTLYFGVPTVWSRIAADPEAAR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 175 ALRLFDAVLVGGAALNPQVAARAEEL-GINVVTTYGSSETA------------GGCVydGQPIEGAQVAIEN-------- 233
Cdd:PRK07787 239 ALRGARLLVSGSAALPVPVFDRLAALtGHRPVERYGMTETLitlstradgerrPGWV--GLPLAGVETRLVDedggpvph 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 234 -----GRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEIH-DGRLVITGRLDT-IIDSGGLKLHPEVLERELLAI 304
Cdd:PRK07787 317 dgetvGELQVRGPTLFDGYLNRPdaTAAAFTADGWFRTGDVAVVDpDGMHRIVGRESTdLIKSGGYRIGAGEIETALLGH 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080381800 305 DGVTGACVVGVPHPRLGHAIVA---AYEGIAElGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:PRK07787 397 PGVREAAVVGVPDDDLGQRIVAyvvGADDVAA-DELIDFV-----AQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
54-326 |
1.06e-19 |
|
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: 90.26 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 54 RAGEPidESIALVVGTSGSTGTPKGA---QLTVDNLVSSATATHQWLGGEGQWLLA-MPAYHIAGLQVLIRSLLAGTNPV 129
Cdd:cd05923 145 PPREP--EQPAFVFYTSGTTGLPKGAvipQRAAESRVLFMSTQAGLRHGRHNVVLGlMPLYHVIGFFAVLVAALALDGTY 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 130 CVdVTDgFDVAAfadgAEALTSDRAYTSL--APMQL-AKAMEEPFGAAALRLFDAVLVGGAALNPQVAARAEE-LGINVV 205
Cdd:cd05923 223 VV-VEE-FDPAD----ALKLIEQERVTSLfaTPTHLdALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQhLPGEKV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 206 TTYGSSETAGGcVYDGQPIEGA-------------------QVAIENGR-----VWLGGPMIAHGYRNAPSHEAFHK-PG 260
Cdd:cd05923 297 NIYGTTEAMNS-LYMRDARTGTemrpgffsevrivriggspDEALANGEegeliVAAAADAAFTGYLNQPEATAKKLqDG 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080381800 261 WFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:cd05923 376 WYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTA 442
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
8-333 |
1.09e-19 |
|
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: 90.11 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 8 LSLLSINPHNPTAILPDLRA----ALDGEVSLLPVPLHDGTRAS------ILRNSQRAGEPID---ESIALVVGTSGSTG 74
Cdd:cd17640 22 LRSLGVKAGEKVALFADNSPrwliADQGIMALGAVDVVRGSDSSveellyILNHSESVALVVEndsDDLATIIYTSGTTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 75 TPKGAQLTVDNLVSSATATHQWLGGE-GQWLLAM-PAYHIAGlqvliRSllagtnpvcvdvtdgFDVAAFADG-AEALTS 151
Cdd:cd17640 102 NPKGVMLTHANLLHQIRSLSDIVPPQpGDRFLSIlPIWHSYE-----RS---------------AEYFIFACGcSQAYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 152 DRAYTS----LAPMQLA---------------KAMEEPFGAAALRLF-------DAVLVGGAALNPQVAARAEELGINVV 205
Cdd:cd17640 162 IRTLKDdlkrVKPHYIVsvprlweslysgiqkQVSKSSPIKQFLFLFflsggifKFGISGGGALPPHVDTFFEAIGIEVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 206 TTYGSSETAG------------GCVydGQPIEGAQVAI------------ENGRVWLGGPMIAHGYRNAPS--HEAFHKP 259
Cdd:cd17640 242 NGYGLTETSPvvsarrlkcnvrGSV--GRPLPGTEIKIvdpegnvvlppgEKGIVWVRGPQVMKGYYKNPEatSKVLDSD 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 260 GWFATSDAGEI-HDGRLVITGRL-DTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAE 333
Cdd:cd17640 320 GWFNTGDLGWLtCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPNFEELEK 395
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
18-378 |
1.69e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 90.06 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 18 PTAILPDLRAALDGEVsllP--VPLHDGTRASILRNSQRAG--EPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATAT 93
Cdd:PRK05605 175 PIPALRKARAALTGPA---PgtVPWETLVDAAIGGDGSDVShpRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 94 HQWLGGEGQ----WLLAMPAYHIAGLQ-VLIRSLLAGTNPVcvdVTDGFDV-----------AAFADGAEALtsdraYTS 157
Cdd:PRK05605 252 KAWVPGLGDgperVLAALPMFHAYGLTlCLTLAVSIGGELV---LLPAPDIdlildamkkhpPTWLPGVPPL-----YEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 158 LApmqlAKAMEEPFGAAALRlfdAVLVGGAALNPQVAARAEEL-GINVVTTYGSSETAGGCV-----------YDGQPIE 225
Cdd:PRK05605 324 IA----EAAEERGVDLSGVR---NAFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSPIIVgnpmsddrrpgYVGVPFP 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 226 GAQVAI-------------ENGRVWLGGPMIAHGYRNAPSH-EAFHKPGWFATSDAGEIH-DGRLVITGRLDTIIDSGGL 290
Cdd:PRK05605 397 DTEVRIvdpedpdetmpdgEEGELLVRGPQVFKGYWNRPEEtAKSFLDGWFRTGDVVVMEeDGFIRIVDRIKELIITGGF 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 291 KLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYegIAELGDVMDGLGDAEDA-GRINHWMIPKDLRRVEVLPLIG 369
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAV--VLEPGAALDPEGLRAYCrEHLTRYKVPRRFYHVDELPRDQ 554
|
....*....
gi 1080381800 370 PGKVDRKKV 378
Cdd:PRK05605 555 LGKVRRREV 563
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
182-375 |
9.56e-19 |
|
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: 85.92 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 182 VLVGGAALNPQVAA--RAEELGINVVTTYGSSET---AGGCVYD-------GQPIEGAQVAIEN------GRVWLGGPMI 243
Cdd:cd17633 115 IFSSGQKLFESTKKklKNIFPKANLIEFYGTSELsfiTYNFNQEsrppnsvGRPFPNVEIEIRNadggeiGKIFVKSEMV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 244 AHGYRNAPSheaFHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH 322
Cdd:cd17633 195 FSGYVRGGF---SNPDGWMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080381800 323 AIVAAYEGI-----AELGDVMDGLGDAEdagrinhwmIPKDLRRVEVLPLIGPGKVDR 375
Cdd:cd17633 272 IAVALYSGDkltykQLKRFLKQKLSRYE---------IPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
65-380 |
1.27e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 87.36 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 65 LVVGTSGSTGTPKGA----QLTVDNLVSSATATHQWLGGEGQWLLAMPAYHIAGLQVLIRSL-LAGTnpvcVDVTDGFDv 139
Cdd:PRK13383 178 IVLLTSGTTGKPKGVprapQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIaLGGT----VLTHRHFD- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 140 aafADGAEALTS-DRAYT-SLAPMQLAKAMEEPFGAAA---LRLFDAVLVGGAALNPQVAAR-AEELGINVVTTYGSSET 213
Cdd:PRK13383 253 ---AEAALAQASlHRADAfTAVPVVLARILELPPRVRArnpLPQLRVVMSSGDRLDPTLGQRfMDTYGDILYNGYGSTEV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 214 AGGCVYD-----------GQPIEGAQVAIEN-----------GRVWLGGPMIAHGYRNAPSHEAFHkpGWFATSDAGEIH 271
Cdd:PRK13383 330 GIGALATpadlrdapetvGKPVAGCPVRILDrnnrpvgprvtGRIFVGGELAGTRYTDGGGKAVVD--GMTSTGDMGYLD 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 272 D-GRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEG----IAELGDVMDglgd 343
Cdd:PRK13383 408 NaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHrlaAFVVLHPGsgvdAAQLRDYLK---- 483
|
330 340 350
....*....|....*....|....*....|....*..
gi 1080381800 344 aedaGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:PRK13383 484 ----DRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
23-308 |
3.82e-18 |
|
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: 85.80 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 23 PDLRAALDGEVSLLPVPLHDGTRASILRNSQR-----AGEPidESIALVVGTSGSTGTPKGAQLTVDNLVSS--ATATHQ 95
Cdd:cd05906 126 AELVAEFAGLETLSGLPGIRVLSIEELLDTAAdhdlpQSRP--DDLALLMLTSGSTGFPKAVPLTHRNILARsaGKIQHN 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 96 WLGGEGQWLLAMPAYHIAGLQVL-IRSLLAGTNPVCV-------------DVTDGFDVA-------AFADGAEALTSDRA 154
Cdd:cd05906 204 GLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVpteeiladplrwlDLIDRYRVTitwapnfAFALLNDLLEEIED 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 155 YT-SLAPMQlakameepfgaaalrlfdAVLVGGAALNPQVAAR----AEELGIN---VVTTYGSSETAGGCVYD------ 220
Cdd:cd05906 284 GTwDLSSLR------------------YLVNAGEAVVAKTIRRllrlLEPYGLPpdaIRPAFGMTETCSGVIYSrsfpty 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 221 -----------GQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEIHDGRLV 276
Cdd:cd05906 346 dhsqalefvslGRPIPGVSMRIvddegqllpegEVGRLQVRGPVVTKGYYNNPeaNAEAFTEDGWFRTGDLGFLDNGNLT 425
|
330 340 350
....*....|....*....|....*....|...
gi 1080381800 277 ITGRL-DTIIdSGGLKLHPEVLERELLAIDGVT 308
Cdd:cd05906 426 ITGRTkDTII-VNGVNYYSHEIEAAVEEVPGVE 457
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
64-377 |
7.23e-18 |
|
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: 84.68 E-value: 7.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 64 ALVVGTSGSTGTPKGAQLTVDNlvssATATHQWLGgegqwlLAMPAYHIAGLqvlirslLAGTnPVCvdvtdgFDVAAF- 142
Cdd:cd12115 108 AYVIYTSGSTGRPKGVAIEHRN----AAAFLQWAA------AAFSAEELAGV-------LAST-SIC------FDLSVFe 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 143 -----ADGAEALTSDRAytsLAPMQLAKAMEE------PFGAAALRLFDA-------VLVGGAALNPQVAAR--AEELGI 202
Cdd:cd12115 164 lfgplATGGKVVLADNV---LALPDLPAAAEVtlintvPSAAAELLRHDAlpasvrvVNLAGEPLPRDLVQRlyARLQVE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 203 NVVTTYGSSET------------AGGCVYDGQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSHEA---- 255
Cdd:cd12115 241 RVVNLYGPSEDttystvapvppgASGEVSIGRPLANTQAYVldralqpvplgVPGELYIGGAGVARGYLGRPGLTAerfl 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 256 ---FHKPGW-FATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVV----GVPHPRLGHAIVA 326
Cdd:cd12115 321 pdpFGPGARlYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVA 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1080381800 327 AYEGIAELGDVMDGLGdaedaGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd12115 401 EPGAAGLVEDLRRHLG-----TRLPAYMVPSRFVRLDALPLTPNGKIDRSA 446
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
44-380 |
1.04e-17 |
|
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: 84.09 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 44 TRASILRNSQRAGEPID-ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ---WLLAMPAYHIAGLQVLI 119
Cdd:cd05969 71 SEAKVLITTEELYERTDpEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDdiyWCTADPGWVTGTVYGIW 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 120 RSLLAGTNPVCVDvtDGFDVAAFADGAEALTSDRAYTslAPMQLAKAMEEpfGAAALRLFDA-----VLVGGAALNPQVA 194
Cdd:cd05969 151 APWLNGVTNVVYE--GRFDAESWYGIIERVKVTVWYT--APTAIRMLMKE--GDELARKYDLsslrfIHSVGEPLNPEAI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 195 ARAEE-LGINVVTTYGSSETAGGCVYD-----------GQPIEGAQVAI-----------ENGRVWL--GGPMIAHGYRN 249
Cdd:cd05969 225 RWGMEvFGVPIHDTWWQTETGSIMIANypcmpikpgsmGKPLPGVKAAVvdengnelppgTKGILALkpGWPSMFRGIWN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 250 APS-HEAFHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA- 326
Cdd:cd05969 305 DEErYKNSFIDGWYLTGDLAYRdEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAf 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080381800 327 -----AYEGIAELGDVMDGLGDAEDAGRInhwmIPKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:cd05969 385 islkeGFEPSDELKEEIINFVRQKLGAHV----APREIEFVDNLPKTRSGKIMRRVLKA 439
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
11-376 |
1.11e-17 |
|
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: 84.25 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 11 LSINPHNPTA----ILPDLRAALDGEVSLLPVPLHDGTRASILRNSQRAGEPID--------ESIALVVGTSGSTGTPKG 78
Cdd:cd17646 76 LPLDPGYPADrlayMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATpplvpprpDNLAYVIYTSGSTGRPKG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 79 AQLTVDNLVSS-ATATHQWLGGEGQWLL--AMPAYHIAGLQVLIrSLLAGTNPVCVDVTDGFDVAAFAdgaeALTSDRAY 155
Cdd:cd17646 156 VMVTHAGIVNRlLWMQDEYPLGPGDRVLqkTPLSFDVSVWELFW-PLVAGARLVVARPGGHRDPAYLA----ALIREHGV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 156 TSL--APMQLAKAMEEPF--GAAALRLfdaVLVGGAALNPQVAAR-AEELGINVVTTYGSSETAGGCVYD---------- 220
Cdd:cd17646 231 TTChfVPSMLRVFLAEPAagSCASLRR---VFCSGEALPPELAARfLALPGAELHNLYGPTEAAIDVTHWpvrgpaetps 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 221 ---GQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSH--EAFhKPGWFA-------TSD-AGEIHDGRLV 276
Cdd:cd17646 308 vpiGRPVPNTRLYVlddalrpvpvgVPGELYLGGVQLARGYLGRPALtaERF-VPDPFGpgsrmyrTGDlARWRPDGALE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 277 ITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGLGDAEDAGRINHWMIP 356
Cdd:cd17646 387 FLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALRAHLAERLPEYMVP 466
|
410 420
....*....|....*....|
gi 1080381800 357 KDLRRVEVLPLIGPGKVDRK 376
Cdd:cd17646 467 AAFVVLDALPLTANGKLDRA 486
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
61-376 |
1.43e-17 |
|
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: 83.68 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ--WLLAMPAYHIAGLQVLIRSLLAGTNPVCvdVTDGFD 138
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSdvILACLPLFHVTGFVGSLNTAVYVGGTYV--LMARWD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 139 VAAFADGAEalTSDRAYTSLAPMQLAKAMEEP-FGAAALRLFDAVLVGGAALNPQVAARAEEL-GINVVTTYGSSETAGG 216
Cdd:cd05935 162 RETALELIE--KYKVTFWTNIPTMLVDLLATPeFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 217 CVYD----------GQP---IEGAQVAIENGRVW---------LGGPMIAHGYRNAP--SHEAFHKPG---WFATSDAGE 269
Cdd:cd05935 240 THTNpplrpklqclGIP*fgVDARVIDIETGRELppnevgeivVRGPQIFKGYWNRPeeTEESFIEIKgrrFFRTGDLGY 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 270 I-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAayegIAELGDVMDGLGDAED-- 346
Cdd:cd05935 320 MdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKA----FIVLRPEYRGKVTEEDii 395
|
330 340 350
....*....|....*....|....*....|...
gi 1080381800 347 ---AGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd05935 396 ewaREQMAAYKYPREVEFVDELPRSASGKILWR 428
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
157-382 |
1.72e-17 |
|
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: 84.04 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 157 SLAPMQLAKAMEEPFGAAALRLfdaVLVGGAALNPQVAARAE-ELGINVVTTYGSSEtaGGCVY----D---------GQ 222
Cdd:COG1021 283 PLALLWLDAAERSRYDLSSLRV---LQVGGAKLSPELARRVRpALGCTLQQVFGMAE--GLVNYtrldDpeevilttqGR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 223 PI-----------EGAQVAI-ENGRVWLGGPMIAHGYRNAPSH--EAFHKPGWFATSDAGEIH-DGRLVITGRLDTIIDS 287
Cdd:COG1021 358 PIspddevrivdeDGNPVPPgEVGELLTRGPYTIRGYYRAPEHnaRAFTPDGFYRTGDLVRRTpDGYLVVEGRAKDQINR 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 288 GGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG---HA-IVAAYEGI--AELGDVMDGLGDAEdagrinhWMIPKDLRR 361
Cdd:COG1021 438 GGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGersCAfVVPRGEPLtlAELRRFLRERGLAA-------FKLPDRLEF 510
|
250 260
....*....|....*....|.
gi 1080381800 362 VEVLPLIGPGKVDRKKVAALF 382
Cdd:COG1021 511 VDALPLTAVGKIDKKALRAAL 531
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
61-326 |
2.41e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 83.69 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQ-WLLAMPAYHIAGLQVLIRSLLAGTNPV--------- 129
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGyGEDDvYLHTAPLCHIGGLSSALAMLMVGACHVllpkfdaka 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 130 CVDVTDGFDVAAF-------AD----GAEALTSDRAYTSLA--------PMQLAKAMEEPFGAAalRLFDAVLVGGA--- 187
Cdd:PLN02860 252 ALQAIKQHNVTSMitvpammADlislTRKSMTWKVFPSVRKilngggslSSRLLPDAKKLFPNA--KLFSAYGMTEAcss 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 188 ----ALNPQVAARAEELGINVVTTYGSSETAGGCVYDGQP---IE---GAQVAIENGRVWLGGPMIAHGYRNAPSHEAFH 257
Cdd:PLN02860 330 ltfmTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPaphVElkiGLDESSRVGRILTRGPHVMLGYWGQNSETASV 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080381800 258 KP--GWFATSDAGEIHD-GRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:PLN02860 410 LSndGWLDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVA 481
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
23-331 |
4.51e-17 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 82.52 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 23 PDLRAALDGEVSLLPVPLHDGTRA-----SILRNSQRAGE---PIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATA-- 92
Cdd:cd05932 91 KAMAPGVPEGLISISLPPPSAANCqyqwdDLIAQHPPLEErptRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAgi 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 93 THQWLGGEGQWLLAMPAYHIAGlQVLIR--SLLAGTNPVCVDVTDGFdvaaFADGAEA-------------LTSDRAYTS 157
Cdd:cd05932 171 EHIGTEENDRMLSYLPLAHVTE-RVFVEggSLYGGVLVAFAESLDTF----VEDVQRArptlffsvprlwtKFQQGVQDK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 158 LAPMQLAKAMEEPF--------GAAALRLfDAVLV---GGAALNPQVAARAEELGINVVTTYGSSETAG----------- 215
Cdd:cd05932 246 IPQQKLNLLLKIPVvnslvkrkVLKGLGL-DQCRLagcGSAPVPPALLEWYRSLGLNILEAYGMTENFAyshlnypgrdk 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 216 -GCVydGQPIEGAQVAI-ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRL-DTIIDSGG 289
Cdd:cd05932 325 iGTV--GNAGPGVEVRIsEDGEILVRSPALMMGYYKDPeaTAEAFTADGFLRTGDKGELdADGNLTITGRVkDIFKTSKG 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1080381800 290 LKLHPEVLERELLAIDGVTGACVVG--VPHPrlgHAIVAAYEGI 331
Cdd:cd05932 403 KYVAPAPIENKLAEHDRVEMVCVIGsgLPAP---LALVVLSEEA 443
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
70-326 |
4.68e-17 |
|
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: 82.28 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 70 SGSTGTPKGAQLTVDNLVSSATATH----QWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCvdVTDGFDVAAFADG 145
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIAMVAQFVagegSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVV--VMPRFDLEELLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 146 AEALTSDRAYtsLAP---MQLAK-AMEEPFGAAALRlfdAVLVGGAALNPQVAARAEEL--GINVVTTYGSSETAGGCVY 219
Cdd:cd05904 245 IERYKVTHLP--VVPpivLALVKsPIVDKYDLSSLR---QIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAM 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 220 DGQPIE-------------GAQVAI------------ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-H 271
Cdd:cd05904 320 CFAPEKdrakygsvgrlvpNVEAKIvdpetgeslppnQTGELWIRGPSIMKGYLNNPeaTAATIDKEGWLHTGDLCYIdE 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1080381800 272 DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:cd05904 400 DGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMA 454
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
61-324 |
9.92e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 81.46 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQW-------LLAMPAYHIAGLQV--LIRSLLAGTNPVcv 131
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLeegcevvITALPLYHIFALTAngLVFMKIGGCNHL-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 132 dVTDGFDVAAFADGAEAlTSDRAYTSLAPMqLAKAMEEP-FGAAALRLFDAVLVGGAALNPQVAARAEEL-GINVVTTYG 209
Cdd:PRK08751 286 -ISNPRDMPGFVKELKK-TRFTAFTGVNTL-FNGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVtGLTLVEAYG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 210 SSETA-GGCV-------YDGQ---PIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATS 265
Cdd:PRK08751 363 LTETSpAACInpltlkeYNGSiglPIPSTDACIkddagtvlaigEIGELCIKGPQVMKGYWKRPeeTAKVMDADGWLHTG 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 266 DAGEIHD-GRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAI 324
Cdd:PRK08751 443 DIARMDEqGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIV 502
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
61-326 |
1.77e-16 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 80.93 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQ------------------WLGGEGQWLLAmpayhiaglqvlirSL 122
Cdd:COG0365 184 DDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyvldlkpgdvfwctadigWATGHSYIVYG--------------PL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 123 LAGTNPVCVDVTDGF-DVAAFADGAEAL------TSDRAYTSLApmqlaKAMEEPFGAAALRLFDAVLVGGAALNPQVAA 195
Cdd:COG0365 250 LNGATVVLYEGRPDFpDPGRLWELIEKYgvtvffTAPTAIRALM-----KAGDEPLKKYDLSSLRLLGSAGEPLNPEVWE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 196 RAEE-LGINVVTTYGSSETAG-------------GCVydGQPIEGAQVAI-----------ENGRVWLGGPM--IAHGYR 248
Cdd:COG0365 325 WWYEaVGVPIVDGWGQTETGGifisnlpglpvkpGSM--GKPVPGYDVAVvdedgnpvppgEEGELVIKGPWpgMFRGYW 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 249 NAPS--HEAFHK--PGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHP-EVlERELLAIDGVTGACVVGVPHPRLGH 322
Cdd:COG0365 403 NDPEryRETYFGrfPGWYRTGDGARRDeDGYFWILGRSDDVINVSGHRIGTaEI-ESALVSHPAVAEAAVVGVPDEIRGQ 481
|
....
gi 1080381800 323 AIVA 326
Cdd:COG0365 482 VVKA 485
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-376 |
2.10e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 81.36 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 35 LLPVPlhDGTRASILRN-----SQRAGE----PID-ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQW--LGGEGQ 102
Cdd:PRK12467 622 QLPVP--AGLRSLCLDEpadllCGYSGHnpevALDpDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERlqLAADDS 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 103 WLL-AMPAYHIAGLQvLIRSLLAGTNPVCVDVTDGFDVAAFAdgaeALTSDRAYTSL-APMQLAKAMEEPFGAAALRLFD 180
Cdd:PRK12467 700 MLMvSTFAFDLGVTE-LFGALASGATLHLLPPDCARDAEAFA----ALMADQGVTVLkIVPSHLQALLQASRVALPRPQR 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 181 AVLVGGAALNPQVAARAEELGIN--VVTTYGSSETA--------------GGCVYDGQPIEGAQVAIEN----------- 233
Cdd:PRK12467 775 ALVCGGEALQVDLLARVRALGPGarLINHYGPTETTvgvstyelsdeerdFGNVPIGQPLANLGLYILDhylnpvpvgvv 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 234 GRVWLGGPMIAHGYRNAPSHEA-------FHKPG--WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLA 303
Cdd:PRK12467 855 GELYIGGAGLARGYHRRPALTAerfvpdpFGADGgrLYRTGDlARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA 934
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080381800 304 IDGVTGACVVGVPHPrlGHAIVAAYEGIAELGDVMDG--LGDAEDAG---RINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:PRK12467 935 QPGVREAVVLAQPGD--AGLQLVAYLVPAAVADGAEHqaTRDELKAQlrqVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
63-375 |
2.79e-16 |
|
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: 79.45 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 63 IALVVGTSGSTGTPKGAQLTVDNLVSSATA-THQWLGGEGQWLL-AMPAYHIAGLQVLIRSLLAGTNPVCVDVTDGF-DV 139
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMlALNSLFDPDDVLLcGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYrNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 140 AAFADGAEALTSDR-AYTSLAPMQLAKAMEEPFGA--AALRLfdaVLVGGAALNPQVAARAEE-LGINVVTTYGSSETAG 215
Cdd:cd05944 84 GLFDNFWKLVERYRiTSLSTVPTVYAALLQVPVNAdiSSLRF---AMSGAAPLPVELRARFEDaTGLPVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 216 GCVYD-----------GQPIEGAQVAI----------------ENGRVWLGGPMIAHGYRNAP-SHEAFHKPGWFATSDA 267
Cdd:cd05944 161 LVAVNppdgpkrpgsvGLRLPYARVRIkvldgvgrllrdcapdEVGEICVAGPGVFGGYLYTEgNKNAFVADGWLNTGDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 268 GEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVaAYEGIAELGDVMDGLGDAED 346
Cdd:cd05944 241 GRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPV-AYVQLKPGAVVEEEELLAWA 319
|
330 340 350
....*....|....*....|....*....|
gi 1080381800 347 AGRI-NHWMIPKDLRRVEVLPLIGPGKVDR 375
Cdd:cd05944 320 RDHVpERAAVPKHIEVLEELPVTAVGKVFK 349
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
61-376 |
2.97e-16 |
|
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: 79.72 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWL-----------------GGEGQWLLAMpayhIAGLQVLIRS-- 121
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYgltpgdrelqfasfnfdGAHEQLLPPL----ICGACVVLRPde 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 122 LLAGTNPVCVDV-TDGFDVAAFADgaealtsdrAYTSlapmQLAKAMEE--PFGAAALRLFdavLVGGAALNPQVAARAE 198
Cdd:cd17649 170 LWASADELAEMVrELGVTVLDLPP---------AYLQ----QLAEEADRtgDGRPPSLRLY---IFGGEALSPELLRRWL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 199 ELGINVVTTYGSSET---------------AGGCVYDGQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAP- 251
Cdd:cd17649 234 KAPVRLFNAYGPTEAtvtplvwkceagaarAGASMPIGRPLGGRSAYIldadlnpvpvgVTGELYIGGEGLARGYLGRPe 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 252 -SHEAF-----HKPG--WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPrLGH 322
Cdd:cd17649 314 lTAERFvpdpfGAPGsrLYRTGDlARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGK 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 323 AIVA--AYEGIAELGDVMDGLGDAEdAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd17649 393 QLVAyvVLRAAAAQPELRAQLRTAL-RASLPDYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
69-377 |
3.79e-16 |
|
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: 79.26 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQ-WLLAMPAYHIAGLQV-LIRSLLAGTNPVcvdVTDGFDVAAFADg 145
Cdd:cd05934 89 TSGTTGPPKGVVITHANLTFAGYYSARRFGlGEDDvYLTVLPLFHINAQAVsVLAALSVGATLV---LLPRFSASRFWS- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 146 aEALTSDRAYTSLAPMQLAKAMEEPFG----AAALRlfdavLVGGAALNPQVAARAEE-LGINVVTTYGSSETAGGCVYD 220
Cdd:cd05934 165 -DVRRYGATVTNYLGAMLSYLLAQPPSpddrAHRLR-----AAYGAPNPPELHEEFEErFGVRLLEGYGMTETIVGVIGP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 221 ----------GQPIEGAQVAI--ENGR------------VWLGGPMIAHGYRNAP--SHEAFhKPGWFATSDAGEI-HDG 273
Cdd:cd05934 239 rdeprrpgsiGRPAPGYEVRIvdDDGQelpagepgelviRGLRGWGFFKGYYNMPeaTAEAM-RNGWFHTGDLGYRdADG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 274 RLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYegIAELGDVMdglgDAED-----AG 348
Cdd:cd05934 318 FFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVV--VLRPGETL----DPEElfafcEG 391
|
330 340
....*....|....*....|....*....
gi 1080381800 349 RINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd05934 392 QLAYFKVPRYIRFVDDLPKTPTEKVAKAQ 420
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
58-373 |
5.11e-16 |
|
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: 79.27 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 58 PIDESIALVVG-TSGSTGTPKGAQLTVDN--LVSSATATHQWLGGEGQWLLAMPAYHIAG-LQVLIRSLLAGTNpVCVDV 133
Cdd:cd12118 129 PADEWDPIALNyTSGTTGRPKGVVYHHRGayLNALANILEWEMKQHPVYLWTLPMFHCNGwCFPWTVAAVGGTN-VCLRK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 134 TDgfdvaafADGAEALTSDRAYTSL--APM---QLAKAMEEPFGAAALRLFdaVLVGGAALNPQVAARAEELGINVVTTY 208
Cdd:cd12118 208 VD-------AKAIYDLIEKHKVTHFcgAPTvlnMLANAPPSDARPLPHRVH--VMTAGAPPPAAVLAKMEELGFDVTHVY 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 209 GSSETAGG---CVY----DGQPIE---------GAQVAIEN--------------------GRVWLGGPMIAHGYRNAP- 251
Cdd:cd12118 279 GLTETYGPatvCAWkpewDELPTEerarlkarqGVRYVGLEevdvldpetmkpvprdgktiGEIVFRGNIVMKGYLKNPe 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 252 -SHEAFhKPGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG---HAIVA 326
Cdd:cd12118 359 aTAEAF-RGGWFHSGDLAVIHpDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGevpCAFVE 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1080381800 327 AYEGIAELG-DVMDGLGDaedagRINHWMIPKDLRRVEvLPLIGPGKV 373
Cdd:cd12118 438 LKEGAKVTEeEIIAFCRE-----HLAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
18-376 |
5.63e-16 |
|
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: 79.17 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 18 PTAILPDLRAALDGEVSLLPVPLHDGTRASILRNSQRAGEPidESIALVVGTSGSTGTPKGAQLTVDNLVSsatathqwl 97
Cdd:cd12117 95 AKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSP--DDLAYVMYTSGSTGRPKGVAVTHRGVVR--------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 98 ggegqwlLAMPAYHIAgLQVLIRSLLAGtnPVcvdvtdGFDVAAFA------DGAEALTSDRaYTSLAPMQLAKAMEE-- 169
Cdd:cd12117 164 -------LVKNTNYVT-LGPDDRVLQTS--PL------AFDASTFEiwgallNGARLVLAPK-GTLLDPDALGALIAEeg 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 170 ---------------PFGAAALRLFDAVLVGGAALNPQ--VAARAEELGINVVTTYGSSET--------------AGGCV 218
Cdd:cd12117 227 vtvlwltaalfnqlaDEDPECFAGLRELLTGGEVVSPPhvRRVLAACPGLRLVNGYGPTENttfttshvvteldeVAGSI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 219 YDGQPIEGAQVAI--ENGRV---------WLGGPMIAHGYRNAP--SHEAF----HKPG--WFATSD-AGEIHDGRLVIT 278
Cdd:cd12117 307 PIGRPIANTRVYVldEDGRPvppgvpgelYVGGDGLALGYLNRPalTAERFvadpFGPGerLYRTGDlARWLPDGRLEFL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 279 GRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELG--DVMDGLgdaedAGRINHWMIP 356
Cdd:cd12117 387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDaaELRAFL-----RERLPAYMVP 461
|
410 420
....*....|....*....|
gi 1080381800 357 KDLRRVEVLPLIGPGKVDRK 376
Cdd:cd12117 462 AAFVVLDELPLTANGKVDRR 481
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
13-376 |
8.35e-16 |
|
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: 78.54 E-value: 8.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 13 INPHNP----TAILPDLRAAL----DGEVSLLPVPLHDGTRasILRNSQRAGEPIDESIAL-------VVGTSGSTGTPK 77
Cdd:cd17651 75 LDPAYPaerlAFMLADAGPVLvlthPALAGELAVELVAVTL--LDQPGAAAGADAEPDPALdaddlayVIYTSGSTGRPK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 78 GAQL---TVDNLVSSATATHQWLGGEGQWLLAMPAYHIAgLQVLIRSLLAGTNPVCVDVTDGFDVAAFADGAEALTSDRA 154
Cdd:cd17651 153 GVVMphrSLANLVAWQARASSLGPGARTLQFAGLGFDVS-VQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 155 YtslAPMQLAKAMEE---PFGAAALRLFDaVLVGGAALNPQVAAR---AEELGINVVTTYGSSE----TAGGCVYD---- 220
Cdd:cd17651 232 F---LPTVALRALAEhgrPLGVRLAALRY-LLTGGEQLVLTEDLRefcAGLPGLRLHNHYGPTEthvvTALSLPGDpaaw 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 221 ------GQPIEGAQVAI--ENGR---------VWLGGPMIAHGYRNAP--SHEAFHKPGWFA------TSDAGEIH-DGR 274
Cdd:cd17651 308 papppiGRPIDNTRVYVldAALRpvppgvpgeLYIGGAGLARGYLNRPelTAERFVPDPFVPgarmyrTGDLARWLpDGE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 275 LVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGLGDAEdAGRINHWM 354
Cdd:cd17651 388 LEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAAL-ATHLPEYM 466
|
410 420
....*....|....*....|..
gi 1080381800 355 IPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd17651 467 VPSAFVLLDALPLTPNGKLDRR 488
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
59-328 |
1.81e-15 |
|
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: 77.38 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 59 IDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG---GEGQWLLAMPAYHIAGLQVLIRSLLAGTnPVCVDVTD 135
Cdd:cd05972 79 DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGlrpDDIHWNIADPGWAKGAWSSFFGPWLLGA-TVFVYEGP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 136 GFDVAAFADGAEALTSDRAYTS-LAPMQLAKAMEEPFGAAALRLfdaVLVGGAALNPQVAARAEE-LGINVVTTYGSSET 213
Cdd:cd05972 158 RFDAERILELLERYGVTSFCGPpTAYRMLIKQDLSSYKFSHLRL---VVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 214 AGGCV----------YDGQPIEGAQVAI--ENGR-----------VWLGGPMIAHGYRNAPSH-EAFHKPGWFATSDAGE 269
Cdd:cd05972 235 GLTVGnfpdmpvkpgSMGRPTPGYDVAIidDDGRelppgeegdiaIKLPPPGLFLGYVGDPEKtEASIRGDYYLTGDRAY 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 270 I-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHaIVAAY 328
Cdd:cd05972 315 RdEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGE-VVKAF 373
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
61-317 |
2.69e-15 |
|
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: 77.26 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG---GEGQWLLA-MPAYHIAGLQVLIRSLLAGT---------- 126
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPellGPDDRYLAyLPLAHIFELAAENVCLYRGGtigygsprtl 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 127 ---------------NPVC-VDVTDGFD-----VAAFADGAEALTS---DRAYTSLApmqlaKAMEEPFGAAAL--RLFD 180
Cdd:cd17639 168 tdkskrgckgdltefKPTLmVGVPAIWDtirkgVLAKLNPMGGLKRtlfWTAYQSKL-----KALKEGPGTPLLdeLVFK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 181 AV-----------LVGGAALNPQVAARAEELGINVVTTYGSSET-AGGCVYD---------GQPIEGAQVAIEN------ 233
Cdd:cd17639 243 KVraalggrlrymLSGGAPLSADTQEFLNIVLCPVIQGYGLTETcAGGTVQDpgdletgrvGPPLPCCEIKLVDweeggy 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 234 --------GRVWLGGPMIAHGYRNAPS--HEAFHKPGWFATSDAGEIH-DGRLVITGRLDTIIDS-GGLKLHPEVLEREL 301
Cdd:cd17639 323 stdkppprGEILIRGPNVFKGYYKNPEktKEAFDGDGWFHTGDIGEFHpDGTLKIIDRKKDLVKLqNGEYIALEKLESIY 402
|
330
....*....|....*.
gi 1080381800 302 LAIDGVTGACVVGVPH 317
Cdd:cd17639 403 RSNPLVNNICVYADPD 418
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
54-320 |
4.38e-15 |
|
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: 76.69 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 54 RAGEPidESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQ-----------------WLGGE----GQWLLA------ 106
Cdd:cd17641 153 AAGKG--EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAadplgpgdeyvsvlplpWIGEQmysvGQALVCgfivnf 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 107 --------------MPAYHIA------GLQVLIRSLLAGTNPVCVDVTD-----GFDVAAFA-DGAEALTSDRAYTSLAP 160
Cdd:cd17641 231 peepetmmedlreiGPTFVLLpprvweGIAADVRARMMDATPFKRFMFElgmklGLRALDRGkRGRPVSLWLRLASWLAD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 161 MQLAKAMEEPFGAAALRlfdAVLVGGAALNPQVAARAEELGINVVTTYGSSETAGGCV--------YD--GQPIEGAQVA 230
Cdd:cd17641 311 ALLFRPLRDRLGFSRLR---SAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTvhrdgdvdPDtvGVPFPGTEVR 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 231 I-ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRL-DTIIDSGGLKLHPEVLERELLAID 305
Cdd:cd17641 388 IdEVGEILVRSPGVFVGYYKNPeaTAEDFDEDGWLHTGDAGYFkENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSP 467
|
330
....*....|....*
gi 1080381800 306 GVTGACVVGVPHPRL 320
Cdd:cd17641 468 YIAEAVVLGAGRPYL 482
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
52-378 |
4.76e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 76.34 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 52 SQRAGEPIDES------IALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG---GEGQWLL--AMPAYHIAGLQV-LI 119
Cdd:PRK05677 192 AKGAGQPVTEAnpqaddVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGsnlNEGCEILiaPLPLYHIYAFTFhCM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 120 RSLLAGTNPVCvdVTDGFDVAAFadgAEALTSDR--AYTSLAPMQLAKAMEEPFGAAALRLFDAVLVGGAALNPQVAARA 197
Cdd:PRK05677 272 AMMLIGNHNIL--ISNPRDLPAM---VKELGKWKfsGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERW 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 198 EEL-GINVVTTYGSSETAGgcVYDGQPIEGAQVAI-----------------------ENGRVWLGGPMIAHGY--RNAP 251
Cdd:PRK05677 347 KEVtGCAICEGYGMTETSP--VVSVNPSQAIQVGTigipvpstlckvidddgnelplgEVGELCVKGPQVMKGYwqRPEA 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 252 SHEAFHKPGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAyeg 330
Cdd:PRK05677 425 TDEILDSDGWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVF--- 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 331 iaelgdVMDGLGDAEDAGRINHWM--------IPKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:PRK05677 502 ------VVVKPGETLTKEQVMEHMranltgykVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
20-373 |
5.58e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 76.35 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 20 AILPDLRAALDGEVSLLPVPLHDGTRA--------SILRNSQRAGEPID---ESIALVVGTSGSTGTPKGAQLTVDNLVS 88
Cdd:PRK07786 122 AALAPVATAVRDIVPLLSTVVVAGGSSddsvlgyeDLLAEAGPAHAPVDipnDSPALIMYTSGTTGRPKGAVLTHANLTG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 89 SATA---THQWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTnPVCVDVTDGFDVAAFADgaeALTSDRAYTS-LAPMQLA 164
Cdd:PRK07786 202 QAMTclrTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGA-PTVIYPLGAFDPGQLLD---VLEAEKVTGIfLVPAQWQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 165 KAMEEPfGAAALRLFDAVLVGGAALNPQVAARAEEL---GINVVTTYGSSETAG-GCVYDGQ-------------PIEGA 227
Cdd:PRK07786 278 AVCAEQ-QARPRDLALRVLSWGAAPASDTLLRQMAAtfpEAQILAAFGQTEMSPvTCMLLGEdairklgsvgkviPTVAA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 228 QVAIEN---------GRVWLGGPMIAHGYRNAP--SHEAFHKpGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPE 295
Cdd:PRK07786 357 RVVDENmndvpvgevGEIVYRAPTLMSGYWNNPeaTAEAFAG-GWFHSGDLVRQdEEGYVWVVDRKKDMIISGGENIYCA 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 296 VLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEGIAELGdvMDGLGDAEDaGRINHWMIPKDLRRVEVLPLIGPGK 372
Cdd:PRK07786 436 EVENVLASHPDIVEVAVIGRADEKWGEvpvAVAAVRNDDAALT--LEDLAEFLT-DRLARYKHPKALEIVDALPRNPAGK 512
|
.
gi 1080381800 373 V 373
Cdd:PRK07786 513 V 513
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-376 |
8.31e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 19 TAILPDLRAALDGEVSLLPVPLHDGTRASIL-RNSQRAGEP------IDESIALVVGTSGSTGTPKGAQLTVDNLVSSAT 91
Cdd:PRK12316 3147 AYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLdRGDENYAEAnpairtMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLC 3226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 92 ATHQWLG-GEGQWLLAMPAYHIAG-LQVLIRSLLAGTNPVCVDVTDGFDVAAFADGAEALTSDraYTSLAPMQLAKAMEE 169
Cdd:PRK12316 3227 WMQQAYGlGVGDRVLQFTTFSFDVfVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVD--VLHAYPSMLQAFLEE 3304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 170 PfGAAALRLFDAVLVGGAALNPQVAARAeELGINVVTTYGSSETA------------GGCVYDGQPIEGAQVAIEN---- 233
Cdd:PRK12316 3305 E-DAHRCTSLKRIVCGGEALPADLQQQV-FAGLPLYNLYGPTEATitvthwqcveegKDAVPIGRPIANRACYILDgsle 3382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 234 -------GRVWLGGPMIAHGYRNAPSHEAF------HKPG--WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVL 297
Cdd:PRK12316 3383 pvpvgalGELYLGGEGLARGYHNRPGLTAErfvpdpFVPGerLYRTGDlARYRADGVIEYIGRVDHQVKIRGFRIELGEI 3462
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080381800 298 ERELLAIDGVTGACVVGVPHPRLGHAIVAAyegiAELGDVMDGLGDAEDAgRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:PRK12316 3463 EARLLEHPWVREAVVLAVDGRQLVAYVVPE----DEAGDLREALKAHLKA-SLPEYMVPAHLLFLERMPLTPNGKLDRK 3536
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
22-326 |
9.80e-15 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 75.47 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 22 LPDLRAAL----DGEVS---LLPVPLHDGTR--ASILRNSQragePIDESIALVVGTSGSTGTPKGAQLTVDNLVSS--A 90
Cdd:PRK13295 153 LPALRHVVvvggDGADSfeaLLITPAWEQEPdaPAILARLR----PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANivP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 91 TATHQWLGGEGQWLLAMPAYHIAGLQVLIR-SLLAGTNPVCVDVtdgFDVAAFAD--GAEALTSDRAYTSLApMQLAKAM 167
Cdd:PRK13295 229 YAERLGLGADDVILMASPMAHQTGFMYGLMmPVMLGATAVLQDI---WDPARAAEliRTEGVTFTMASTPFL-TDLTRAV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 168 EE-PFGAAALRLFdavLVGGAALNPQVAARAEE-LGINVVTTYGSSETAGGCVY------------DGQPIEGAQVAI-- 231
Cdd:PRK13295 305 KEsGRPVSSLRTF---LCAGAPIPGALVERARAaLGAKIVSAWGMTENGAVTLTklddpderasttDGCPLPGVEVRVvd 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 232 ---------ENGRVWLGGPMIAHGYRNAPSHEAFHKPGWFATSDAGEIH-DGRLVITGRLDTIIDSGG-----------L 290
Cdd:PRK13295 382 adgaplpagQIGRLQVRGCSNFGGYLKRPQLNGTDADGWFDTGDLARIDaDGYIRISGRSKDVIIRGGenipvveiealL 461
|
330 340 350
....*....|....*....|....*....|....*.
gi 1080381800 291 KLHPEVLErellaidgvtgACVVGVPHPRLGHAIVA 326
Cdd:PRK13295 462 YRHPAIAQ-----------VAIVAYPDERLGERACA 486
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
69-375 |
1.14e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 75.19 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQWLLA-MPAYHIAGLqVLirsllagTNPVCVDV-------TDGFDV 139
Cdd:PRK12583 209 TSGTTGFPKGATLSHHNILNNGYFVAESLGlTEHDRLCVpVPLYHCFGM-VL-------ANLGCMTVgaclvypNEAFDP 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 140 AAF--ADGAEALTsdrAYTSLAPMQLAKAMEEPFGAAALRLFDAVLVGGAALNPQVAARA-EELGINVVT-TYGSSETAG 215
Cdd:PRK12583 281 LATlqAVEEERCT---ALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVmDEMHMAEVQiAYGMTETSP 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 216 ----GCVYDGQPI-------------------EGAQVAI-ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGE 269
Cdd:PRK12583 358 vslqTTAADDLERrvetvgrtqphlevkvvdpDGATVPRgEIGELCTRGYSVMKGYWNNPeaTAESIDEDGWMHTGDLAT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 270 I-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYE----GIAELGDVMDGLGDa 344
Cdd:PRK12583 438 MdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRlhpgHAASEEELREFCKA- 516
|
330 340 350
....*....|....*....|....*....|.
gi 1080381800 345 edagRINHWMIPKDLRRVEVLPLIGPGKVDR 375
Cdd:PRK12583 517 ----RIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
55-373 |
1.50e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 74.99 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 55 AGEPIDES-IALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQWLL-AMPAYHIAGLQVLIRSLLAGTNPVCV 131
Cdd:PRK07529 206 SGRPIGPDdVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGlGPGDTVFcGLPLFHVNALLVTGLAPLARGAHVVL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 132 DVTDGF-DVAAFADGAEALTSDR-AYTSLAPMQLAKAMEEPFGAAALRLFDAVLVGGAALNPQVAARAEE-LGINVVTTY 208
Cdd:PRK07529 286 ATPQGYrGPGVIANFWKIVERYRiNFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAaTGVRIVEGY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 209 GSSETAGGCVYD-----------GQPIEGAQVAI----ENGRVW------------LGGPMIAHGYRNAP-SHEAFHKPG 260
Cdd:PRK07529 366 GLTEATCVSSVNppdgerrigsvGLRLPYQRVRVvildDAGRYLrdcavdevgvlcIAGPNVFSGYLEAAhNKGLWLEDG 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 261 WFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAelgdvmd 339
Cdd:PRK07529 446 WLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKP------- 518
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1080381800 340 glGDAEDAGRINHWM---------IPKDLRRVEVLPLIGPGKV 373
Cdd:PRK07529 519 --GASATEAELLAFArdhiaeraaVPKHVRILDALPKTAVGKI 559
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
61-377 |
2.48e-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: 73.83 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATA--THQWLGGEGQWL-LAMPAYHIAGLQVLIrSLLAGTNPVcvdVTDGF 137
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAqiAAFDVGPGSRVLqFASPSFDASVWELLM-ALLAGATLV---LAPAE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 138 DVAAFADGAEALTSDRAYTSLAPMQLAKAMEepfgAAALRLFDAVLVGGAALNPQVAAR--AEELGIN--------VVTT 207
Cdd:cd17652 169 ELLPGEPLADLLREHRITHVTLPPAALAALP----PDDLPDLRTLVVAGEACPAELVDRwaPGRRMINaygptettVCAT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 208 YGSSETAGGCVYDGQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSHEA-------FHKPG--WFATSD- 266
Cdd:cd17652 245 MAGPLPGGGVPPIGRPVPGTRVYVldarlrpvppgVPGELYIAGAGLARGYLNRPGLTAerfvadpFGAPGsrMYRTGDl 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 267 AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGAcVVGVPHPRLGHAIVAAYegiaelgdVMDGLGDAED 346
Cdd:cd17652 325 ARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA-VVVVRDDRPGDKRLVAY--------VVPAPGAAPT 395
|
330 340 350
....*....|....*....|....*....|....*....
gi 1080381800 347 AGRINHW--------MIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd17652 396 AAELRAHlaerlpgyMVPAAFVVLDALPLTPNGKLDRRA 434
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
60-326 |
2.73e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 74.30 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWL----GGEGQWLLAMPAYHIAGLQVLIR-SLLAGTNPVCVDvt 134
Cdd:PRK06710 205 ENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLynckEGEEVVLGVLPFFHVYGMTAVMNlSIMQGYKMVLIP-- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 135 dGFDVAAFAdgaEALTSDRAYT-SLAPMQLAKAMEEPFgaaaLRLFD-----AVLVGGAALNPQVAARAEEL-GINVVTT 207
Cdd:PRK06710 283 -KFDMKMVF---EAIKKHKVTLfPGAPTIYIALLNSPL----LKEYDissirACISGSAPLPVEVQEKFETVtGGKLVEG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 208 YGSSE----TAGGCVYD-------GQP---IEGAQVAIENGRVW---------LGGPMIAHGYRNAPSHEA-FHKPGWFA 263
Cdd:PRK06710 355 YGLTEsspvTHSNFLWEkrvpgsiGVPwpdTEAMIMSLETGEALppgeigeivVKGPQIMKGYWNKPEETAaVLQDGWLH 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080381800 264 TSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:PRK06710 435 TGDVGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKA 498
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-376 |
3.18e-14 |
|
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: 73.62 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 49 LRNSQRAGEPIDES--IALVVGTSGSTGTPKGA--------------QLTVDNL-----VSSATATHQWLGGEgqwllam 107
Cdd:cd05971 74 LSNSGASALVTDGSddPALIIYTSGTTGPPKGAlhahrvllghlpgvQFPFNLFprdgdLYWTPADWAWIGGL------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 108 payhiagLQVLIRSLLAGTnPVCVDVTDGFDVAAFADGAEALTSDRAYTSLAPMQLAKAMEEPFGAAALRLfDAVLVGGA 187
Cdd:cd05971 147 -------LDVLLPSLYFGV-PVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKL-RAIATGGE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 188 ALNPQVAARA-EELGINVVTTYGSSET---AGGC--VYD------GQPIEGAQVAI--ENGR-----------VWLGGPM 242
Cdd:cd05971 218 SLGEELLGWArEQFGVEVNEFYGQTECnlvIGNCsaLFPikpgsmGKPIPGHRVAIvdDNGTplppgevgeiaVELPDPV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 243 IAHGYRNAPS-HEAFHKPGWFATSDAG-EIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRL 320
Cdd:cd05971 298 AFLGYWNNPSaTEKKMAGDWLLTGDLGrKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080381800 321 GHaIVAAYEGIAElgdvmdGLGDAED---------AGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd05971 378 GE-IVKAFVVLNP------GETPSDAlareiqelvKTRLAAHEYPREIEFVNELPRTATGKIRRR 435
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
69-374 |
3.24e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 73.77 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKG----------AQL------------TVDNLVSSATAthqwlGGEGQWLLAMPAYHIAGLQVLIRSLLAGT 126
Cdd:PRK07798 171 TGGTTGMPKGvmwrqedifrVLLggrdfatgepieDEEELAKRAAA-----GPGMRRFPAPPLMHGAGQWAAFAALFSGQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 127 NPVCVDVTDgFDVAAFADGAE-------ALTSDrAYtsLAPMqlAKAMEEPFGAAALRLFdAVLVGGAALNPQVAARAEE 199
Cdd:PRK07798 246 TVVLLPDVR-FDADEVWRTIErekvnviTIVGD-AM--ARPL--LDALEARGPYDLSSLF-AIASGGALFSPSVKEALLE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 200 LGINVVTT--YGSSET--------AGGCVYDGQPI----EGAQVAIENGRV---------WLG-GPMIAHGYRNAP--SH 253
Cdd:PRK07798 319 LLPNVVLTdsIGSSETgfggsgtvAKGAVHTGGPRftigPRTVVLDEDGNPvepgsgeigWIArRGHIPLGYYKDPekTA 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 254 EAFHK--------PGWFATSDAgeihDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH--- 322
Cdd:PRK07798 399 ETFPTidgvryaiPGDRARVEA----DGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQevv 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1080381800 323 AIVAAYEGI-AELGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVD 374
Cdd:PRK07798 475 AVVQLREGArPDLAELRAHC-----RSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
221-378 |
3.42e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 73.66 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 221 GQPIEGAQVAIEN-----------GRVWLGGPMIAHGYRN-APSHEAFHKPGWFATSDAG-EIHDGRLVITGRLDTIIDS 287
Cdd:PRK07638 310 GRPFHNVQVRICNeageevqkgeiGTVYVKSPQFFMGYIIgGVLARELNADGWMTVRDVGyEDEEGFIYIVGREKNMILF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 288 GGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGLGDaedagRINHWMIPKDLRRVEVLPL 367
Cdd:PRK07638 390 GGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQLKSFCLQ-----RLSSFKIPKEWHFVDEIPY 464
|
170
....*....|.
gi 1080381800 368 IGPGKVDRKKV 378
Cdd:PRK07638 465 TNSGKIARMEA 475
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
45-376 |
4.46e-14 |
|
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: 73.11 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 45 RASILRNSQRA---GEPidESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLampaYHIAGLQV-- 117
Cdd:cd17643 76 IAFILADSGPSlllTDP--DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGfnEDDVWTL----FHSYAFDFsv 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 118 --LIRSLLAGTNPVCVDvtdgFDVAAFADGAEALTSDRAYTSL-----APMQLAKAMEEPFGA-AALRLfdaVLVGGAAL 189
Cdd:cd17643 150 weIWGALLHGGRLVVVP----YEVARSPEDFARLLRDEGVTVLnqtpsAFYQLVEAADRDGRDpLALRY---VIFGGEAL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 190 NPQV----AARAEELGINVVTTYGSSET---------------AGGCVYDGQPIEGAQVAI-----------ENGRVWLG 239
Cdd:cd17643 223 EAAMlrpwAGRFGLDRPQLVNMYGITETtvhvtfrpldaadlpAAAASPIGRPLPGLRVYVldadgrpvppgVVGELYVS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 240 GPMIAHGYRNAPSHEA-------FHKPG--WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTG 309
Cdd:cd17643 303 GAGVARGYLGRPELTAerfvanpFGGPGsrMYRTGDlARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRD 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080381800 310 AcVVGVPHPRLG-HAIVAAYEGIAELGDVMDGLgDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd17643 383 A-AVIVREDEPGdTRLVAYVVADDGAAADIAEL-RALLKELLPDYMVPARYVPLDALPLTVNGKLDRA 448
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
69-380 |
1.03e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 72.48 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQ---WLGGEGQWLLAmPAYHIAGL-QVLIRSLLAgtnpvCVDVTD-GFDVAAFA 143
Cdd:PRK13382 204 TSGTTGTPKGARRSGPGGIGTLKAILDrtpWRAEEPTVIVA-PMFHAWGFsQLVLAASLA-----CTIVTRrRFDPEATL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 144 DGAEAltsDRAYT-SLAPMQLAKAMEEP------FGAAALRLFDAvlvGGAALNPQVA-ARAEELGINVVTTYGSSE--- 212
Cdd:PRK13382 278 DLIDR---HRATGlAVVPVMFDRIMDLPaevrnrYSGRSLRFAAA---SGSRMRPDVViAFMDQFGDVIYNNYNATEagm 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 213 --------------TAGgcvydgQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSHEaFHKpGWFATSDA 267
Cdd:PRK13382 352 iatatpadlraapdTAG------RPAEGTEIRIldqdfrevptgEVGTIFVRNDTQFDGYTSGSTKD-FHD-GFMASGDV 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 268 GEIHD-GRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGLGDAED 346
Cdd:PRK13382 424 GYLDEnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVR 503
|
330 340 350
....*....|....*....|....*....|....
gi 1080381800 347 AGRINHwMIPKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:PRK13382 504 DNLANY-KVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
60-378 |
1.12e-13 |
|
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: 72.17 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLTVDNLVssATATHQ-------WLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVcvd 132
Cdd:cd17642 183 DEQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHArdpifgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVV--- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 133 VTDGFDVAAFadgaeaLTSDRAY----TSLAPMQLA----KAMEEPFGAAALRlfdAVLVGGAALNPQVA-ARAEELGIN 203
Cdd:cd17642 258 LMYKFEEELF------LRSLQDYkvqsALLVPTLFAffakSTLVDKYDLSNLH---EIASGGAPLSKEVGeAVAKRFKLP 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 204 VVTT-YGSSETAG------------GCVYDGQPIEGAQV----------AIENGRVWLGGPMIAHGYRNAP--SHEAFHK 258
Cdd:cd17642 329 GIRQgYGLTETTSailitpegddkpGAVGKVVPFFYAKVvdldtgktlgPNERGELCVKGPMIMKGYVNNPeaTKALIDK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 259 PGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEG--IA 332
Cdd:cd17642 409 DGWLHSGDIAYYdEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGElpaAVVVLEAGktMT 488
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1080381800 333 ElGDVMDGLGD-AEDAGRINhwmipKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:cd17642 489 E-KEVMDYVASqVSTAKRLR-----GGVKFVDEVPKGLTGKIDRRKI 529
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
69-374 |
1.70e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 70.87 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKG----------AQLTVDNLVSSATATHQWLGGEG------QWLLAMPAYHIAGLQVLIRSLLAGTNPVCVD 132
Cdd:cd05924 11 TGGTTGMPKGvmwrqedifrMLMGGADFGTGEFTPSEDAHKAAaaaagtVMFPAPPLMHGTGSWTAFGGLLGGQTVVLPD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 133 vtDGFDVAAFADGAE-------ALTSDrAYtsLAPMQLAKAMEEPFGAAALRlfdAVLVGGAALNPQVAARAEELGINVV 205
Cdd:cd05924 91 --DRFDPEEVWRTIEkhkvtsmTIVGD-AM--ARPLIDALRDAGPYDLSSLF---AISSGGALLSPEVKQGLLELVPNIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 206 TT--YGSSET-------AGGCVYDGQPI----EGAQVAIENGRVWLGGP----------MIAHGYRNAP--SHEAFHK-- 258
Cdd:cd05924 163 LVdaFGSSETgftgsghSAGSGPETGPFtranPDTVVLDDDGRVVPPGSggvgwiarrgHIPLGYYGDEakTAETFPEvd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 259 ------PGWFATSDAgeihDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYE 329
Cdd:cd05924 243 gvryavPGDRATVEA----DGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQevvAVVQLRE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1080381800 330 GI-AELGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVD 374
Cdd:cd05924 319 GAgVDLEELREHC-----RTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
182-378 |
2.81e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.20 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 182 VLVGGAALNPQVAARAEELGINVVTTYGSSETAGGCVY-----------DGQPIEG-----------AQVAIEN------ 233
Cdd:PLN03102 305 VLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFcewqdewnrlpENQQMELkarqgvsilglADVDVKNketqes 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 234 --------GRVWLGGPMIAHGYRNAP--SHEAFhKPGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELL 302
Cdd:PLN03102 385 vprdgktmGEIVIKGSSIMKGYLKNPkaTSEAF-KHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLY 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 303 AIDGVTGACVVGVPHPRLGH---AIVAAYEGIAELGDVMDGL----GDAEDAGRIN--HWMIPKDLRRVEVLPLIGPGKV 373
Cdd:PLN03102 464 KYPKVLETAVVAMPHPTWGEtpcAFVVLEKGETTKEDRVDKLvtreRDLIEYCRENlpHFMCPRKVVFLQELPKNGNGKI 543
|
....*
gi 1080381800 374 DRKKV 378
Cdd:PLN03102 544 LKPKL 548
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
19-327 |
3.27e-13 |
|
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: 70.73 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 19 TAILPDLRA--ALDGEVSLLPVPLHDGTRASILRNSQRAGEPIDEsIALVVGTSGSTGTPKGAQLTVDNLVSSATA-THQ 95
Cdd:cd05931 106 AAALAAVRAfaASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDD-IAYLQYTSGSTGTPKGVVVTHRNLLANVRQiRRA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 96 WLGGEGQ----WLlamPAYHIAGL-QVLIRSLLAG-----TNPvcvdvtdgfdvAAFADG----AEALTSDRAYTSLAP- 160
Cdd:cd05931 185 YGLDPGDvvvsWL---PLYHDMGLiGGLLTPLYSGgpsvlMSP-----------AAFLRRplrwLRLISRYRATISAAPn 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 161 --MQLA--KAME------------------EPFGAAALRLFDA----------------------VLVGGAALNPQ---V 193
Cdd:cd05931 251 faYDLCvrRVRDedlegldlsswrvalngaEPVRPATLRRFAEafapfgfrpeafrpsyglaeatLFVSGGPPGTGpvvL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 194 AARAEELGINVVTTYGSSETAGGCVYDGQPIEGAQVAIEN------------GRVWLGGPMIAHGYRNAP--SHEAFHK- 258
Cdd:cd05931 331 RVDRDALAGRAVAVAADDPAARELVSCGRPLPDQEVRIVDpetgrelpdgevGEIWVRGPSVASGYWGRPeaTAETFGAl 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080381800 259 -----PGWFATSDAGEIHDGRLVITGRL-DTIIDSgGLKLHPEVLERELLAIDGV--TGACVV-GVPHPRLGHAIVAA 327
Cdd:cd05931 411 aatdeGGWLRTGDLGFLHDGELYITGRLkDLIIVR-GRNHYPQDIEATAEEAHPAlrPGCVAAfSVPDDGEERLVVVA 487
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
61-378 |
5.17e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 70.24 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSS---ATATHQWLGGEGQWLL---------AMPAYHIAGLQVLIRSLLAGTNP 128
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqVRACLSQLGPDGQPLMkegqevmiaPLPLYHIYAFTANCMCMMVSGNH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 129 vCVDVTDGFDVAAFAdgaEALTSDRAYTSLAPMQLAKA-MEEP----FGAAALRLFDAvlvGGAALNPQVAARAEEL-GI 202
Cdd:PRK12492 287 -NVLITNPRDIPGFI---KELGKWRFSALLGLNTLFVAlMDHPgfkdLDFSALKLTNS---GGTALVKATAERWEQLtGC 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 203 NVVTTYGSSETAG-------------GCVydGQPI----------EGAQVAI-ENGRVWLGGPMIAHGYRNAP--SHEAF 256
Cdd:PRK12492 360 TIVEGYGLTETSPvastnpygelarlGTV--GIPVpgtalkviddDGNELPLgERGELCIKGPQVMKGYWQQPeaTAEAL 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 257 HKPGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAI---VAAYEGIA 332
Cdd:PRK12492 438 DAEGWFKTGDIAVIDpDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVklfVVARDPGL 517
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1080381800 333 ELGDVmdglgDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:PRK12492 518 SVEEL-----KAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
61-324 |
5.95e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 70.08 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSS---ATATHQWLGGEGQWL--LAMPAYHIAGLQV--LIRSLLAGTNpvcVDV 133
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANleqAKAAYGPLLHPGKELvvTALPLYHIFALTVncLLFIELGGQN---LLI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 134 TDGFDVAAFADgaealtsdraytslapmQLAKameEPFGA--AALRLFDAVLV-----------------GGAALNPQVA 194
Cdd:PRK08974 283 TNPRDIPGFVK-----------------ELKK---YPFTAitGVNTLFNALLNneefqeldfsslklsvgGGMAVQQAVA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 195 ARAEEL-GINVVTTYGSSETA---GGCVYD--------GQPI----------EGAQVAI-ENGRVWLGGPMIAHGYRNAP 251
Cdd:PRK08974 343 ERWVKLtGQYLLEGYGLTECSplvSVNPYDldyysgsiGLPVpsteiklvddDGNEVPPgEPGELWVKGPQVMLGYWQRP 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 252 SHEA-FHKPGWFATSDAGEIHD-GRLVITGR-LDTIIDSG----------GLKLHPEVLErellaidgvtgACVVGVPHP 318
Cdd:PRK08974 423 EATDeVIKDGWLATGDIAVMDEeGFLRIVDRkKDMILVSGfnvypneiedVVMLHPKVLE-----------VAAVGVPSE 491
|
....*.
gi 1080381800 319 RLGHAI 324
Cdd:PRK08974 492 VSGEAV 497
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
27-381 |
7.06e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 69.50 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 27 AALDGEVSLLPVPLHDGTRASILRNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSA---TATHQwLGGEGQW 103
Cdd:PRK06839 115 LSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNAlnnTFAID-LTMHDRS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 104 LLAMPAYHIAGLQVL-IRSLLAGTNPVcvdVTDGFD---------------VAAFADGAEAL--TSDRAYTSLA------ 159
Cdd:PRK06839 194 IVLLPLFHIGGIGLFaFPTLFAGGVII---VPRKFEptkalsmiekhkvtvVMGVPTIHQALinCSKFETTNLQsvrwfy 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 160 ------PMQLAKAMEE---PFGAAalrlfdavlVGGAALNPQVAARAEELGINVVTTYGssETAGGCVYDGQPIEGAQVA 230
Cdd:PRK06839 271 nggapcPEELMREFIDrgfLFGQG---------FGMTETSPTVFMLSEEDARRKVGSIG--KPVLFCDYELIDENKNKVE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 231 I-ENGRVWLGGPMIAHGYRNAPSHEAFH-KPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGV 307
Cdd:PRK06839 340 VgEVGELLIRGPNVMKEYWNRPDATEETiQDGWLCTGDLARVdEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDV 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080381800 308 TGACVVGVPHPRLGHAIVAAYegIAELGDVMDGLGDAEDA-GRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAAL 381
Cdd:PRK06839 420 YEVAVVGRQHVKWGEIPIAFI--VKKSSSVLIEKDVIEHCrLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
23-377 |
7.17e-13 |
|
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: 69.41 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 23 PDLRAALDGEVSLLPVP------LHDGTRASILRNSQ-RAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQ 95
Cdd:cd05919 46 PELVQLFLGCLARGAIAvvinplLHPDDYAYIARDCEaRLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 96 WLGG--EGQWLLAMPAYHIA-GL-QVLIRSLLAGTNPVCvdvtdgFDVAAFADGAEALTSDRAYTSL--APMQLAKAMEE 169
Cdd:cd05919 126 EALGltPGDRVFSSAKMFFGyGLgNSLWFPLAVGASAVL------NPGWPTAERVLATLARFRPTVLygVPTFYANLLDS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 170 P-FGAAALRLFDAVLVGGAALNPQVAAR-AEELGINVVTTYGSSET-------------AGGCvydGQPIEGAQVAI--- 231
Cdd:cd05919 200 CaGSPDALRSLRLCVSAGEALPRGLGERwMEHFGGPILDGIGATEVghiflsnrpgawrLGST---GRPVPGYEIRLvde 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 232 --------ENGRVWLGGPMIAHGYRNAP-SHEAFHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLEREL 301
Cdd:cd05919 277 eghtippgEEGDLLVRGPSAAVGYWNNPeKSRATFNGGWYRTGDKFCRdADGWYTHAGRADDMLKVGGQWVSPVEVESLI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 302 LAIDGVTGACVVGVPHP----RLGHAIVAAYEGIAE---LGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVD 374
Cdd:cd05919 357 IQHPAVAEAAVVAVPEStglsRLTAFVVLKSPAAPQeslARDIHRHL-----LERLSAHKVPRRIAFVDELPRTATGKLQ 431
|
...
gi 1080381800 375 RKK 377
Cdd:cd05919 432 RFK 434
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
38-335 |
7.17e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 69.79 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 38 VPLHDGTRASILRNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEG------QWLlamPAYH 111
Cdd:PRK05851 129 VTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAatdvgcSWL---PLYH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 112 IAGLQVLIRSLLAGTnPVCVDVTDGFDVAAFAdGAEALTSDRAYTSLAP---------------------MQLAKAMEEP 170
Cdd:PRK05851 206 DMGLAFLLTAALAGA-PLWLAPTTAFSASPFR-WLSWLSDSRATLTAAPnfaynligkyarrvsdvdlgaLRVALNGGEP 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 171 FGAAALRLFDAVLvGGAALNPQVAARA----------------EELGINVVTTYGSSETAGGCVYdGQPIEGAQVAI--- 231
Cdd:PRK05851 284 VDCDGFERFATAM-APFGFDAGAAAPSyglaestcavtvpvpgIGLRVDEVTTDDGSGARRHAVL-GNPIPGMEVRIspg 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 232 ---------ENGRVWLGGPMIAHGYRNAPSHEAfhkPGWFATSDAGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELL 302
Cdd:PRK05851 362 dgaagvagrEIGEIEIRGASMMSGYLGQAPIDP---DDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAA 438
|
330 340 350
....*....|....*....|....*....|....*..
gi 1080381800 303 AIDGVTGACVVGV----PHPRLGHAIVAAYEGIAELG 335
Cdd:PRK05851 439 QVRGVREGAVVAVgtgeGSARPGLVIAAEFRGPDEAG 475
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
69-373 |
9.18e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 69.53 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDvtDGFDVAAFAdga 146
Cdd:PRK06145 157 TSGTTDRPKGVMHSYGNLHWKSIDHVIALGltASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIH--REFDPEAVL--- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 147 EALTSDRAYTS-LAPMQLAKAMEEP----FGAAALRLfdavLVGGAALNPQVAARA-EEL--GINVVTTYGSSETAGGCV 218
Cdd:PRK06145 232 AAIERHRLTCAwMAPVMLSRVLTVPdrdrFDLDSLAW----CIGGGEKTPESRIRDfTRVftRARYIDAYGLTETCSGDT 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 219 Y------------DGQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAP--SHEAFHKpGWFATSDAGEIHD- 272
Cdd:PRK06145 308 LmeagreiekigsTGRALAHVEIRIadgagrwlppnMKGEICMRGPKVTKGYWKDPekTAEAFYG-DWFRSGDVGYLDEe 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 273 GRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGLgDAEDAGRINH 352
Cdd:PRK06145 387 GFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEAL-DRHCRQRLAS 465
|
330 340
....*....|....*....|.
gi 1080381800 353 WMIPKDLRRVEVLPLIGPGKV 373
Cdd:PRK06145 466 FKVPRQLKVRDELPRNPSGKV 486
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
17-380 |
1.94e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 68.50 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 17 NPTAILPDLRAALDGevSLLPVPLHD------------GTRASILRNSQRAGEP---IDESIALVVgTSGSTGTPKGAQL 81
Cdd:PRK05857 113 DPAAALVAPGSKMAS--SAVPEALHSipviavdiaavtRESEHSLDAASLAGNAdqgSEDPLAMIF-TSGTTGEPKAVLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 82 -------TVDNLVSSATATHQWLGGEGQWLlAMPAYHIAGLQVLIRSLLAGTnpVCVdvTDGFDVAAFAdgaEALTSDR- 153
Cdd:PRK05857 190 anrtffaVPDILQKEGLNWVTWVVGETTYS-PLPATHIGGLWWILTCLMHGG--LCV--TGGENTTSLL---EILTTNAv 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 154 AYTSLAPMQLAKAMEE-PFGAAALRLFDAVLVGGAALNPQVAARAEELGINVVTTYGSSETagGCVY------------- 219
Cdd:PRK05857 262 ATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSET--GCTAlclptddgsivki 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 220 ----DGQPIEGAQVAIEN-----------------GRVWLGGPMIAHGYRNAPSH-EAFHKPGWFATSDAGEIH-DGRLV 276
Cdd:PRK05857 340 eagaVGRPYPGVDVYLAAtdgigptapgagpsasfGTLWIKSPANMLGYWNNPERtAEVLIDGWVNTGDLLERReDGFFY 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 277 ITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELgdvmDGLGDAEDAGRI------ 350
Cdd:PRK05857 420 IKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEL----DESAARALKHTIaarfrr 495
|
410 420 430
....*....|....*....|....*....|..
gi 1080381800 351 --NHWMIPKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:PRK05857 496 esEPMARPSTIVIVTDIPRTQSGKVMRASLAA 527
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
69-378 |
1.96e-12 |
|
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: 68.17 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQ-----LTVDNLVSSATATHQWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVcvdVTDGFDVAAFA 143
Cdd:cd05929 133 SGGTTGRPKGIKrglpgGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLV---LMEKFDPEEFL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 144 DgaeALTSDR-AYTSLAP---MQLAKAMEEPFGAAALRLFDAVLVGGAALNPQVAARAEELGINVV-TTYGSSETAGGCV 218
Cdd:cd05929 210 R---LIERYRvTFAQFVPtmfVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIwEYYGGTEGQGLTI 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 219 YD-----------GQPIEGaQVAI--ENGR---------VW-LGGPMIAHGYRNAPSHEAFHKPGWFATSDAGEI-HDGR 274
Cdd:cd05929 287 INgeewlthpgsvGRAVLG-KVHIldEDGNevppgeigeVYfANGPGFEYTNDPEKTAAARNEGGWSTLGDVGYLdEDGY 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 275 LVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAyegIAELGDVMDGLGDAED-----AGR 349
Cdd:cd05929 366 LYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAV---VQPAPGADAGTALAEEliaflRDR 442
|
330 340
....*....|....*....|....*....
gi 1080381800 350 INHWMIPKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:cd05929 443 LSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
65-381 |
2.00e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 68.42 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 65 LVVGTSGSTGTPKGAQLTVDNLVSSATA--THQWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVcvdVTDGFD-VAA 141
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLAGllSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVV---LRRRFDpEAT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 142 FADGAEaltsDRAYTSLA-PMQLAKAMEEP------FGAAALRLfdaVLVGGAALNPQVAARA-EELGINVVTTYGSSE- 212
Cdd:PRK07788 288 LEDIAK----HKATALVVvPVMLSRILDLGpevlakYDTSSLKI---IFVSGSALSPELATRAlEAFGPVLYNLYGSTEv 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 213 ------------TAGGCVydGQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSHEAFHkpGWFATSDAGE 269
Cdd:PRK07788 361 afatiatpedlaEAPGTV--GRPPKGVTVKIldengnevprgVVGRIFVGNGFPFEGYTDGRDKQIID--GLLSSGDVGY 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 270 I-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAyegiaelgdVMDGLGDAEDAG 348
Cdd:PRK07788 437 FdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAF---------VVKAPGAALDED 507
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1080381800 349 RINHWM--------IPKDLRRVEVLPLIGPGKVDRKKVAAL 381
Cdd:PRK07788 508 AIKDYVrdnlarykVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
61-380 |
3.32e-12 |
|
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: 68.34 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQWLLAMPAYH--IAGLQVLiRSLLAGTNPVCVDVTDGF 137
Cdd:COG1020 617 DDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGlGPGDRVLQFASLSfdASVWEIF-GALLSGATLVLAPPEARR 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 138 DVAAFADgaeaLTSDRAYTSL--APMQLAKAMEEPFGA-AALRLfdaVLVGGAALNPQVAARAEEL--GINVVTTYGSSE 212
Cdd:COG1020 696 DPAALAE----LLARHRVTVLnlTPSLLRALLDAAPEAlPSLRL---VLVGGEALPPELVRRWRARlpGARLVNLYGPTE 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 213 TAGGCVYD--------------GQPIEGAQVAI--ENGRV---------WLGGPMIAHGYRNAPSHEA-------FHKPG 260
Cdd:COG1020 769 TTVDSTYYevtppdadggsvpiGRPIANTRVYVldAHLQPvpvgvpgelYIGGAGLARGYLNRPELTAerfvadpFGFPG 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 261 --WFATSDAGEIH-DGRLVITGRLDTIIdsgglKLH------PEVlERELLAIDGVTGACVVGVPHpRLGHAIVAAYEGI 331
Cdd:COG1020 849 arLYRTGDLARWLpDGNLEFLGRADDQV-----KIRgfrielGEI-EAALLQHPGVREAVVVARED-APGDKRLVAYVVP 921
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1080381800 332 AELGDVMDGLGDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:COG1020 922 EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
60-376 |
6.58e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGaqltVDNlvssataTHQWLGGEGQWLLAmpAYHIAGLQVLIRS---------------LLA 124
Cdd:PRK05691 1272 GDNLAYVIYTSGSTGQPKG----VGN-------THAALAERLQWMQA--TYALDDSDVLMQKapisfdvsvwecfwpLIT 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 125 GTNPVCVDVTDGFDVAAFAdgaeALTSDRAYTSL--APMQLAKAMEEPFGAA--ALRLfdaVLVGGAALNPQVAARAEEL 200
Cdd:PRK05691 1339 GCRLVLAGPGEHRDPQRIA----ELVQQYGVTTLhfVPPLLQLFIDEPLAAActSLRR---LFSGGEALPAELRNRVLQR 1411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 201 --GINVVTTYGSSETAGGCVY------DGQ--PI--------------EGAQVAIE-NGRVWLGGPMIAHGYRNAPSHEA 255
Cdd:PRK05691 1412 lpQVQLHNRYGPTETAINVTHwqcqaeDGErsPIgrplgnvlcrvldaELNLLPPGvAGELCIGGAGLARGYLGRPALTA 1491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 256 -------FHKPG--WFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVgVPHPRLGHAIV 325
Cdd:PRK05691 1492 erfvpdpLGEDGarLYRTGDRARWNaDGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLV 1570
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1080381800 326 AAYEGIAELGDVMDGLGDAEdAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:PRK05691 1571 GYYTGEAGQEAEAERLKAAL-AAELPEYMVPAQLIRLDQMPLGPSGKLDRR 1620
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
60-381 |
9.30e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVTDGF 137
Cdd:PRK12467 1717 PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQlsAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHR 1796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 138 DVAAFADgaeaLTSDRAYTSL--------APMQLAKAMEEPfgaAALRLfdaVLVGGAALNPQVAARA-EELGIN-VVTT 207
Cdd:PRK12467 1797 DPEQLIQ----LIERQQVTTLhfvpsmlqQLLQMDEQVEHP---LSLRR---VVCGGEALEVEALRPWlERLPDTgLFNL 1866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 208 YGSSETA---------------GGCVYDGQPIEGAQVAIEN-----------GRVWLGGPMIAHGYRNAPSHEA------ 255
Cdd:PRK12467 1867 YGPTETAvdvthwtcrrkdlegRDSVPIGQPIANLSTYILDaslnpvpigvaGELYLGGVGLARGYLNRPALTAerfvad 1946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 256 -FHKPG--WFATSDAGEIH-DGRLVITGRLDTIIDSGGLKL-----------HPEVLERELLAIDGVTGACVVG--VPhp 318
Cdd:PRK12467 1947 pFGTVGsrLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIelgeiearlreQGGVREAVVIAQDGANGKQLVAyvVP-- 2024
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080381800 319 rLGHAIVAAYEGIAELGDVmdgLGDAEDAgRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAAL 381
Cdd:PRK12467 2025 -TDPGLVDDDEAQVALRAI---LKNHLKA-SLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
156-376 |
1.37e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.78 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 156 TSLAPMQLA---KAMEEPFGAAALRLFDAVLVGGAALNPQVAAR-AEELGINVVTTYGSSEtagGCV-Y----------- 219
Cdd:PRK10946 276 TALVPPAVSlwlQAIAEGGSRAQLASLKLLQVGGARLSETLARRiPAELGCQLQQVFGMAE---GLVnYtrlddsderif 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 220 --DGQPI-----------EGAQVAI-ENGRVWLGGPMIAHGYRNAPSH--EAFHKPGWFATSDAGEI-HDGRLVITGRLD 282
Cdd:PRK10946 353 ttQGRPMspddevwvadaDGNPLPQgEVGRLMTRGPYTFRGYYKSPQHnaSAFDANGFYCSGDLVSIdPDGYITVVGREK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 283 TIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEGI--AELGDVMDGLGDAEdagrinhWMIPK 357
Cdd:PRK10946 433 DQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEkscAFLVVKEPLkaVQLRRFLREQGIAE-------FKLPD 505
|
250
....*....|....*....
gi 1080381800 358 DLRRVEVLPLIGPGKVDRK 376
Cdd:PRK10946 506 RVECVDSLPLTAVGKVDKK 524
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
65-326 |
1.38e-11 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 65.02 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 65 LVVGTSGSTGTPKGAQLTVDNLVSSAT--ATHQWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVTDGFDVAAF 142
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALvlAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 143 ADgAEALTSdrAYtsLAPMQLAKAMEepfgAAALRLFDAvlvggAALNPQVAARAEELGINVVTT--------YGSSETA 214
Cdd:cd17636 84 IE-AERCTH--AF--LLPPTIDQIVE----LNADGLYDL-----SSLRSSPAAPEWNDMATVDTSpwgrkpggYGQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 215 GGCVYD----------GQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAPSHEAF-HKPGWFATSDAGE-IH 271
Cdd:cd17636 150 GLATFAalgggaiggaGRPSPLVQVRIldedgrevpdgEVGEIVARGPTVMAGYWNRPEVNARrTRGGWHHTNDLGRrEP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1080381800 272 DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:cd17636 230 DGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKA 284
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
48-376 |
2.04e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.39 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 48 ILRNSQRAGEPIDESIALVVG------TSGSTGTPKGAQLTVDNLVSSATATHQWLGGE--GQ--WLLAMPAYHIAGLQV 117
Cdd:PLN02330 165 LLEAADRAGDTSDNEEILQTDlcalpfSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEmiGQvvTLGLIPFFHIYGITG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 118 LIRSLLAGTNPVCvdVTDGFDVAAFADGaeALTSDRAYTSLAP---MQLAK-AMEEPFGAAALRLfDAVLVGGAALNPQV 193
Cdd:PLN02330 245 ICCATLRNKGKVV--VMSRFELRTFLNA--LITQEVSFAPIVPpiiLNLVKnPIVEEFDLSKLKL-QAIMTAAAPLAPEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 194 --AARAEELGINVVTTYGSSETAGGCVYDGQPIEGAQVAIEN---------------------------GRVWLGGPMIA 244
Cdd:PLN02330 320 ltAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAKKNsvgfilpnlevkfidpdtgrslpkntpGELCVRSQCVM 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 245 HGYRNAPSHEA--FHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG 321
Cdd:PLN02330 400 QGYYNNKEETDrtIDEDGWLHTGDIGYIdDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAG 479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080381800 322 H----AIVAAYEGIAELGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:PLN02330 480 EipaaCVVINPKAKESEEDILNFV-----AANVAHYKKVRVVQFVDSIPKSLSGKIMRR 533
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
18-317 |
2.34e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 65.15 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 18 PTAILPDLR--AALDGEVSLLPVPLHDGTRASILRNSQR----AGEPIDESIALVV--GTSGSTGTPKGAQLTVDNLVSS 89
Cdd:PRK06164 130 PPDALPPLRaiAVVDDAADATPAPAPGARVQLFALPDPAppaaAGERAADPDAGALlfTTSGTTSGPKLVLHRQATLLRH 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 90 ATATHQWLG-GEGQWLLAM-PAYHIAGLQVLIRSLLAGTNPVCVDVTDGFDVAAFADGAE---ALTSDRAYTslapmQLA 164
Cdd:PRK06164 210 ARAIARAYGyDPGAVLLAAlPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRvthTFGNDEMLR-----RIL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 165 KAMEEPFGAAALRLFdavlvGGAALNP---QVAARAEELGINVVTTYGSSET----AGGCVYD---------GQPIEG-A 227
Cdd:PRK06164 285 DTAGERADFPSARLF-----GFASFAPalgELAALARARGVPLTGLYGSSEVqalvALQPATDpvsvrieggGRPASPeA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 228 QVAI------------ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKL 292
Cdd:PRK06164 360 RVRArdpqdgallpdgESGEIEIRAPSLMRGYLDNPdaTARALTDDGYFRTGDLGYTrGDGQFVYQTRMGDSLRLGGFLV 439
|
330 340
....*....|....*....|....*
gi 1080381800 293 HPEVLERELLAIDGVTGACVVGVPH 317
Cdd:PRK06164 440 NPAEIEHALEALPGVAAAQVVGATR 464
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
62-377 |
2.72e-11 |
|
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: 64.66 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 62 SIALVVGTSGSTGTPKGAQLT---VDNLVSSATATHqWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVTDGFD 138
Cdd:cd17655 138 DLAYVIYTSGSTGKPKGVMIEhrgVVNLVEWANKVI-YQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 139 VAAFAdgaEALTSDRA-YTSLAP--MQLAKAMEEPFGAAALRLfdavLVGGAALNPQVAARAEEL---GINVVTTYGSSE 212
Cdd:cd17655 217 GQALT---QYIRQNRItIIDLTPahLKLLDAADDSEGLSLKHL----IVGGEALSTELAKKIIELfgtNPTITNAYGPTE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 213 TAGGC---VYD-----------GQPIEGAQVAI--ENGRV---------WLGGPMIAHGYRNAP--SHEAF----HKPG- 260
Cdd:cd17655 290 TTVDAsiyQYEpetdqqvsvpiGKPLGNTRIYIldQYGRPqpvgvagelYIGGEGVARGYLNRPelTAEKFvddpFVPGe 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 261 -WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRlGHAIVAAY---EGIAELG 335
Cdd:cd17655 370 rMYRTGDlARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQ-GQNYLCAYivsEKELPVA 448
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1080381800 336 DVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd17655 449 QLREFL-----ARELPDYMIPSYFIKLDEIPLTPNGKVDRKA 485
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
69-378 |
5.13e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 63.91 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLT-------VDNLVSSAT--ATHQwlggeGQWLLAMPAYHIAGLQVLIRsLLAGTNPVCVdVTDGFDV 139
Cdd:PRK07470 171 TSGTTGRPKAAVLThgqmafvITNHLADLMpgTTEQ-----DASLVVAPLSHGAGIHQLCQ-VARGAATVLL-PSERFDP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 140 AAFADGAEALTSDRAYTslAPMQLAKAMEEP----FGAAALRLfdaVLVGGAALNPQVAARA-EELGINVVTTYGSSETA 214
Cdd:PRK07470 244 AEVWALVERHRVTNLFT--VPTILKMLVEHPavdrYDHSSLRY---VIYAGAPMYRADQKRAlAKLGKVLVQYFGLGEVT 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 215 GG------CVYD------------GQPIEGAQVAI-----------ENGRVWLGGPMIAHGYRNAP--SHEAFhKPGWFA 263
Cdd:PRK07470 319 GNitvlppALHDaedgpdarigtcGFERTGMEVQIqddegrelppgETGEICVIGPAVFAGYYNNPeaNAKAF-RDGWFR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 264 TSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEGI----AELG 335
Cdd:PRK07470 398 TGDLGHLDaRGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEvgvAVCVARDGApvdeAELL 477
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1080381800 336 DVMDglgdaedaGRINHWMIPKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:PRK07470 478 AWLD--------GKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
54-382 |
5.22e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.86 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 54 RAGEPIDE------SIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ------WLlamPAYHIAGL-QVLIR 120
Cdd:PRK07768 139 LAADPIDPvetgedDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtdvmvsWL---PLFHDMGMvGFLTV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 121 SLLAGTNPVCVDVTDgFdVAAFADGAEALTSDR---------AYTSLAPMQLAKAMEEPFGAAALRLfdaVLVGGAALNP 191
Cdd:PRK07768 216 PMYFGAELVKVTPMD-F-LRDPLLWAELISKYRgtmtaapnfAYALLARRLRRQAKPGAFDLSSLRF---ALNGAEPIDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 192 QVAARAEELGIN-------VVTTYGSSETA---------GGCVYD---------------------------GQPIEGAQ 228
Cdd:PRK07768 291 ADVEDLLDAGARfglrpeaILPAYGMAEATlavsfspcgAGLVVDevdadllaalrravpatkgntrrlatlGPPLPGLE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 229 VAI-----------ENGRVWLGGPMIAHGYRNAPSHEAFHKP-GWFATSDAGEIHD-GRLVITGRLDTIIDSGGLKLHPE 295
Cdd:PRK07768 371 VRVvdedgqvlpprGVGVIELRGESVTPGYLTMDGFIPAQDAdGWLDTGDLGYLTEeGEVVVCGRVKDVIIMAGRNIYPT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 296 VLERELLAIDGVTGACVVGVPHPRlGHaivaAYEGIAELGDVMDGlGDAEDAGRINHWMIPKDLRRVEVLP----LIGP- 370
Cdd:PRK07768 451 DIERAAARVEGVRPGNAVAVRLDA-GH----SREGFAVAVESNAF-EDPAEVRRIRHQVAHEVVAEVGVRPrnvvVLGPg 524
|
410
....*....|....*....
gi 1080381800 371 -------GKVDRKKVAALF 382
Cdd:PRK07768 525 sipktpsGKLRRANAAELV 543
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
27-378 |
5.82e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 27 AALDGEVSL----LPVPLHDGTR----ASILRNSQRAGEPIDESI--ALVVGTSGSTGTPKGAQLTV---------DNLV 87
Cdd:PRK13390 104 AALDGLAAKvgadLPLRLSFGGEidgfGSFEAALAGAGPRLTEQPcgAVMLYSSGTTGFPKGIQPDLpgrdvdapgDPIV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 88 SSATATHQwLGGEGQWLLAMPAYHIAGLQ-VLIRSLLAGTnpvcVDVTDGFDVAAFADGAEALTSdrAYTSLAP------ 160
Cdd:PRK13390 184 AIARAFYD-ISESDIYYSSAPIYHAAPLRwCSMVHALGGT----VVLAKRFDAQATLGHVERYRI--TVTQMVPtmfvrl 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 161 MQLAKAMEEPFGAAALRlfdAVLVGGAALNPQVA-ARAEELGINVVTTYGSSETAGGCVYD-----------GQPIEGAQ 228
Cdd:PRK13390 257 LKLDADVRTRYDVSSLR---AVIHAAAPCPVDVKhAMIDWLGPIVYEYYSSTEAHGMTFIDspdwlahpgsvGRSVLGDL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 229 ----------VAIENGRVWLGGPMIAHGYRNAP--SHEAFH--KPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLH 293
Cdd:PRK13390 334 hicdddgnelPAGRIGTVYFERDRLPFRYLNDPekTAAAQHpaHPFWTTVGDLGSVdEDGYLYLADRKSFMIISGGVNIY 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 294 PEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEGIAELGDVMDGLGDAEDAgRINHWMIPKDLRRVEVLPLIGP 370
Cdd:PRK13390 414 PQETENALTMHPAVHDVAVIGVPDPEMGEqvkAVIQLVEGIRGSDELARELIDYTRS-RIAHYKAPRSVEFVDELPRTPT 492
|
....*...
gi 1080381800 371 GKVDRKKV 378
Cdd:PRK13390 493 GKLVKGLL 500
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
23-366 |
7.42e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 63.38 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 23 PDLRAALDGEVSLLPVPL---------HDGTRA-SILRNSQRAGEPIDESI-ALVVGTSGSTGTPKG-------AQLTVD 84
Cdd:PRK08276 91 AALADTAAELAAELPAGVplllvvagpVPGFRSyEEALAAQPDTPIADETAgADMLYSSGTTGRPKGikrplpgLDPDEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 85 NLVSSATATHQWLGGEGQ-WLLAMPAYHIAGLQVLIRSL-LAGTnpvcVDVTDGFDvaafADGAEALTsDR---AYTSLA 159
Cdd:PRK08276 171 PGMMLALLGFGMYGGPDSvYLSPAPLYHTAPLRFGMSALaLGGT----VVVMEKFD----AEEALALI-ERyrvTHSQLV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 160 PMQ------LAKAMEEPFGAAALRlfdaVLVGGAALNPQVAARA--EELGINVVTTYGSSETAGGCVYD----------- 220
Cdd:PRK08276 242 PTMfvrmlkLPEEVRARYDVSSLR----VAIHAAAPCPVEVKRAmiDWWGPIIHEYYASSEGGGVTVITsedwlahpgsv 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 221 GQPIEGaQVAI-----------ENGRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGR-LDTII 285
Cdd:PRK08276 318 GKAVLG-EVRIldedgnelppgEIGTVYFEMDGYPFEYHNDPekTAAARNPHGWVTVGDVGYLdEDGYLYLTDRkSDMII 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 286 dSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEgiaelgdVMDG--LGDAEDA-------GRINHWMIP 356
Cdd:PRK08276 397 -SGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQ-------PADGadAGDALAAeliawlrGRLAHYKCP 468
|
410
....*....|
gi 1080381800 357 KDLRRVEVLP 366
Cdd:PRK08276 469 RSIDFEDELP 478
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
61-373 |
8.68e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 63.44 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGG--EGQWLLAMPAYHIAGLQ-VLIRSLLAGTNPVCVDVTDGf 137
Cdd:PRK08314 190 DDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNStpESVVLAVLPLFHVTGMVhSMNAPIYAGATVVLMPRWDR- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 138 DVAAFADGAEALTSdraYTSLAPMqlakaMEEPFGAAALRLFD----AVLVGGAALNPQ-VAARAEEL-GINVVTTYGSS 211
Cdd:PRK08314 269 EAAARLIERYRVTH---WTNIPTM-----VVDFLASPGLAERDlsslRYIGGGGAAMPEaVAERLKELtGLDYVEGYGLT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 212 ETAG------------GC-----------VYDgqPIEGAQVAI-ENGRVWLGGPMIAHGYRNAP--SHEAFHKPG---WF 262
Cdd:PRK08314 341 ETMAqthsnppdrpklQClgiptfgvdarVID--PETLEELPPgEVGEIVVHGPQVFKGYWNRPeaTAEAFIEIDgkrFF 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 263 ATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAayegiaeLGDVM 338
Cdd:PRK08314 419 RTGDLGRMdEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGEtvkAVVV-------LRPEA 491
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1080381800 339 DGLGDAEDagrINHW----M----IPKDLRRVEVLPLIGPGKV 373
Cdd:PRK08314 492 RGKTTEEE---IIAWarehMaaykYPRIVEFVDSLPKSGSGKI 531
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
42-377 |
1.61e-10 |
|
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: 62.33 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 42 DGTRASILRNSQRAGEPidesiALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQWLLAM--PAYHiAGLQVL 118
Cdd:cd17653 91 RTSGATLLLTTDSPDDL-----AYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDvGPGSRVAQVlsIAFD-ACIGEI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 119 IRSLLAGTNPVCVDVTDgfDVAAFADGAEALTSdraytslAPMQLAKAMEEPFGAaalrlFDAVLVGGAALnPQVAARAE 198
Cdd:cd17653 165 FSTLCNGGTLVLADPSD--PFAHVARTVDALMS-------TPSILSTLSPQDFPN-----LKTIFLGGEAV-PPSLLDRW 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 199 ELGINVVTTYGSSETAGGCVYD----------GQPIEGAQVAI-----------ENGRVWLGGPMIAHGY--RNAPSHEA 255
Cdd:cd17653 230 SPGRRLYNAYGPTECTISSTMTellpgqpvtiGKPIPNSTCYIldadlqpvpegVVGEICISGVQVARGYlgNPALTASK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 256 FH----KPGW--FATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDG-VTGACVVGVphprlGHAIVAA 327
Cdd:cd17653 310 FVpdpfWPGSrmYRTGDYGRWtEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPeVTQAAAIVV-----NGRLVAF 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1080381800 328 YegiAELGDVMDGLgDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd17653 385 V---TPETVDVDGL-RSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKA 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
61-380 |
2.65e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.28 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQWLLA-MPAYHIAGLQVLIRSLLAGTNPVCVDVTDGFD 138
Cdd:PRK12316 655 ENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGlGVGDTVLQkTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 139 VAAFadgAEALTSDRAYT-SLAPMQLAKAMEEPFGAAALRLFDAVLVGGA---ALNPQVAARAEELGInvVTTYGSSETA 214
Cdd:PRK12316 735 PAKL---VELINREGVDTlHFVPSMLQAFLQDEDVASCTSLRRIVCSGEAlpaDAQEQVFAKLPQAGL--YNLYGPTEAA 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 215 ------------GGCVYDGQPIEGAQVAIEN-----------GRVWLGGPMIAHGY--RNAPSHEAFhKPGWFA------ 263
Cdd:PRK12316 810 idvthwtcveegGDSVPIGRPIANLACYILDanlepvpvgvlGELYLAGRGLARGYhgRPGLTAERF-VPSPFVagermy 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 264 -TSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEGIAELGDVMDGL 341
Cdd:PRK12316 889 rTGDlARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDWREALKAHL 968
|
330 340 350
....*....|....*....|....*....|....*....
gi 1080381800 342 gdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:PRK12316 969 -----AASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
61-376 |
3.22e-10 |
|
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: 61.30 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDVTDGFD 138
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGitSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 139 VAAFADGAE-----ALTSDRAYTSLAPMQLAKAMEEpfGAAALRLfdaVLVGGAALNPQ-VAARAEELG--INVVTTYGS 210
Cdd:cd17644 186 LEDFVQYIQqwqltVLSLPPAYWHLLVLELLLSTID--LPSSLRL---VIVGGEAVQPElVRQWQKNVGnfIQLINVYGP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 211 SE-TAGGCVYD--------------GQPIEGAQVAI--EN---------GRVWLGGPMIAHGYRNAP--------SHEAF 256
Cdd:cd17644 261 TEaTIAATVCRltqlternitsvpiGRPIANTQVYIldENlqpvpvgvpGELHIGGVGLARGYLNRPeltaekfiSHPFN 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 257 HKPG--WFATSDAGE-IHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHP----RLGHAIVAAYE 329
Cdd:cd17644 341 SSESerLYKTGDLARyLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQpgnkRLVAYIVPHYE 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1080381800 330 GIAELGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd17644 421 ESPSTVELRQFL-----KAKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
69-376 |
3.38e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 61.31 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQ----WLGGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVdvtdgfdvAAFAD 144
Cdd:PRK06018 185 TSGTTGDPKGVLYSHRSNVLHALMANNgdalGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMP--------GAKLD 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 145 GA---EALTSDR-AYTSLAP---MQLAKAMEEPfgAAALRLFDAVLVGGAALnPQVAARA-EELGINVVTTYGSSETA-- 214
Cdd:PRK06018 257 GAsvyELLDTEKvTFTAGVPtvwLMLLQYMEKE--GLKLPHLKMVVCGGSAM-PRSMIKAfEDMGVEVRHAWGMTEMSpl 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 215 ----------GGCVYD---------GQPIEGAQVAIEN-------------GRVWLGGPMIAHGYRNAPSHeAFHKPGWF 262
Cdd:PRK06018 334 gtlaalkppfSKLPGDarldvlqkqGYPPFGVEMKITDdagkelpwdgktfGRLKVRGPAVAAAYYRVDGE-ILDDDGFF 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 263 ATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHA---IVAAYEGI----AEL 334
Cdd:PRK06018 413 DTGDVATIdAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERpllIVQLKPGEtatrEEI 492
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1080381800 335 GDVMDGlgdaedagRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:PRK06018 493 LKYMDG--------KIAKWWMPDDVAFVDAIPHTATGKILKT 526
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
59-382 |
4.03e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 61.34 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 59 IDESIALVVGTS-GSTGTPKGAQLTVDNL---------VSSATATHqwlgGEgQWLLAMPAYHIAGLQVLIRSLLAGTnP 128
Cdd:PRK05620 178 LDETTAAAICYStGTTGAPKGVVYSHRSLylqslslrtTDSLAVTH----GE-SFLCCVPIYHVLSWGVPLAAFMSGT-P 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 129 VcvdVTDGFDVAA-------------FADGAEALtsdraYTSLapmqLAKAMEEPFGAAALRlfdAVLVGGAALNPQVAA 195
Cdd:PRK05620 252 L---VFPGPDLSAptlakiiatamprVAHGVPTL-----WIQL----MVHYLKNPPERMSLQ---EIYVGGSAVPPILIK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 196 RAEE-LGINVVTTYGSSET-------------AGGC-------------------VYDGQPIEGAQVaiENGRVWLGGPM 242
Cdd:PRK05620 317 AWEErYGVDVVHVWGMTETspvgtvarppsgvSGEArwayrvsqgrfpasleyriVNDGQVMESTDR--NEGEIQVRGNW 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 243 IAHGYRNAPSHEA------------------FHKPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLA 303
Cdd:PRK05620 395 VTASYYHSPTEEGggaastfrgedvedandrFTADGWLRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMA 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 304 IDGVTGACVVGVPHPRLGH---AIVAAYEGI------AElgDVMDGLGDaedagRINHWMIPKDLRRVEVLPLIGPGKVD 374
Cdd:PRK05620 475 APEVVECAVIGYPDDKWGErplAVTVLAPGIeptretAE--RLRDQLRD-----RLPNWMLPEYWTFVDEIDKTSVGKFD 547
|
....*...
gi 1080381800 375 RKKVAALF 382
Cdd:PRK05620 548 KKDLRQHL 555
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
40-376 |
4.33e-10 |
|
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: 61.03 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 40 LHDGTRASILRNSqragepidESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQW--LGGEGQWLLAMPAYHIAGLQV 117
Cdd:cd17645 91 LADSSAKILLTNP--------DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYfgVTPADKSLVYASFSFDASAWE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 118 LIRSLLAGTNPVCVDVTDGFDVAAFADGAEaltSDRAYTSLAPMQLAkameEPFGAAALRLFDAVLVGGAALNpqvaaRA 197
Cdd:cd17645 163 IFPHLTAGAALHVVPSERRLDLDALNDYFN---QEGITISFLPTGAA----EQFMQLDNQSLRVLLTGGDKLK-----KI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 198 EELGINVVTTYGSSETA-----------GGCVYDGQPIEGAQVAIEN-----------GRVWLGGPMIAHGYRNAP--SH 253
Cdd:cd17645 231 ERKGYKLVNNYGPTENTvvatsfeidkpYANIPIGKPIDNTRVYILDealqlqpigvaGELCIAGEGLARGYLNRPelTA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 254 EAF----HKPG--WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:cd17645 311 EKFivhpFVPGerMYRTGDlAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVA 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1080381800 327 AY--EGIAELGDVMDGLGDAedagrINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd17645 391 YVtaPEEIPHEELREWLKND-----LPDYMIPTYFVHLKALPLTANGKVDRK 437
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
61-376 |
7.48e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.13 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQW--LGGEGQWLLAMP-AYHIAGLQvLIRSLLAGTNPVCVDVTDGF 137
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERyeLTPDDRVLQFMSfSFDGSHEG-LYHPLINGASVVIRDDSLWD 4772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 138 DVAAFADGAEALTSDRAYTSLAPMQLAKAMEEPFGAAALRlfdAVLVGGAALNPQVAARAEELGINV--VTTYGSSETA- 214
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR---VYCFGGEAVAQASYDLAWRALKPVylFNGYGPTETTv 4849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 215 ------------GGCVYD--GQPIEGAQVAIEN-----------GRVWLGGPMIAHGYrnapsheaFHKPGW----FATS 265
Cdd:PRK12316 4850 tvllwkardgdaCGAAYMpiGTPLGNRSGYVLDgqlnplpvgvaGELYLGGEGVARGY--------LERPALtaerFVPD 4921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 266 DAGEiHDGRLVITG-----RLDTIIDSGG---------------------LKLHPEVLERELLAIDGVTGACVVGVPHPR 319
Cdd:PRK12316 4922 PFGA-PGGRLYRTGdlaryRADGVIDYLGrvdhqvkirgfrielgeiearLREHPAVREAVVIAQEGAVGKQLVGYVVPQ 5000
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080381800 320 lGHAIVAAYEGIAELGDVMdglgDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:PRK12316 5001 -DPALADADEAQAELRDEL----KAALRERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
15-382 |
7.56e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 60.44 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 15 PHNPTAILPDL----RAALDGEVSLLPVpLHDGTRASilrnsqRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSA 90
Cdd:PRK06178 166 PAEPTLPLPDSlrapRLAAAGAIDLLPA-LRACTAPV------PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 91 TATHQWLGGEGQ---WLLAMPAYHIAGLQV-LIRSLLAGTNPVCVDVTDgfdvaafADGAEALTSDRAYTSLAPM--QLA 164
Cdd:PRK06178 239 AAAYAVAVVGGEdsvFLSFLPEFWIAGENFgLLFPLFSGATLVLLARWD-------AVAFMAAVERYRVTRTVMLvdNAV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 165 KAMEEP-FGAAALRLFDAVLVGG--AALNPQVAARAEELGINVVT--TYGSSET-----------------AGGCVYDGQ 222
Cdd:PRK06178 312 ELMDHPrFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAeaAWGMTEThtcdtftagfqdddfdlLSQPVFVGL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 223 PIEGAQVAI---ENGR-VWLGG--------PMIAHGYRNAP--SHEAFhKPGWFATSDAGEI-HDGRLVITGRLDTIIDS 287
Cdd:PRK06178 392 PVPGTEFKIcdfETGElLPLGAegeivvrtPSLLKGYWNKPeaTAEAL-RDGWLHTGDIGKIdEQGFLHYLGRRKEMLKV 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 288 GGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAyegiaelgdVMDGLGDAEDAGRINHW----M----IPkDL 359
Cdd:PRK06178 471 NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAF---------VQLKPGADLTAAALQAWcrenMavykVP-EI 540
|
410 420
....*....|....*....|...
gi 1080381800 360 RRVEVLPLIGPGKVDRKKVAALF 382
Cdd:PRK06178 541 RIVDALPMTATGKVRKQDLQALA 563
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-376 |
1.94e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.79 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQW--LGGEGQWLLAMP-AYHIAGLQVLiRSLLAGTnpvCVDVTDGf 137
Cdd:PRK12467 3237 ENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAyeLDANDRVLLFMSfSFDGAQERFL-WTLICGG---CLVVRDN- 3311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 138 DVAAFADGAEALTSDRAYTSLAPMQLAKAMEEPFGAAALRLFDAVLVGGAALNP----QVAARAEELGInvVTTYGSSET 213
Cdd:PRK12467 3312 DLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPaafeQVKRKLKPRGL--TNGYGPTEA 3389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 214 A-----GGCVYDGQPIE-----GAQVA------IEN----------GRVWLGGPMIAHGYRNAPSHEA-------FHKPG 260
Cdd:PRK12467 3390 VvtvtlWKCGGDAVCEApyapiGRPVAgrsiyvLDGqlnpvpvgvaGELYIGGVGLARGYHQRPSLTAerfvadpFSGSG 3469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 261 --WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRlGHAIVAAYEGIAELGDV 337
Cdd:PRK12467 3470 grLYRTGDlARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAG-GKQLVAYVVPADPQGDW 3548
|
330 340 350
....*....|....*....|....*....|....*....
gi 1080381800 338 MDGLGDaEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:PRK12467 3549 RETLRD-HLAASLPDYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
58-357 |
2.32e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 59.09 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 58 PIDE--SIALVVgTSGSTGTPKGAQLTVDN-LVSSATATHQWLGGEGQ-WLLAMPAYHIAG-LQVLIRSLLAGTNPVCVD 132
Cdd:PLN02479 191 PADEwqSIALGY-TSGTTASPKGVVLHHRGaYLMALSNALIWGMNEGAvYLWTLPMFHCNGwCFTWTLAALCGTNICLRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 133 VTdgfdvaafadgAEALTSDRAYTSL-----APMQLAKAMEEPFGAAALRLFDA--VLVGGAALNPQVAARAEELGINVV 205
Cdd:PLN02479 270 VT-----------AKAIYSAIANYGVthfcaAPVVLNTIVNAPKSETILPLPRVvhVMTAGAAPPPSVLFAMSEKGFRVT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 206 TTYGSSETAGG---CV----YDGQPIE---------GAQ-VAIEN-------------------GRVWLGGPMIAHGYRN 249
Cdd:PLN02479 339 HTYGLSETYGPstvCAwkpeWDSLPPEeqarlnarqGVRyIGLEGldvvdtktmkpvpadgktmGEIVMRGNMVMKGYLK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 250 AP--SHEAFHKpGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:PLN02479 419 NPkaNEEAFAN-GWFHSGDLGVKHpDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCA 497
|
330 340 350
....*....|....*....|....*....|....*....
gi 1080381800 327 ayegIAELGDVMDGLGDAEDAG--------RINHWMIPK 357
Cdd:PLN02479 498 ----FVTLKPGVDKSDEAALAEdimkfcreRLPAYWVPK 532
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
61-307 |
2.91e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 58.65 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ-----WL-----LAMPAYH----IAGLQVLI------- 119
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKdrilsWMplthdMGLIAFHlaplIAGMNQYLmptrlfi 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 120 -------------------------RSLLAGTNPVCVDVTDGFDVAAFADGAEALTS---DRAYTSLAPMQLAK-AMEEP 170
Cdd:cd05908 186 rrpilwlkkasehkativsspnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYelcHEFLDHMSKYGLKRnAILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 171 FGAAALRLfdavlvgGAALNPQ--------VAARAEELGINVVTTYGSSETAGGCVYDGQPIEGAQVAIEN--------- 233
Cdd:cd05908 266 YGLAEASV-------GASLPKAqspfktitLGRRHVTHGEPEPEVDKKDSECLTFVEVGKPIDETDIRICDednkilpdg 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080381800 234 --GRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGV 307
Cdd:cd05908 339 yiGHIQIRGKNVTPGYYNNPeaTAKVFTDDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGV 416
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
30-377 |
4.62e-09 |
|
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: 57.87 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 30 DGEVSLLPVPLHDGTRASILRnsqragepIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATathqwlggegqwllampa 109
Cdd:cd17654 95 NKELDNAPLSFTPEHRHFNIR--------TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQ------------------ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 110 yHIAGLQVLIRS-LLAGTNPVCVDVTDGFDVAAFADGAEALTSDRAYTSLaPMQLAKAMEEPFG-------AAALRLFDA 181
Cdd:cd17654 149 -HFRSLFNITSEdILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVL-PSKLADILFKRHRitvlqatPTLFRRFGS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 182 V----------------LVGGAALnPQ----VAARAEELGINVVTTYGSSETAGGCVYD-----------GQPIEGAQVA 230
Cdd:cd17654 227 QsikstvlsatsslrvlALGGEPF-PSlvilSSWRGKGNRTRIFNIYGITEVSCWALAYkvpeedspvqlGSPLLGTVIE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 231 IEN-------GRVWLGGpMIAHGYRNAPSHEAFHKpgWFATSDAGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLA 303
Cdd:cd17654 306 VRDqngsegtGQVFLGG-LNRVCILDDEVTVPKGT--MRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIES 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 304 IDGVTGACVVGVPHPRLgHAIVAAYEGIAELGD--VMDGLGDAEdagrinhwmIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd17654 383 CLGVESCAVTLSDQQRL-IAFIVGESSSSRIHKelQLTLLSSHA---------IPDTFVQIDKLPLTSHGKVDKSE 448
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
69-326 |
5.87e-09 |
|
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: 57.59 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQWL----GGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVD-VTDGFDVAAFA 143
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVfdygPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWPTPARMW 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 144 D-----GAEAL-TSDRAYTSLAPMQlAKAMEEpFGAAALRLFDAVlvgGAALNPQVAARAEEL----GINVVTTYGSSET 213
Cdd:cd17634 320 QvvdkhGVNILyTAPTAIRALMAAG-DDAIEG-TDRSSLRILGSV---GEPINPEAYEWYWKKigkeKCPVVDTWWQTET 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 214 AGGCV---------------------------YDGQPIEGAQVaienGRVWLGGP---MIAHGYRNAPSHEAFHKP---G 260
Cdd:cd17634 395 GGFMItplpgaielkagsatrpvfgvqpavvdNEGHPQPGGTE----GNLVITDPwpgQTRTLFGDHERFEQTYFStfkG 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080381800 261 WFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:cd17634 471 MYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
61-376 |
7.34e-09 |
|
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: 57.09 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLvssATATHQWlggEGQWLLAmpAYHIAGLQV-----------LIRSLLAGTNPV 129
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNV---AHAAHAW---RREYELD--SFPVRLLQMasfsfdvfagdFARSLLNGGTLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 130 CVDVTDGFDVAAFADgaeALTSDRAYTSLAPMQLAKAM-----EEPFGAAALRLFDAVLVGGAALNPQVAARAEELGINV 204
Cdd:cd17650 165 ICPDEVKLDPAALYD---LILKSRITLMESTPALIRPVmayvyRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 205 VTTYGSSETAGGCVY----DGQPIEGAQVAIEN----------------------GRVWLGGPMIAHGYRNAP--SHEAF 256
Cdd:cd17650 242 INSYGVTEATIDSTYyeegRDPLGDSANVPIGRplpntamyvlderlqpqpvgvaGELYIGGAGVARGYLNRPelTAERF 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 257 ----HKPG--WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGAcVVGVPHPRLGHAIVAAYE 329
Cdd:cd17650 322 venpFAPGerMYRTGDlARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEA-VVAVREDKGGEARLCAYV 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1080381800 330 GIAELGDVMDGlgDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd17650 401 VAAATLNTAEL--RAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
61-326 |
1.04e-08 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 56.77 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSA-------TATHQWLGGEGQWLLAMPAYHIAGLQVLIRSLLA-GTNPVC-- 130
Cdd:PLN02574 198 DDVAAIMYSSGTTGASKGVVLTHRNLIAMVelfvrfeASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVmr 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 131 -------VDVTDGFDVAAFADGAEALTS-DRAYTSLAPMQLAKAMEEPFGAAALR---------------------LFDA 181
Cdd:PLN02574 278 rfdasdmVKVIDRFKVTHFPVVPPILMAlTKKAKGVCGEVLKSLKQVSCGAAPLSgkfiqdfvqtlphvdfiqgygMTES 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 182 VLVGGAALNPQVAARAEELGI-------NVVT-TYGSSETAGGCvydgqpiegaqvaienGRVWLGGPMIAHGYRNAPSH 253
Cdd:PLN02574 358 TAVGTRGFNTEKLSKYSSVGLlapnmqaKVVDwSTGCLLPPGNC----------------GELWIQGPGVMKGYLNNPKA 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 254 EAFH--KPGWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:PLN02574 422 TQSTidKDGWLRTGDIAYFdEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVA 497
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
18-379 |
1.92e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 56.06 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 18 PTAILpdlrAALDGEVSLLPVPLHDgtrASILRNSQRAGEPIDESiALVVG--------TSGSTGTPKGAQLTVDNLVSS 89
Cdd:PRK04813 100 PSLII----ATEELPLEILGIPVIT---LDELKDIFATGNPYDFD-HAVKGddnyyiifTSGTTGKPKGVQISHDNLVSF 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 90 AtathQWLG-----GEGQWLLAMPAYHIaGLQV--LIRSLLAGTNPVCV--DVTDGF----------DVAA------FAD 144
Cdd:PRK04813 172 T----NWMLedfalPEGPQFLNQAPYSF-DLSVmdLYPTLASGGTLVALpkDMTANFkqlfetlpqlPINVwvstpsFAD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 145 ---GAEALTSDRaYTSLA---------PMQLAKAMEEPFGAAalRLFDA-------VLVGGAALNPQVAARAEELGINVV 205
Cdd:PRK04813 247 mclLDPSFNEEH-LPNLThflfcgeelPHKTAKKLLERFPSA--TIYNTygpteatVAVTSIEITDEMLDQYKRLPIGYA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 206 ----TTYGSSEtaggcvyDGQPIEgaqvAIENGRVWLGGPMIAHGYRNAPSHEA---FHKPGWFA--TSDAGEIHDGRLV 276
Cdd:PRK04813 324 kpdsPLLIIDE-------EGTKLP----DGEQGEIVISGPSVSKGYLNNPEKTAeafFTFDGQPAyhTGDAGYLEDGLLF 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 277 ITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVvgVPHPRLG--HAIVAA-------YEGIAELGDVMdglgDAEDA 347
Cdd:PRK04813 393 YQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV--VPYNKDHkvQYLIAYvvpkeedFEREFELTKAI----KKELK 466
|
410 420 430
....*....|....*....|....*....|..
gi 1080381800 348 GRINHWMIPKDLRRVEVLPLIGPGKVDRKKVA 379
Cdd:PRK04813 467 ERLMEYMIPRKFIYRDSLPLTPNGKIDRKALI 498
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
46-315 |
1.93e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 56.19 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 46 ASILRNSQRAG----EPID-ESIALVVGTSGSTGTPKGA---QLTVDNLVSSATATHQWLGGEGQWLLAMPAYHIAGLQV 117
Cdd:PRK06060 125 AELMSEAARVApggyEPMGgDALAYATYTSGTTGPPKAAihrHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 118 LIRSLLA-GTNPVCVDVTDGFDVAAfadgaeaLTSDRAYTSL---APMQLAKAMEePFGAAALRLFDAVLVGGAALNPQV 193
Cdd:PRK06060 205 SVWFPLAtGGSAVINSAPVTPEAAA-------ILSARFGPSVlygVPNFFARVID-SCSPDSFRSLRCVVSAGEALELGL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 194 AARAEEL--GINVVTTYGSSETAGGCVYDG-------------QPIEGAQVAIE--------NGRVWLGGPMIAHGYRNA 250
Cdd:PRK06060 277 AERLMEFfgGIPILDGIGSTEVGQTFVSNRvdewrlgtlgrvlPPYEIRVVAPDgttagpgvEGDLWVRGPAIAKGYWNR 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 251 PShEAFHKPGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGV 315
Cdd:PRK06060 357 PD-SPVANEGWLDTRDRVCIDsDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAV 421
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
58-330 |
2.49e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 55.72 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 58 PIDE--SIALVVgTSGSTGTPKG-------AQLtvdNLVSSATAthqW-LGGEGQWLLAMPAYHIAGL----QVLIRsll 123
Cdd:PRK08162 178 PADEwdAIALNY-TSGTTGNPKGvvyhhrgAYL---NALSNILA---WgMPKHPVYLWTLPMFHCNGWcfpwTVAAR--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 124 AGTNpVC---VDVTDGFDVAAfadgAEALTsdraYTSLAPM---QLAKAMEEPFGAAALRLfdAVLVGGAALNPQVAARA 197
Cdd:PRK08162 248 AGTN-VClrkVDPKLIFDLIR----EHGVT----HYCGAPIvlsALINAPAEWRAGIDHPV--HAMVAGAAPPAAVIAKM 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 198 EELGINVVTTYGSSETAGGCV-------YDGQPI-----------------EGAQVAIEN------------GRVWLGGP 241
Cdd:PRK08162 317 EEIGFDLTHVYGLTETYGPATvcawqpeWDALPLderaqlkarqgvryplqEGVTVLDPDtmqpvpadgetiGEIMFRGN 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 242 MIAHGYRNAP--SHEAFHKpGWFATSDAGEIH-DGRLVITGRLDTIIDSGG-----------LKLHPEVLErellaidgv 307
Cdd:PRK08162 397 IVMKGYLKNPkaTEEAFAG-GWFHTGDLAVLHpDGYIKIKDRSKDIIISGGenissievedvLYRHPAVLV--------- 466
|
330 340
....*....|....*....|....*.
gi 1080381800 308 tgACVVGVPHPRLG---HAIVAAYEG 330
Cdd:PRK08162 467 --AAVVAKPDPKWGevpCAFVELKDG 490
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
245-373 |
2.73e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 55.59 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 245 HGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRL-DTIIdSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRL 320
Cdd:PRK08315 410 KGYWNDPekTAEAIDADGWMHTGDLAVMdEEGYVNIVGRIkDMII-RGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKY 488
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080381800 321 GHAIVAAYegIAELGDVMdglgDAED-----AGRINHWMIPKDLRRVEVLPLIGPGKV 373
Cdd:PRK08315 489 GEEVCAWI--ILRPGATL----TEEDvrdfcRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
55-222 |
3.21e-08 |
|
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: 55.15 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 55 AGEPIDESIALVVGTSGSTGTPKGAQLTvDNLVSSATATHQWLGGEGQW----LLAMPAYHIAGLQVLIRSLLAGTNPVC 130
Cdd:cd17632 217 RPEPDDDPLALLIYTSGSTGTPKGAMYT-ERLVATFWLKVSSIQDIRPPasitLNFMPMSHIAGRISLYGTLARGGTAYF 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 131 V---DVTDGFDVAAFADGAEALTSDRA-------YTSLAPMQLAKAMEEPFGAAALR--LFDAVL--------VGGAALN 190
Cdd:cd17632 296 AaasDMSTLFDDLALVRPTELFLVPRVcdmlfqrYQAELDRRSVAGADAETLAERVKaeLRERVLggrllaavCGSAPLS 375
|
170 180 190
....*....|....*....|....*....|...
gi 1080381800 191 PQVAARAEE-LGINVVTTYGSSEtAGGCVYDGQ 222
Cdd:cd17632 376 AEMKAFMESlLDLDLHDGYGSTE-AGAVILDGV 407
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
59-375 |
3.27e-08 |
|
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: 55.22 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 59 IDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG---GEGQWLLAMPA------YHIAG-LQVLIRSLL---AG 125
Cdd:cd05973 86 LDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDlrpEDSFWNAADPGwayglyYAITGpLALGHPTILlegGF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 126 TNPVCVDVTDGFDVAAFADGAEALTSDRAYTSLAP------MQLAKAMEEPFGAAALRLFDAVLvgGAALNPQVAarAEE 199
Cdd:cd05973 166 SVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVParpkgrLRRVSSAGEPLTPEVIRWFDAAL--GVPIHDHYG--QTE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 200 LGINVVTTYGSSET--AGGCvydGQPIEGAQVAI-----------ENGRVWL---GGP-MIAHGYRNAPSHEAfhKPGWF 262
Cdd:cd05973 242 LGMVLANHHALEHPvhAGSA---GRAMPGWRVAVldddgdelgpgEPGRLAIdiaNSPlMWFRGYQLPDTPAI--DGGYY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 263 ATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA------AYEGIAELG 335
Cdd:cd05973 317 LTGDTVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAfvvlrgGHEGTPALA 396
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1080381800 336 DVMDGLGDAedagRINHWMIPKDLRRVEVLPLIGPGKVDR 375
Cdd:cd05973 397 DELQLHVKK----RLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
23-377 |
3.73e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 55.09 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 23 PDLRAALDGEVSLLPVPLHDGTRASILRNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ 102
Cdd:PRK12406 114 PEIAAAYRISPALLTPPAGAIDWEGWLAQQEPYDGPPVPQPQSMIYTSGTTGHPKGVRRAAPTPEQAAAAEQMRALIYGL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 103 -----WLLAMPAYHIAGLQVLIRSLLAGTNPVcvdVTDGFDVAAFADGAEALTSDRAYtsLAP------MQLAKAMEEPF 171
Cdd:PRK12406 194 kpgirALLTGPLYHSAPNAYGLRAGRLGGVLV---LQPRFDPEELLQLIERHRITHMH--MVPtmfirlLKLPEEVRAKY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 172 GAAALRLfdavLVGGAALNPQVAARA--EELGINVVTTYGSSETAG-------------GCVydGQPIEGAQVAI--ENG 234
Cdd:PRK12406 269 DVSSLRH----VIHAAAPCPADVKRAmiEWWGPVIYEYYGSTESGAvtfatsedalshpGTV--GKAAPGAELRFvdEDG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 235 RVwLG----GPMIAH-------GYRNAPSHEA-FHKPGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLEREL 301
Cdd:PRK12406 343 RP-LPqgeiGEIYSRiagnpdfTYHNKPEKRAeIDRGGFITSGDVGYLDaDGYLFLCDRKRDMVISGGVNIYPAEIEAVL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 302 LAIDGVTGACVVGVPHPRLGHAIVAAYE----GIAELGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:PRK12406 422 HAVPGVHDCAVFGIPDAEFGEALMAVVEpqpgATLDEADIRAQL-----KARLAGYKVPKHIEIMAELPREDSGKIFKRR 496
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
52-378 |
3.87e-08 |
|
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: 54.79 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 52 SQRAGEPID-----ESIALVVGTSGSTGTPKGAQL---TVDNLVSSATATHQWLGGEGQWLLAMPAYHIAgLQVLIRSLL 123
Cdd:cd17656 114 SQEDTSNIDyinnsDDLLYIIYTSGTTGKPKGVQLehkNMVNLLHFEREKTNINFSDKVLQFATCSFDVC-YQEIFSTLL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 124 AGTNPVCVDVTDGFDVAAFADgaeALTSDRAYTSLAPMQLAKAMEEPFGAAAlRLFDAV---LVGGAAL---NPQVAARA 197
Cdd:cd17656 193 SGGTLYIIREETKRDVEQLFD---LVKRHNIEVVFLPVAFLKFIFSEREFIN-RFPTCVkhiITAGEQLvitNEFKEMLH 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 198 EElGINVVTTYGSSETAGGCVYD-------------GQPIEGAQVAIEN-----------GRVWLGGPMIAHGYRNAPS- 252
Cdd:cd17656 269 EH-NVHLHNHYGPSETHVVTTYTinpeaeipelppiGKPISNTWIYILDqeqqlqpqgivGELYISGASVARGYLNRQEl 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 253 -HEAF----HKPG--WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAI 324
Cdd:cd17656 348 tAEKFfpdpFDPNerMYRTGDlARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYL 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 325 VAAYEGIAELG--DVMDGLGDAedagrINHWMIPKDLRRVEVLPLIGPGKVDRKKV 378
Cdd:cd17656 428 CAYFVMEQELNisQLREYLAKQ-----LPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
60-301 |
4.91e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEG-------QWLlamPAYHIAGL-QVLIRSLLAGTNpvCV 131
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLnpddvivSWL---PLYHDMGLiGGLLQPIFSGVP--CV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 132 DVTDGF-----------------DVAAFADGAEALTSDR-AYTSLAPMQL-----AKAMEEPFGAAALRLF--------- 179
Cdd:PRK05691 240 LMSPAYflerplrwleaiseyggTISGGPDFAYRLCSERvSESALERLDLsrwrvAYSGSEPIRQDSLERFaekfaacgf 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 180 ------------DAVL-VGGAALN---PQVAARAEELGINVVTTyGSSETAGGCVYdGQPIEGA--------QVAIEN-- 233
Cdd:PRK05691 320 dpdsffasyglaEATLfVSGGRRGqgiPALELDAEALARNRAEP-GTGSVLMSCGR-SQPGHAVlivdpqslEVLGDNrv 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080381800 234 GRVWLGGPMIAHGY-RNA-PSHEAF-HKPG--WFATSDAGEIHDGRLVITGRLDTIIDSGGLKLHPEVLEREL 301
Cdd:PRK05691 398 GEIWASGPSIAHGYwRNPeASAKTFvEHDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
61-382 |
5.19e-08 |
|
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: 54.47 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEGQ--WL-LAMPAYHIAgLQVLIRSLLAG-TnpVCVdvtdg 136
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSEsrVLqFASYTFDVS-ILEIFTTLAAGgC--LCI----- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 fdvaafadgaealTSDRAYTSlapmQLAKAMEEpFGA-------AALRLFDAVLV--------GGAALNPQVAARAEElG 201
Cdd:cd05918 178 -------------PSEEDRLN----DLAGFINR-LRVtwafltpSVARLLDPEDVpslrtlvlGGEALTQSDVDTWAD-R 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 202 INVVTTYGSSETAGGCVYD-----------GQPIEGAQ--VAIEN----------GRVWLGGPMIAHGYRNAP--SHEAF 256
Cdd:cd05918 239 VRLINAYGPAECTIAATVSpvvpstdprniGRPLGATCwvVDPDNhdrlvpigavGELLIEGPILARGYLNDPekTAAAF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 257 -HKPGWFATSDAGEI-------------HDGRLVITGRLDTIIdsgglKLH------PEVlERELLAIDGVTGACVVGV- 315
Cdd:cd05918 319 iEDPAWLKQEGSGRGrrlyrtgdlvrynPDGSLEYVGRKDTQV-----KIRgqrvelGEI-EHHLRQSLPGAKEVVVEVv 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 316 ------PHPRLGHAIVAAYEGIAELGDVMDGLGDAEDAGRIN------------HWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd05918 393 kpkdgsSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVaelrsklrqrlpSYMVPSVFLPLSHLPLTASGKIDRRA 472
|
....*
gi 1080381800 378 VAALF 382
Cdd:cd05918 473 LRELA 477
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
27-376 |
6.92e-08 |
|
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: 54.20 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 27 AALDGEVSLLPVPLHDGTRASILRNSQRAgEPIDesIALVVGTSGSTGTPKGAQLTVDNLVSS-ATATHQW-LGGEGQWL 104
Cdd:cd12114 95 AQLDVAVFDVLILDLDALAAPAPPPPVDV-APDD--LAYVIFTSGSTGTPKGVMISHRAALNTiLDINRRFaVGPDDRVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 105 LA------MPAYHIAGLqvlirsLLAGTNPVCVDVTDGFDVAAFADGAE--ALTSDRAYTSLAPMQLAKAMEEPFGAAAL 176
Cdd:cd12114 172 ALsslsfdLSVYDIFGA------LSAGATLVLPDEARRRDPAHWAELIErhGVTLWNSVPALLEMLLDVLEAAQALLPSL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 177 RLfdaVLVGGAALNPQVAARAEEL--GINVVTTYGSSETAGGCVYD--------------GQPIEGAQVAIEN------- 233
Cdd:cd12114 246 RL---VLLSGDWIPLDLPARLRALapDARLISLGGATEASIWSIYHpidevppdwrsipyGRPLANQRYRVLDprgrdcp 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 234 ----GRVWLGGPMIAHGYRNAP--SHEAF--HKPG--WFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELL 302
Cdd:cd12114 323 dwvpGELWIGGRGVALGYLGDPelTAARFvtHPDGerLYRTGDLGRYrPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQ 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080381800 303 AIDGVTGACVVGVPHP---RLGHAIVAAYEGIAELGDVMDGLGdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:cd12114 403 AHPGVARAVVVVLGDPggkRLAAFVVPDNDGTPIAPDALRAFL----AQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
56-380 |
2.58e-07 |
|
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: 52.46 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 56 GEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDV 133
Cdd:cd05910 80 GIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGirPGEVDLATFPLFALFGPALGLTSVIPDMDPTRPAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 134 TDGfdvAAFADGAEALTSDRAYTSLAPMQLAKAMEEPFGAAaLRLFDAVLVGGAALNPQVAARAEEL---GINVVTTYGS 210
Cdd:cd05910 160 ADP---QKLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT-LPSLRRVLSAGAPVPIALAARLRKMlsdEAEILTPYGA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 211 SET----------------------AGGCVydGQPIEGAQVAI--------------------ENGRVWLGGPMIAHGYR 248
Cdd:cd05910 236 TEAlpvssigsrellatttaatsggAGTCV--GRPIPGVRVRIieiddepiaewddtlelprgEIGEITVTGPTVTPTYV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 249 NAPSHEAFHKPG------WFATSDAGEIHD-GRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGV--PHPR 319
Cdd:cd05910 314 NRPVATALAKIDdnsegfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVgkPGCQ 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 320 LGHAIVAAYEGIAE-----LGDVMDGLGDAEDAGRINHWMI----PKDLRRvevlpligPGKVDRKKVAA 380
Cdd:cd05910 394 LPVLCVEPLPGTITprarlEQELRALAKDYPHTQRIGRFLIhpsfPVDIRH--------NAKIFREKLAV 455
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
63-377 |
3.14e-07 |
|
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: 52.02 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 63 IALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLGGEG---QWLLAMPAY---HIagLQVLIRSLLAGTNPVCVDVTDG 136
Cdd:cd17648 96 LAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDngdEAVLFFSNYvfdFF--VEQMTLALLNGQKLVVPPDEMR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 FDVAAFAD--GAEALTsdraYTSLAPMQLakAMEEPFGAAALRLFDAvlVGGAALNPQVAARAEELGINVVTTYGSSETA 214
Cdd:cd17648 174 FDPDRFYAyiNREKVT----YLSGTPSVL--QQYDLARLPHLKRVDA--AGEEFTAPVFEKLRSRFAGLIINAYGPTETT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 215 ---------GGCVYD---GQPIEGAQVAIEN-----------GRVWLGGPMIAHGYRNAP--SHEAFhKPGWFAT-SDAG 268
Cdd:cd17648 246 vtnhkrffpGDQRFDkslGRPVRNTKCYVLNdamkrvpvgavGELYLGGDGVARGYLNRPelTAERF-LPNPFQTeQERA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 269 E---------------IHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHA-----IVAAY 328
Cdd:cd17648 325 RgrnarlyktgdlvrwLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYY 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1080381800 329 ---EGIAELGDVMDGLgdaedAGRINHWMIPKDLRRVEVLPLIGPGKVDRKK 377
Cdd:cd17648 405 lpePGHVPESDLLSFL-----RAKLPRYMVPARLVRLEGIPVTINGKLDVRA 451
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
52-314 |
4.90e-07 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 51.59 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 52 SQRAGEpidesIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG----GEGQWLLA--MPAYHIA------------ 113
Cdd:cd05933 146 SQKPNQ-----CCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDlrpaTVGQESVVsyLPLSHIAaqildiwlpikv 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 114 GLQV-----------LIRSLLAGTNPVCVDVTDGFD--------VAAFADGAEALTSDRAYTSLAPMQLAKAMEE----- 169
Cdd:cd05933 221 GGQVyfaqpdalkgtLVKTLREVRPTAFMGVPRVWEkiqekmkaVGAKSGTLKRKIASWAKGVGLETNLKLMGGEspspl 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 170 PFGAAALRLFDAV------------LVGGAALNPQVAARAEELGINVVTTYGSSETAGG---CVYD-------GQPIEGA 227
Cdd:cd05933 301 FYRLAKKLVFKKVrkalgldrcqkfFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPhtiSNPQayrllscGKALPGC 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 228 QVAIEN------GRVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEI-HDGRLVITGRL-DTIIDSGGLKLHP--- 294
Cdd:cd05933 381 KTKIHNpdadgiGEICFWGRHVFMGYLNMEdkTEEAIDEDGWLHSGDLGKLdEDGFLYITGRIkELIITAGGENVPPvpi 460
|
330 340
....*....|....*....|
gi 1080381800 295 EVLERELLAIdgVTGACVVG 314
Cdd:cd05933 461 EDAVKKELPI--ISNAMLIG 478
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
179-380 |
6.72e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 50.81 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 179 FDAVLVGGAALNPQVAARAEELGINVVTTYGSSEtaGGCVYDGQPIEGAQVaiengrvwLGGP-----MIAHGYRNAPSh 253
Cdd:PRK08308 214 FHAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSE--AGCVSICPDMKSHLD--------LGNPlphvsVSAGSDENAPE- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 254 EAFHKPG--WFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYeg 330
Cdd:PRK08308 283 EIVVKMGdkEIFTKDLGYKsERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKV-- 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080381800 331 IAElgdvmdglgDAEDAGRINHWMI--------PKDLRRVEVLPLIGPGKVDRKKVAA 380
Cdd:PRK08308 361 ISH---------EEIDPVQLREWCIqhlapyqvPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
60-381 |
9.50e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.12 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLTVDNLVSSA--TATHQWLGGEGQWLLAMPAYHIAGLQV-LIRSLLAG----------- 125
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRaqVAARIDFSPEDKVFNALPVFHSFGLTGgLVLPLLSGvkvflypsplh 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 126 ----------TNPVCVDVTDGFdVAAFADGAEaltsdraytslapmqlakameePFGAAALRLfdaVLVGGAALNPqvAA 195
Cdd:PRK06814 872 yriipeliydTNATILFGTDTF-LNGYARYAH----------------------PYDFRSLRY---VFAGAEKVKE--ET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 196 R---AEELGINVVTTYGSSETA--------------------GGCVYDGQPIEGAQvaiENGRVWLGGPMIAHGYRNAPS 252
Cdd:PRK06814 924 RqtwMEKFGIRILEGYGVTETApvialntpmhnkagtvgrllPGIEYRLEPVPGID---EGGRLFVRGPNVMLGYLRAEN 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 253 HEAFHKP--GWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAaye 329
Cdd:PRK06814 1001 PGVLEPPadGWYDTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIIL--- 1077
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080381800 330 giaelgdvmdgLGDAEDAGR---INHW--------MIPKDLRRVEVLPLIGPGKVDRKKVAAL 381
Cdd:PRK06814 1078 -----------LTTASDATRaafLAHAkaagaselMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
260-382 |
1.87e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 49.70 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 260 GWFATSDAGEI-HDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGH---AIVAAYEGIAELG 335
Cdd:PRK07008 409 GWFPTGDVATIdADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDErplLVVVKRPGAEVTR 488
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1080381800 336 DVMDGLGDaedaGRINHWMIPKDLRRVEVLPLIGPGKVDRKKVAALF 382
Cdd:PRK07008 489 EELLAFYE----GKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
61-376 |
2.00e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQwlggegqwllampayhiaglqvliRSLLAGTNPVCVDVTDGFDVA 140
Cdd:PRK12316 2146 ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGE------------------------RYELSPADCELQFMSFSFDGA 2201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 141 A------FADGAEALTSDRAYTSlaPMQLAKAMEE------PFGAAALRLFDAVL-------------VGGAALnPQVAA 195
Cdd:PRK12316 2202 HeqwfhpLLNGARVLIRDDELWD--PEQLYDEMERhgvtilDFPPVYLQQLAEHAerdgrppavrvycFGGEAV-PAASL 2278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 196 RAEELGIN---VVTTYGSSET-------------AGGCVYD--GQPIEGAQVAIEN-----------GRVWLGGPMIAHG 246
Cdd:PRK12316 2279 RLAWEALRpvyLFNGYGPTEAvvtpllwkcrpqdPCGAAYVpiGRALGNRRAYILDadlnllapgmaGELYLGGEGLARG 2358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 247 YRNAPSHEA-------FHKPG--WFATSD-AGEIHDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVV--- 313
Cdd:PRK12316 2359 YLNRPGLTAerfvpdpFSASGerLYRTGDlARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVaqd 2438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080381800 314 GVPHPRLghaivAAYEGIAELGDVMDGLGDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVDRK 376
Cdd:PRK12316 2439 GASGKQL-----VAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRK 2496
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
20-373 |
2.34e-06 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 49.37 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 20 AILPDLRAALDGEVSLLPVPLHDGTRASILRNSQRAGE--PIDESI----------ALVVGTSGSTGTPKGAQLTvdnlv 87
Cdd:PRK06155 127 ALLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPlpPLDAPApaaavqpgdtAAILYTSGTTGPSKGVCCP----- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 88 ssaTATHQWLG---------GEGQWLLA-MPAYHIAGLQVLIRSLLAGTNPVcvdVTDGFDVAAFADGAEALTSDRAYT- 156
Cdd:PRK06155 202 ---HAQFYWWGrnsaedleiGADDVLYTtLPLFHTNALNAFFQALLAGATYV---LEPRFSASGFWPAVRRHGATVTYLl 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 157 -SLAPMQLAKAMEEPFGAAALRlfdavlvggAALNPQVAARA-----EELGINVVTTYGSSETAGGCV---------YDG 221
Cdd:PRK06155 276 gAMVSILLSQPARESDRAHRVR---------VALGPGVPAALhaafrERFGVDLLDGYGSTETNFVIAvthgsqrpgSMG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 222 QPIEG--AQVAIENGR-VWLGGP-----------MIAHGYRNAPSH--EAFhKPGWFATSDAGEI-HDGRLVITGRLDTI 284
Cdd:PRK06155 347 RLAPGfeARVVDEHDQeLPDGEPgelllradepfAFATGYFGMPEKtvEAW-RNLWFHTGDRVVRdADGWFRFVDRIKDA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 285 IDSGGLKLHPEVLERELLAIDGVTGACVVGVPhPRLGHAIVAAYEGIAElGDVMDGLGDAEDA-GRINHWMIPKDLRRVE 363
Cdd:PRK06155 426 IRRRGENISSFEVEQVLLSHPAVAAAAVFPVP-SELGEDEVMAAVVLRD-GTALEPVALVRHCePRLAYFAVPRYVEFVA 503
|
410
....*....|
gi 1080381800 364 VLPLIGPGKV 373
Cdd:PRK06155 504 ALPKTENGKV 513
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
301-372 |
6.05e-06 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 43.69 E-value: 6.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 301 LLAIDGVTGACVVGVPHPRLGHAIVAAY---EGIAEL-GDVMDGLGDaedagRINHWMIPKDLRRVEVLPLIGPGK 372
Cdd:pfam13193 6 LVSHPAVAEAAVVGVPDELKGEAPVAFVvlkPGVELLeEELVAHVRE-----ELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
58-318 |
7.02e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 47.97 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 58 PIDEsIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG-GEGQWLLAM-PAYHIAGLQVLIRSLLAGTNPVCVdvtd 135
Cdd:PRK09274 172 APDD-MAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGiEPGEIDLPTfPLFALFGPALGMTSVIPDMDPTRP---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 136 gfdvaAFADgaealtsdraytslaPMQLAKAMEE-----PFGAAAL--RLFDA-------------VLVGGAALNPQVAA 195
Cdd:PRK09274 247 -----ATVD---------------PAKLFAAIERygvtnLFGSPALleRLGRYgeangiklpslrrVISAGAPVPIAVIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 196 RAEEL---GINVVTTYGSSET----------------------AGGCVydGQPIEGAQVAI------------------- 231
Cdd:PRK09274 307 RFRAMlppDAEILTPYGATEAlpissiesreilfatraatdngAGICV--GRPVDGVEVRIiaisdapipewddalrlat 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 232 -ENGRVWLGGPMIAHGYRNAPSHEAFHK------PGWFATSDAGEIHD-GRLVITGRLDTIIDSGGLKLHPEVLERELLA 303
Cdd:PRK09274 385 gEIGEIVVAGPMVTRSYYNRPEATRLAKipdgqgDVWHRMGDLGYLDAqGRLWFCGRKAHRVETAGGTLYTIPCERIFNT 464
|
330
....*....|....*
gi 1080381800 304 IDGVTGACVVGVPHP 318
Cdd:PRK09274 465 HPGVKRSALVGVGVP 479
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
75-288 |
7.39e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 47.69 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 75 TPKGAQLTVDNLVSSATAT--HQWL-------------------------GGEGQWLLAMPAYHIAGLqvlirsllaGTN 127
Cdd:PRK09192 239 TPVATQLSVDYLPTRDFARrpLQWLdlisrnrgtisysppfgyelcarrvNSKDLAELDLSCWRVAGI---------GAD 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 128 PVCVDVTDGFdVAAFAdgaEALTSDRAYTS---LAPMQLAKAMEEP-FGAAALRLFDAVLVG-GAALNPQVAARAEELGI 202
Cdd:PRK09192 310 MIRPDVLHQF-AEAFA---PAGFDDKAFMPsygLAEATLAVSFSPLgSGIVVEEVDRDRLEYqGKAVAPGAETRRVRTFV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 203 NvvttygssetaggCvydGQPIEGAQVAIEN-----------GRVWLGGPMIAHGY-RNAPSHEAFHKPGWFATSDAGEI 270
Cdd:PRK09192 386 N-------------C---GKALPGHEIEIRNeagmplpervvGHICVRGPSLMSGYfRDEESQDVLAADGWLDTGDLGYL 449
|
250
....*....|....*....
gi 1080381800 271 HDGRLVITGRL-DTIIDSG 288
Cdd:PRK09192 450 LDGYLYITGRAkDLIIING 468
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
61-379 |
9.29e-06 |
|
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: 47.47 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGA-QLTVDNLVSSATATHQWLGG-EGQWLLAMP--AYHIAGLQVLIRSLLAGTNPVCVDVTDG 136
Cdd:cd05958 97 DDICILAFTSGTTGAPKATmHFHRDPLASADRYAVNVLRLrEDDRFVGSPplAFTFGLGGVLLFPFGVGASGVLLEEATP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 FDVAAFADGAEALTSDRAYTSLAPMQLAKAMEEPFGAAALRLFDAvlvgGAALNPQVAARAEE-LGINVVTTYGSSE--- 212
Cdd:cd05958 177 DLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSA----GEALPAALHRAWKEaTGIPIIDGIGSTEmfh 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 213 ----TAGGCVY---DGQPIEGAQVAI-----------ENGRVWLGGPMIAHgYRNAPSHEAFHKPGWFATSDAGEIH-DG 273
Cdd:cd05958 253 ifisARPGDARpgaTGKPVPGYEAKVvddegnpvpdgTIGRLAVRGPTGCR-YLADKRQRTYVQGGWNITGDTYSRDpDG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 274 RLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGhAIVAAY----EGIAELGDVMDGLGDAEDAgR 349
Cdd:cd05958 332 YFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRG-VVVKAFvvlrPGVIPGPVLARELQDHAKA-H 409
|
330 340 350
....*....|....*....|....*....|
gi 1080381800 350 INHWMIPKDLRRVEVLPLIGPGKVDRKKVA 379
Cdd:cd05958 410 IAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-373 |
2.43e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 46.08 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 19 TAILPDLRAALDGEVS-------LLPVPLHDGTRASILRNSQRAGEPI------DESIALVVGTSGSTGTPKGAQLTVDN 85
Cdd:PRK08316 116 PALAPTAEAALALLPVdtlilslVLGGREAPGGWLDFADWAEAGSVAEpdvelaDDDLAQILYTSGTESLPKGAMLTHRA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 86 L----VSSATATHqwLGGEGQWLLAMPAYHIAGLQV-LIRSLLAG-TN--------PVCVDVTDGFDVAAF--------- 142
Cdd:PRK08316 196 LiaeyVSCIVAGD--MSADDIPLHALPLYHCAQLDVfLGPYLYVGaTNvildapdpELILRTIEAERITSFfapptvwis 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 143 ----ADGAEA-LTSDR-AY--TSLAPMQLAKAMEEPFgaAALRLFD-------AVLvgGAALNPQVAAR----AEELGIN 203
Cdd:PRK08316 274 llrhPDFDTRdLSSLRkGYygASIMPVEVLKELRERL--PGLRFYNcygqteiAPL--ATVLGPEEHLRrpgsAGRPVLN 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 204 VvttygssETAggcVYDgqpIEGAQVAI-ENGRVWLGGPMIAHGYRNAP--SHEAFhKPGWFATSDAGEI-HDGRLVITG 279
Cdd:PRK08316 350 V-------ETR---VVD---DDGNDVAPgEVGEIVHRSPQLMLGYWDDPekTAEAF-RGGWFHSGDLGVMdEEGYITVVD 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 280 RLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVAAYEgiaelgdVMDGLGDAEDA------GRINHW 353
Cdd:PRK08316 416 RKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVV-------PKAGATVTEDEliahcrARLAGF 488
|
410 420
....*....|....*....|
gi 1080381800 354 MIPKDLRRVEVLPLIGPGKV 373
Cdd:PRK08316 489 KVPKRVIFVDELPRNPSGKI 508
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
220-326 |
4.07e-05 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 45.63 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 220 DGQPIEGAQ---VAIEngRVWlggPMIAHG-YRNapsHEAFHK------PGWFATSD-AGEIHDGRLVITGRLDTIIDSG 288
Cdd:cd05966 427 EGNEVEGEVegyLVIK--RPW---PGMARTiYGD---HERYEDtyfskfPGYYFTGDgARRDEDGYYWITGRVDDVINVS 498
|
90 100 110
....*....|....*....|....*....|....*...
gi 1080381800 289 GLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA 326
Cdd:cd05966 499 GHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYA 536
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
50-95 |
6.00e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 45.09 E-value: 6.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1080381800 50 RNSQRAGEPIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQ 95
Cdd:PLN02736 210 SSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSL 255
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
61-283 |
6.38e-05 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 44.73 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSAT---ATHQWLGGEGQWLLA-MPAYHIAGLQVLIRSLLAGTNPVCVDvtDG 136
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAmleQTYPFFGEEPPVLVDwLPWNHTFGGNHNFNLVLYNGGTLYID--DG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 137 FDVAA-FADGAEALT--SDRAYTSlAPM---QLAKAMEEPFGAAAlRLFDAVLV---GGAALNPQVAARAEELG------ 201
Cdd:cd05921 243 KPMPGgFEETLRNLReiSPTVYFN-VPAgweMLVAALEKDEALRR-RFFKRLKLmfyAGAGLSQDVWDRLQALAvatvge 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 202 -INVVTTYGSSETAGGCV----------YDGQPIEGAQVAI--ENGR--VWLGGPMIAHGYRNAP--SHEAFHKPGWFAT 264
Cdd:cd05921 321 rIPMMAGLGATETAPTATfthwptersgLIGLPAPGTELKLvpSGGKyeVRVKGPNVTPGYWRQPelTAQAFDEEGFYCL 400
|
250 260 270
....*....|....*....|....*....|
gi 1080381800 265 SDA-----------GEIHDGRLVITGRLDT 283
Cdd:cd05921 401 GDAakladpddpakGLVFDGRVAEDFKLAS 430
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
69-281 |
7.19e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 44.65 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 69 TSGSTGTPKGAQLTVDNLVSSATATHQWL-----GGEGQWLLAMPAYHIAGLQVLIRSLLAGTNPVCVDvtDGFDVAA-F 142
Cdd:PRK12582 228 TSGSTGMPKAVINTQRMMCANIAMQEQLRprepdPPPPVSLDWMPWNHTMGGNANFNGLLWGGGTLYID--DGKPLPGmF 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 143 ADGAEALT--SDRAYTSlAPM---QLAKAME--EPFGAAALRLFDAVLVGGAALNPQVAARAEELG-------INVVTTY 208
Cdd:PRK12582 306 EETIRNLReiSPTVYGN-VPAgyaMLAEAMEkdDALRRSFFKNLRLMAYGGATLSDDLYERMQALAvrttghrIPFYTGY 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 209 GSSETAGGCVYD----------GQPIEGAQVA-IENG---RVWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEIHD 272
Cdd:PRK12582 385 GATETAPTTTGThwdtervgliGLPLPGVELKlAPVGdkyEVRVKGPNVTPGYHKDPelTAAAFDEEGFYRLGDAARFVD 464
|
250
....*....|....
gi 1080381800 273 GR-----LVITGRL 281
Cdd:PRK12582 465 PDdpekgLIFDGRV 478
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
260-382 |
1.54e-04 |
|
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: 43.63 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 260 GWFATSDAgeihDGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLGHAIVA---AYEGIAELGD 336
Cdd:cd05968 476 GDFAYYDE----EGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCfvvLKPGVTPTEA 551
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1080381800 337 VMDGL--GDAEDAGRInhwMIPKDLRRVEVLPLIGPGKVDRKKVAALF 382
Cdd:cd05968 552 LAEELmeRVADELGKP---LSPERILFVKDLPKTRNAKVMRRVIRAAY 596
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
61-286 |
2.11e-04 |
|
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: 43.36 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATAT------HQWLGGEGQWLLAMPAYHIAGLQVLIRSLLAGtnpVCVDVT 134
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkileiLNKINPTDVYISYLPLAHIFERVVEALFLYHG---AKIGFY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 135 DGfDVAAFADGAEAL--TS--------DRAYTSLAPMQLAK----------------AMEEPFGAAALRLFDAV------ 182
Cdd:cd05927 191 SG-DIRLLLDDIKALkpTVfpgvprvlNRIYDKIFNKVQAKgplkrklfnfalnyklAELRSGVVRASPFWDKLvfnkik 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 183 ----------LVGGAALNPQVA--ARAeELGINVVTTYGSSETAGGCV----YD------GQPIEGAQV----------- 229
Cdd:cd05927 270 qalggnvrlmLTGSAPLSPEVLefLRV-ALGCPVLEGYGQTECTAGATltlpGDtsvghvGGPLPCAEVklvdvpemnyd 348
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080381800 230 -AIENGR--VWLGGPMIAHGYRNAP--SHEAFHKPGWFATSDAGEIH-DGRLvitgrldTIID 286
Cdd:cd05927 349 aKDPNPRgeVCIRGPNVFSGYYKDPekTAEALDEDGWLHTGDIGEWLpNGTL-------KIID 404
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
61-272 |
2.37e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 42.94 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 61 ESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQ---WLGGEGQ----WLlamPAYHIAGLQVLIRSLLA--GTnpVCV 131
Cdd:PRK08180 209 DTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQtfpFLAEEPPvlvdWL---PWNHTFGGNHNLGIVLYngGT--LYI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 132 DvtDGFDVAA-FADGAEAL--TSDRAYTSL--APMQLAKAMEEPfgaAALR--LFDAVLV---GGAALNPQVAARAEELG 201
Cdd:PRK08180 284 D--DGKPTPGgFDETLRNLreISPTVYFNVpkGWEMLVPALERD---AALRrrFFSRLKLlfyAGAALSQDVWDRLDRVA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 202 INVV-------TTYGSSETAGGCV----------YDGQPIEGAQVAI--ENGR--VWLGGPMIAHGYRNAP--SHEAFHK 258
Cdd:PRK08180 359 EATCgerirmmTGLGMTETAPSATfttgplsragNIGLPAPGCEVKLvpVGGKleVRVKGPNVTPGYWRAPelTAEAFDE 438
|
250
....*....|....
gi 1080381800 259 PGWFATSDAGEIHD 272
Cdd:PRK08180 439 EGYYRSGDAVRFVD 452
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
58-332 |
1.03e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 41.22 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 58 PI-DESI-ALVVGTSGSTGTPKG--AQLTVDNLVSSATATH----QWLGGEGQ-WLLAMPAYHIAGLQ-VLIRSLLAGTn 127
Cdd:PRK13391 149 PIaDESLgTDMLYSSGTTGRPKGikRPLPEQPPDTPLPLTAflqrLWGFRSDMvYLSPAPLYHSAPQRaVMLVIRLGGT- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 128 pvcVDVTDGFDvaafADGAEALTSDRA--YTSLAP------MQLAKAMEEPFGAAALRlfdaVLVGGAALNPQVAARA-- 197
Cdd:PRK13391 228 ---VIVMEHFD----AEQYLALIEEYGvtHTQLVPtmfsrmLKLPEEVRDKYDLSSLE----VAIHAAAPCPPQVKEQmi 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 198 EELGINVVTTYGSSETAGGCVYDgqpiegAQVAIEN----GRVWLGGPMI--AHG--------------------YRNAP 251
Cdd:PRK13391 297 DWWGPIIHEYYAATEGLGFTACD------SEEWLAHpgtvGRAMFGDLHIldDDGaelppgepgtiwfeggrpfeYLNDP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 252 --SHEAFH-KPGWFATSDAGEIH-DGRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHPRLG---HAI 324
Cdd:PRK13391 371 akTAEARHpDGTWSTVGDIGYVDeDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGeevKAV 450
|
....*...
gi 1080381800 325 VAAYEGIA 332
Cdd:PRK13391 451 VQPVDGVD 458
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
60-125 |
1.13e-03 |
|
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: 40.88 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080381800 60 DESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQWLG--GEGQWLLAMPAYH-IAGLQVLIRSLLAG 125
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNlkNGDRTYTCMPLYHgTAAFLGACNCLMSG 154
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
234-299 |
1.56e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 40.48 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 234 GRVWLGGPMIAHGYRNAP--SHEAFH-----------------KPGWFATSDAGEIHDGRLVITGRLD--TIIDsgGLKL 292
Cdd:PRK07769 419 GEIWLHGNNIGTGYWGKPeeTAATFQnilksrlseshaegapdDALWVRTGDYGVYFDGELYITGRVKdlVIID--GRNH 496
|
....*..
gi 1080381800 293 HPEVLER 299
Cdd:PRK07769 497 YPQDLEY 503
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
58-112 |
2.36e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 40.10 E-value: 2.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080381800 58 PIDESIALVVGTSGSTGTPKGAQLTVDNLVSSATATHQW---LGGEGQWLLAMPAYHI 112
Cdd:PLN02387 247 PSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVvpkLGKNDVYLAYLPLAHI 304
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
50-374 |
6.74e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 38.54 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 50 RNSQRAGEPIDEsiALVVGTSGSTGTPKG-----AQL--TVDNLVSSATATHQwlggeGQWLLAMPAYHIAGLQV-LIRS 121
Cdd:PRK08043 356 RLAQVKQQPEDA--ALILFTSGSEGHPKGvvhshKSLlaNVEQIKTIADFTPN-----DRFMSALPLFHSFGLTVgLFTP 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 122 LLAGT------NPVCVDVTdgfdvaafadgaEALTSDRAYTSLAPM-----QLAKaMEEPFGAAALRLfdaVLVGGAALN 190
Cdd:PRK08043 429 LLTGAevflypSPLHYRIV------------PELVYDRNCTVLFGTstflgNYAR-FANPYDFARLRY---VVAGAEKLQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 191 PQVAAR-AEELGINVVTTYGSSETAG---------------GCVYDGqpIEGAQVAI----ENGRVWLGGPMIAHGYR-- 248
Cdd:PRK08043 493 ESTKQLwQDKFGLRILEGYGVTECAPvvsinvpmaakpgtvGRILPG--MDARLLSVpgieQGGRLQLKGPNIMNGYLrv 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 249 ------NAPSHEAFH---KPGWFATSDAGEIHD-GRLVITGRLDTIIDSGGLKLHPEVLERELLAIDGVTGACVVGVPHP 318
Cdd:PRK08043 571 ekpgvlEVPTAENARgemERGWYDTGDIVRFDEqGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDA 650
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080381800 319 RLGHAIVAaYEGIAELGdvMDGLGDAEDAGRINHWMIPKDLRRVEVLPLIGPGKVD 374
Cdd:PRK08043 651 SKGEALVL-FTTDSELT--REKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
234-380 |
7.22e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 38.61 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 234 GRVWLGGPMIAHGYRNAP--SHEAFhKPGWFAtSDAGEIH----------DGRLVITGRLDTIIDSGGLKLHPEVLEREL 301
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPglTAERF-VADPFA-ADGGRLYrtgdlvrlraDGLVEYVGRIDHQVKIRGFRIELGEIESRL 2610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381800 302 LAIDGVTGACVVGVPHPrlGHAIVAAY--EGIAELGD-VMDGLGDAEDAGRINH---WMIPKDLRRVEVLPLIGPGKVDR 375
Cdd:PRK05691 2611 LEHPAVREAVVLALDTP--SGKQLAGYlvSAVAGQDDeAQAALREALKAHLKQQlpdYMVPAHLILLDSLPLTANGKLDR 2688
|
....*
gi 1080381800 376 KKVAA 380
Cdd:PRK05691 2689 RALPA 2693
|
|
| |
